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.