wanglab/gogpt-training-data huggingface dataset:
Protein: Feruloyl esterase B (EC 3.1.1.73) (Cinnamoyl esterase) (CinnAE) (FAE-I) (Ferulic acid esterase B) (FAEB) (Q8WZI8)
Organism: Aspergillus niger
Function: Involved in degradation of plant cell walls. Hydrolyzes of the feruloyl-arabinose ester bond in arabinoxylans as well as the feruloyl-galactose and feruloyl-arabinose ester bonds in pectin.
Subcellular location: Secreted {ECO:0000269|PubMed:11931668}.
Interaction partners:
Sequence:
MKVASLLSLALPGAALAATDPFQSRCNEFQNKIDIANVTVRSVAYVAAGQNISQAEVASVCKASVQASVDLCRVTMNISTSDRSHLWAEAWLPRNYTGRFVSTGNGGLAGCVQETDLNFAANFGFATVGTNGGHDGDTAKYFLNNSEVLADFAYRSVHEGTVVGKQLTQLFYDEGYNYSYYLGCSTGGRQGYQQVQRFPDDYDGVIAGSAAMNFINLISWGAFLWKATGLADDPDFISANLWSVIHQEIVRQCDLVDGALDGIIEDPDFCAPVIERLICDGTTNGTSCITGAQAAKVNRALSDFYGPDGTVYYPRLNYGGEADSASLYFTGSMYSRTEEWYKYVVYNDTNWNSSQWTLESAKLALEQNPFNIQAFDPNITAFRDRGGKLLSYHGTQDPIISSTDSKLYYRRVANALNAAPSELDEFYRFFQISGMGHCGDGTGASYIGQGYGTYTSKAPQVNLLRTMVDWVENGKAPEYMPGNKLNANGSIEYMRKHCRYPKHNIHTGPGNYTDPNSWTCV
Protein: Serine protease grass (EC 3.4.21.-) (Gram-positive specific serine protease) (Q9VB68)
Organism: Drosophila melanogaster (Fruit fly)
Function: Endopeptidase (By similarity). Plays a key role in innate immunity by activating the Toll pathway in response to fungal and Gram-positive bacterial infections, presumably downstream of pattern-recognition receptors (PRR), such as PGRP-SA, GNBP1 and GNBP3, and upstream of spz processing enzyme SPE.
Subcellular location: Secreted {ECO:0000305|PubMed:21310954}. Note=Probably secreted in the hemolymph. {ECO:0000305}.
Interaction partners:
- Sphinx1
- GH03360p
- trypsin
- Modular serine protease
- Sphinx2, isoform B
Sequence:
MMIASSLAVLYGIAIVSSMGVQSARADYADDCTTPDGDQGQCMPFSSCRTIEERLTEAQKAGQKVPADYASYLQKALCGEFNGVRHFCCPSANIQHNSKVMSLFKDENFDCGNFLSQRVSNGYEVKLSSRPWMALLRYQQFGESRFLCGGAMISERYILTAAHCVHGLQNDLYEIRLGEHRISTEEDCRQQGRKKKCAPPVVNVGIEKHLIHEKYDARHIMHDIALLKLNRSVPFQKHIKPICLPITDELKEKAEQISTYFVTGWGTTENGSSSDVLLQANVPLQPRSACSQAYRRAVPLSQLCVGGGDLQDSCKGDSGGPLQAPAQYLGEYAPKMVEFGIVSQGVVTCGQISLPGLYTNVGEYVQWITDTMASNGL
Protein: MYB-like DNA-binding domain protein (O49020)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MFTREVSYLKLQEVKKRWRLRKGPWTEEEDSMLRAYVNIHGEGRWNAVARLSGLRRTGKSCRLRWLNYMRPEIKRGNISLEEQLLILELHSRWGNRWSKIAQHLPGRTDNEIKNYWRTRVQKQAKQLNCDVNSKQFKDAMRYVWIPRLVERIRASSESPSSQPSTTTNTTYNDRISNISSSQMSYANASGSVQVDPSLLPELSGTSSDSLDTQVSSVSDLTDCYNPQSLSNYLHKGLGLEKEGAATWGRDEEFQATEEHSNGWLVGGGESSMDTVWNEENVWFLQQQLHDDGI
Protein: Ca(2+)-sensitive chloride channel 2 (Q9R070)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MVPGLQVLLFLTLHLLQNTESSMVHLNSNGYEGVVIAINPSVPEDERLIPSIKEMVTQASTYLFEASQGRVYFRNISILVPMTWKSKSEYLMPKRESYDKADVIVADPHLQHGDDPYTLQYGQCGDRGQYIHFTPNFLLTDNLRIYGPRGRVFVHEWAHLRWGVFDEYNVDRPFYISRKNTIEATRCSASITGKKVVHECQRGSCVTRACRRDSKTRLYEPKCTFIPDKIQTAGASIMFMQNLNSVVEFCTENNHNAEAPNLQNKMCNRRSTWDVIKASADFQNSPPMRGTEAPPPPTFSLLKSRRRVVCLVLDKSGSMDKEDRLIRMNQAAELYLTQIVEKESMVGLVTFDSAAHIQNYLIKITSSSDYQKITANLPQQATGGTSICHGLQAGFQAITSSDQSTSGSEIVLLTDGEDNGISSCFEAVSRSGAIIHTIALGPSAARELETLSDMTGGLRFYANKHVSSLIDAFSRISSTSGSVSQQALQLESKAFNVRAGAWINSTVLVDSTVGNDTFFVITWTVQKPEIILQDPKGKKYITSDFQDDELNIRSARLQIPGTAETGTWTYSITGTKSQLITMTVTTRARSPTMEPLLATAHMSQSTAQYPSRMIVYVRVSQGFLPVLGADVTAIIEAEHGHQVTLELWDNGAGADTVKNDGIYTRYFTDYHGNGRYSLKVRVQARKNKARLSLRQKNKSLYIPGYVENGKIVLNPPRPDVQEEAIEATVEDFNRVTSGGSLTVSGAPPDGDHARVFPPSKVTDLEAEFIGDYIQLTWTAPGKVLDKGRAHRYIIRVSQHPLGLQEDFNNVTLVNASSLIPKEAGSKETFKFKPETFKIANDTQLYIAIQAYNEAGLTSEVSNIAQAVKFTSLEDSISALGADISAISMTVWGLAVIFNSILN
Protein: Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 4 (EC 2.4.1.102) (Core 2-branching enzyme 3) (Core2-GlcNAc-transferase 3) (C2GnT3) (Q9P109)
Organism: Homo sapiens (Human)
Function: Glycosyltransferase that mediates core 2 O-glycan branching, an important step in mucin-type biosynthesis. Does not have core 4 O-glycan or I-branching enzyme activity.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
- C1GALT1-specific chaperone 1
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- C1GALT1-specific chaperone 1-like protein
- Alpha-1,4-N-acetylglucosaminyltransferase
- Mucin-6
Sequence:
MKIFKCYFKHTLQQKVFILFLTLWLLSLLKLLNVRRLFPQKDIYLVEYSLSTSPFVRNRYTHVKDEVRYEVNCSGIYEQEPLEIGKSLEIRRRDIIDLEDDDVVAMTSDCDIYQTLRGYAQKLVSKEEKSFPIAYSLVVHKDAIMVERLIHAIYNQHNIYCIHYDRKAPDTFKVAMNNLAKCFSNIFIASKLEAVEYAHISRLQADLNCLSDLLKSSIQWKYVINLCGQDFPLKSNFELVSELKKLNGANMLETVKPPNSKLERFTYHHELRRVPYEYVKLPIRTNISKEAPPHNIQIFVGSAYFVLSQAFVKYIFNNSIVQDFFAWSKDTYSPDEHFWATLIRVPGIPGEISRSAQDVSDLQSKTRLVKWNYYEGFFYPSCTGSHLRSVCIYGAAELRWLIKDGHWFANKFDSKVDPILIKCLAEKLEEQQRDWITLPSEKLFMDRNLTTTS
Protein: Tissue inhibitor of metalloproteinase (Q9VH14)
Organism: Drosophila melanogaster (Fruit fly)
Function: Metalloproteinase inhibitor that acts on both matrix metalloproteinases Mmp1 and Mmp2 in vitro. Complexes with metalloproteinases and irreversibly inactivates them by binding to their catalytic zinc cofactor (By similarity). Required for wing maturation which is the final step in morphogenesis of the adult fly. Involved in the negative regulation of developmental tissue invasion for imaginal disk eversion during metamorphosis by inhibiting Mmp-mediated basement membrane (BM) degradation. Required for oogenesis and for the long-term maintainance of germarial structure and shape in the adult ovaries. Required for maintaining composition and biophysical properties of the extracellular matrix (ECM), and for the normal organization and cyst production of the germline stem cell (GSC) niche.
Subcellular location: Secreted {ECO:0000269|PubMed:14567681}.
Interaction partners:
- Matrix metalloproteinase-2
- Matrix metalloproteinase 1, isoform C
- Protein timeless
- ADAM 17-like protease
- FI21605p1
- ADAM10 endopeptidase
- ADAM10 endopeptidase
Sequence:
MDLRKHLGLLTLLLVAVFAFYGRPADACSCMPSHPQTHFAQADYVVQLRVLRKSDTIEPGRTTYKVHIKRTYKATSEARRMLRDGRLSTPQDDAMCGINLDLGKVYIVAGRMPTLNICSYYKEYTRMTITERHGFSGGYAKATNCTVTPCFGERCFKGRNYADTCKWSPFGKCETNYSACMPHKVQTVNGVISRCRWRRTQLYRKCMSNP
Protein: Thioredoxin-T (ThioredoxinT) (Q8IFW4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probably participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Its tissue specificity suggests a regulatory role in the germline.
Subcellular location: Nucleus {ECO:0000269|PubMed:14579129}. Chromosome {ECO:0000269|PubMed:14579129}. Note=Specifically associated with the Y chromosome loops.
Interaction partners:
- Regulatory protein zeste
- Dorsal interacting protein 4
- Homeobox protein goosecoid
- IP01435p
- Boundary element associated factor
- LD32860p
- DISCO interacting protein 1, isoform D
- 10 kDa heat shock protein, mitochondrial
- Thioredoxin reductase 2, mitochondrial
- GEO12122p1
Sequence:
MVYPVRNKDDLDQQLILAEDKLVVIDFYADWCGPCKIIAPKLDELAHEYSDRVVVLKVNVDENEDITVEYNVNSMPTFVFIKGGNVLELFVGCNSDKLAKLMEKHAGVYTDEAADVKAVHIDGECIVDLTAESSESDNDNNNVNEVSAHDENAVLEH
Protein: Tail spike protein (TSP) (Endo-1,3-alpha-L-rhamnosidase) (EC 3.2.1.-) (Endorhamnosidase) (Gene product 9) (gp9) (P12528)
Organism: Salmonella phage P22 (Bacteriophage P22)
Function: Structural component of the short non-contractile tail. The tail comprises six spikes that mediate primary attachment to the host cell lipopolysaccharides (LPS) and display endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide. Digestion of the LPS brings the capsid near the cell outer membrane.
Subcellular location: Virion {ECO:0000305}.
Interaction partners:
Sequence:
MTDITANVVVSNPRPIFTESRSFKAVANGKIYIGQIDTDPVNPANQIPVYIENEDGSHVQITQPLIINAAGKIVYNGQLVKIVTVQGHSMAIYDANGSQVDYIANVLKYDPDQYSIEADKKFKYSVKLSDYPTLQDAASAAVDGLLIDRDYNFYGGETVDFGGKVLTIECKAKFIGDGNLIFTKLGKGSRIAGVFMESTTTPWVIKPWTDDNQWLTDAAAVVATLKQSKTDGYQPTVSDYVKFPGIETLLPPNAKGQNITSTLEIRECIGVEVHRASGLMAGFLFRGCHFCKMVDANNPSGGKDGIITFENLSGDWGKGNYVIGGRTSYGSVSSAQFLRNNGGFERDGGVIGFTSYRAGESGVKTWQGTVGSTTSRNYNLQFRDSVVIYPVWDGFDLGADTDMNPELDRPGDYPITQYPLHQLPLNHLIDNLLVRGALGVGFGMDGKGMYVSNITVEDCAGSGAYLLTHESVFTNIAIIDTNTKDFQANQIYISGACRVNGLRLIGIRSTDGQGLTIDAPNSTVSGITGMVDPSRINVANLAEEGLGNIRANSFGYDSAAIKLRIHKLSKTLDSGALYSHINGGAGSGSAYTQLTAISGSTPDAVSLKVNHKDCRGAEIPFVPDIASDDFIKDSSCFLPYWENNSTSLKALVKKPNGELVRLTLATL
Protein: Growth/differentiation factor 15 (GDF-15) (Macrophage inhibitory cytokine 1) (MIC-1) (Q9Z0J7)
Organism: Mus musculus (Mouse)
Function: Regulates food intake, energy expenditure and body weight in response to metabolic and toxin-induced stresses. Binds to its receptor, GFRAL, and activates GFRAL-expressing neurons localized in the area postrema and nucleus tractus solitarius of the brainstem. It then triggers the activation of neurons localized within the parabrachial nucleus and central amygdala, which constitutes part of the 'emergency circuit' that shapes feeding responses to stressful conditions. On hepatocytes, inhibits growth hormone signaling.
Subcellular location: Secreted {ECO:0000269|PubMed:28572090, ECO:0000269|PubMed:29046435, ECO:0000269|PubMed:32694673, ECO:0000269|PubMed:35202387, ECO:0000269|PubMed:36001956, ECO:0000269|PubMed:36465107}. Note=Secreted in the plasma. {ECO:0000269|PubMed:28572090, ECO:0000269|PubMed:29046435}.
Interaction partners:
- GDNF family receptor alpha-like
- TGF-beta receptor type-2
- GDNF family receptor alpha-4
- Proto-oncogene tyrosine-protein kinase receptor Ret
- Fibroblast growth factor 21
- Hepcidin
- Hepcidin-2
- Twisted gastrulation protein homolog 1
Sequence:
MAPPALQAQPPGGSQLRFLLFLLLLLLLLSWPSQGDALAMPEQRPSGPESQLNADELRGRFQDLLSRLHANQSREDSNSEPSPDPAVRILSPEVRLGSHGQLLLRVNRASLSQGLPEAYRVHRALLLLTPTARPWDITRPLKRALSLRGPRAPALRLRLTPPPDLAMLPSGGTQLELRLRVAAGRGRRSAHAHPRDSCPLGPGRCCHLETVQATLEDLGWSDWVLSPRQLQLSMCVGECPHLYRSANTHAQIKARLHGLQPDKVPAPCCVPSSYTPVVLMHRTDSGVSLQTYDDLVARGCHCA
Protein: Uncharacterized amino-acid permease C1039.01 (Q9US40)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized permease C29B12.14c
Sequence:
MSSIMEKTDVSSSKHSFTFEPSSDEVGKAAEIVDTHENFYDDQGDIDNPEELAELGYKQEFRRQLSLFGIFSISFSVLGMLPSVASTLVFGLWYVGYPGLLWAWLIAMFFLICVSMSMAEICSAMPTSGGLYYAAAVFAPKGWGPLASWITGWSNYIGNIIGQPSVNSSAASMILGAVTVNRPDFVIQRWQWFLLAVAIQCFNCVLACLPTRIISRINGVATYLNTAFLFIAGITILAYGGKNHNFVKGTKIWGDYINTTQWPTGFAILLSFNSPIWTMSGYDAPFHLSEECSNASVNAPKAIVMTAVIGGVVGWIMQIIVAYTLTDIDSVMNTSGSMWTAYLVQAMPPKAALGILSLTIISAIIMGQSALIASSRIAYSYARDGILPFSGWIGTVNPYTQTPVNAVICNCIISILILFLTFAGTVTLDAVFSVGAVAAFIAFTVPIAIRVFFTKDADFRRGPWNLGKFSRPIGLLAVSFVALMIPILCFPSVKNPTAQEMNWTCLVYGGPMLFTLVWYAISARKWFKGPKASAHYKRPGEESSDIVEGVQADIPSSSDQLKIKGDL
Protein: Euchromatic histone lysine methyltransferase 2 (A2ABF9)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
Interaction partners:
Sequence:
MRGLPRGRGLMRARGRGRAAPPGSRGRGRGGPHRGRGRPRSLLSLPRAQASWTPQLSTGLTSPPVPCLPSQGEAPAEMGALLLEKETRGATERVHGSLGDTPRSEETLPKATPDSLEPAGPSSPASVTVTVGDEGADTPVGATPLIGDESENLEGDGDLRGGRILLGHATKSFPSSPSKGGSCPSRAKMSMTGAGKSPPSVQSLAMRLLSMPGAQGAAAAGSEPPPATTSPEGQPKVHRARKTMSKPGNGQPPVPEKRPPEIQHFRMSDDVHSLGKVTSDLAKRRKLNSGGGLSEELGSARRSGEVTLTKGDPGSLEEWETVVGDDFSLYYDSYSVDERVDSDSKSEVEALTEQLSEEEEEEEEEEEEEEEEEEEEEEEEDEESGNQSDRSGSSGRRKAKKKWRKDSPWVKPSRKRRKREPPRAKEPRGVNGVGSSGPSEYMEVPLGSLELPSEGTLSPNHAGVSNDTSSLETERGFEELPLCSCRMEAPKIDRISERAGHKCMATESVDGELSGCNAAILKRETMRPSSRVALMVLCETHRARMVKHHCCPGCGYFCTAGTFLECHPDFRVAHRFHKACVSQLNGMVFCPHCGEDASEAQEVTIPRGDGVTPPAGTAAPAPPPLSQDVPGRADTSQPSARMRGHGEPRRPPCDPLADTIDSSGPSLTLPNGGCLSAVGLPLGPGREALEKALVIQESERRKKLRFHPRQLYLSVKQGELQKVILMLLDNLDPNFQSDQQSKRTPLHAAAQKGSVEICHVLLQAGANINAVDKQQRTPLMEAVVNNHLEVARYMVQRGGCVYSKEEDGSTCLHHAAKIGNLEMVSLLLSTGQVDVNAQDSGGWTPIIWAAEHKHIEVIRMLLTRGADVTLTDNEENICLHWASFTGSAAIAEVLLNARCDLHAVNYHGDTPLHIAARESYHDCVLLFLSRGANPELRNKEGDTAWDLTPERSDVWFALQLNRKLRLGVGNRAIRTEKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQSRLARLDPHPELLPELGSLPPVNT
Protein: Glycerophosphodiester phosphodiesterase, cytoplasmic (Glycerophosphoryl diester phosphodiesterase, cytoplasmic) (EC 3.1.4.46) (P10908)
Organism: Escherichia coli (strain K12)
Function: Glycerophosphoryl diester phosphodiesterase hydrolyzes deacylated phospholipids to G3P and the corresponding alcohols.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18083802}.
Interaction partners:
- Glycerophosphodiester phosphodiesterase, periplasmic
- sn-glycerol-3-phosphate import ATP-binding protein UgpC
- sn-glycerol-3-phosphate transport system permease protein UgpE
- sn-glycerol-3-phosphate transport system permease protein UgpA
- Lysophospholipase L2
- Ethanolamine ammonia-lyase reactivase EutA
- Ethanolamine ammonia-lyase large subunit
- Ethanolamine ammonia-lyase small subunit
- sn-glycerol-3-phosphate-binding periplasmic protein UgpB
Sequence:
MSNWPYPRIVAHRGGGKLAPENTLASIDVGAKYGHKMIEFDAKLSKDGEIFLLHDDNLERTSNGWGVAGELNWQDLLRVDAGSWYSKMFKGEPLPLLSQVAERCREHGMMANIEIKPTTGTGPLTGKMVALAARELWAGMTPPLLSSFEIDALEAAQQAAPELPRGLLLDEWRDDWRELTARLGCVSIHLNHKLLNKARVMQLKDAGLRILVYTVNKPQRAAELLRWGVDCICTDAIDVIGPNFTAQ
Protein: Candida glabrata strain CBS138 chromosome J complete sequence (Q6FPD2)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome H complete sequence
- GTP-binding protein RHO1
- Candida glabrata strain CBS138 chromosome C complete sequence
- Protein kinase C-like 1
- GTP-binding protein RHO4
Sequence:
MYRYNTPNTPERSKGGNTRSRDSPGVQGDVILPKLPPLNTRSSFLESDMMQSDVSIGWTPLTENTISTSGQFADEHIGYGNSPQLRSPKSPANRRNSLIYENFNGDSPMSVKSVGNGKSRRRPPPPSLQHSISQLDSYQSSPGSPATPFITKRRTNDFITPTKTKPYKSPFVGEQDIEDSMLQQSTHFAGKVYKSPFVGDLDSDIIISPSNANETTKTRKESSRVQSKTISNTELNFYSKPQIPLTSSRNITGISRFSDQVESFYSDSNYTFNNSSARNSSFNSFLGAKPLQYAPSVTAPTQAFSIDLIDEHKLYQCYSIYRLSDIYEWLLKVYFEWFNEYIFEKLDLFQIVQLLLEFQSPKTYEQEVIDSNVDRIMSSLINQGAIKFEVDNEQEIAVIVAGLTISSIFTDLLPCYSFIDSTFNEFDHSTICYSTTCCNRLSNESRQEIKVSEIINKSVGLWTDYWQLSAEELSEINPKEIQRQSFIFDLIILEERSLSMANAAVEIYGKRFDPDLLPDETNFASLAFDIFLPIIEIHKEFILKPLFWKIKTRGKFIDGIGKIYLKWCHEVRDAYLNYANAMATVHEVISWEKTHHTKFAEWLLETDNLPEITRSKMYHDVIFFGGYFKSLQNMPVTLSSILKNTSPSSEDYGALQLVIKEVTQLSADVDKVHGMAIDRRKLIRFSKQLVYSSGNKGSTTGYINIGNPEKMVKGDKLSLGLADPKRVMINCDTVLKKSDHWLEPYPVFLALLDNFLLITELVSKGLEKKYKLIDRPIPIEYLNLEIKRAPEEFNKDLPLGDSRPTSQIVSDLDNKSSLNSRSSVVGDLNYGHTGISNNLPSSTEFAFKVRNTATNDSYTFYVPNSIEWNNWMNAFKCCFKNRNNDDNRHPINLSIITAEFSYQDRNAPVNLPVAPEGSEIDSALKTYKRYLKDEFENIATTVFCSTEFDNEDTKFNLIATNSGVFLRRKNDYTTKFVKVLQNISVSRLQAVPKLGLLFVLDGQKLCYFSISSILAVYYNPERFLNANFVVGIVLKDKVSFFKFADDFGNSKQLFYERKGKIVVSTPEFHSIMNNFNCFKIYKKYYLPSSSKMLASHSISDIVIFKKSFMVFTKKNVFLFNDAFNELGASLPGFYNDKEMIAYIKHPHLNSGRFSSSSSKLDANLSMVTDVKKDIASGKTKPITAFRLQSGDGFLMVYDEAIVKINSSGMIPNWKNDILILDFYCTGASYHNGYLFLIGENLILVYQLSYEGTPISELTPVQIINSKKIELLNSGGMDYPTVTSSHPKIPNRQLLFSCIPANYQVK
Protein: C5orf34-like C-terminal domain-containing protein (Q586X3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSLRRFYNEVSVADHVVKACAWTDSSVDFVYGDGTVLSFCDEMQTFVAIDGSMGARSRLDISETGDEGKGGDYYFTALTLSKYEKKVSEALQIYNYYSPHPRVISGLTVTPCEVWRHPGPIDSLVVAVDRRLFERCGSRATLWCALRRVSLTLHGGRMTFSVRWPAPAVERSGARSIFVRPTDSRGFITGTVDSLRAFHYVWMEQTFPLIDPPREWIRMLEVALQFDEELPADHTPAEAAALATEDEECRMYYETTPRTAQDHKPCRFSSIRYDHVHALIANPQMQNAMCNGQIRNPRERVVWRYDADPMGRVPHAIYWGLGVCETKDVRHSLCLPEGRKASWPNSGVNRENTRTVDASATSGPREPYFVAGSVLCMIREDESVALVEPIGESYVVHHWRRSGGYKVYHQSADGLLGLPPVIPPEQHEGPLSNNGNSQLPPEDPSSPPVPEGEYSDGVVMSRAGGSLLYFSSVLEEAPFAVAQRGRYLPEVGGSCIEISQRNIAAARVEKQREMFDEIAGFDLRFALANGADRIARSATACSTSGLTIGPISPSDAAEAAIDRTQMRMVSDDPAINAAATAGSVVFLTSAIDGIGTFAALTNGTVRCHFDDRTILYLIPGGDDKEENLVATCLFRDATQCSIRLSKCLNNNPMFQYVAYALRFRRFVRLSPEARNAVVEGTNELKLQFLEETEWQQTNQVERNLQALFERTRELLDGSDKLCRTNRSLLNRDDSTYFT
Protein: Cyclic di-GMP phosphodiesterase PdeF (EC 3.1.4.52) (P77172)
Organism: Escherichia coli (strain K12)
Function: Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG. Truncated proteins consisting of the GGDEF/EAL domains (residues 319-747) or of the EAL domain alone (481-747) have c-di-GMP phosphodiesterase activity. They do not have diguanylate cyclase activity. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cyclic di-GMP phosphodiesterase PdeH
- Probable diguanylate cyclase CdgI
- Probable diguanylate cyclase DgcF
- Diguanylate cyclase DgcP
- Probable diguanylate cyclase DgcJ
- Diguanylate cyclase DgcM
- Probable diguanylate cyclase DgcT
- Probable diguanylate cyclase DgcI
- Probable diguanylate cyclase DgcC
- Diguanylate cyclase DgcN
Sequence:
MKLNATYIKIRDKWWGLPLFLPSLILPIFAHINTFAHISSGEVFLFYLPLALMISMMMFFSWAALPGIALGIFVRKYAELGFYETLSLTANFIIIIILCWGGYRVFTPRRNNVSHGDTRLISQRIFWQIVFPATLFLILFQFAAFVGLLASRENLVGVMPFNLGTLINYQALLVGNLIGVPLCYFIIRVVRNPFYLRSYYSQLKQQVDAKVTKKEFALWLLALGALLLLLCMPLNEKSTIFSTNYTLSLLLPLMMWGAMRYGYKLISLLWAVVLMISIHSYQNYIPIYPGYTTQLTITSSSYLVFSFIVNYMAVLATRQRAVVRRIQRLAYVDPVVHLPNVRALNRALRDAPWSALCYLRIPGMEMLVKNYGIMLRIQYKQKLSHWLSPLLEPGEDVYQLSGNDLALRLNTESHQERITALDSHLKQFRFFWDGMPMQPQIGVSYCYVRSPVNHIYLLLGELNTVAELSIVTNAPENMQRRGAMYLQRELKDKVAMMNRLQQALEHNHFFLMAQPITGMRGDVYHEILLRMKGENDELISPDSFLPVAHEFGLSSSIDMWVIEHTLQFMAENRAKMPAHRFAINLSPTSVCQARFPVEVSQLLAKYQIEAWQLIFEVTESNALTNVKQAQITLQHLQELGCQIAIDDFGTGYASYARLKNVNADLLKIDGSFIRNIVSNSLDYQIVASICHLARMKKMLVVAEYVENEEIREAVLSLGIDYMQGYLIGKPQPLIDTLNEIEPIRESA
Protein: Uncharacterized protein (Q38CF5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Katanin p60 ATPase-containing subunit A-like 2
- Katanin p60 ATPase-containing subunit A1
- Katanin p60 ATPase-containing subunit A1
Sequence:
MAMRRSSPSPRPRVRSASVASIPDTQRCEGILSSRSIAGTARSIEYVGDRCVWAAAVDGRVLVYSLSDGEVVAEAAVRENTFCTVLRLVSRRRIWAGFADGFICCYDSSTANLLNEFVQHDGAVNCLATTPYSEFVYSGGEDWKVYQWLKESCTYVRLFSGHSNAVRCVVAHIVESASTRSVSEGVRSLGDDMYNNEEDEGGEGCNARVNESMEEYIISGSDDMTIKIWDPRAPLQIELNLACLTTLRGHNGGVHSMEVFRRKQELWSGDGEGALRVWDLHDVRKPSCVAVLEGQHSASISSIVRIDSCMWSSGKDSFVVLWDAYEKVALRRFVPGGRAASRPIFVMRRLYRAAHWVIWLGGLDRNIHSLSFAADGDIDGKLLRSEKRCAANKLRYMRLQERTMELCTLVEELEEKNKALETQVQQLNALLHRSLEASQPLDHGSGRSRSAGKGGVTFRRLKSDAEGDKAPSRLAVDTTLKLPSGIASRCSTADPSPEKSFKKDVRAWEKQEKQTITGDISDGQKLIDQMELITSAEFTLQDVSGVDGTSRLAFEAYKKEVELKLAEEELSRQALQRELAEATKYKTMWETKNDALRDAYEQIENLQRNLEGEQRYVNDLLQEMAQLSNKKVRGEGEEDLPCADNRTPTEPRDPSTGYSLYKSIPGNYWDNICTNYPDVLRDTLFSELSELVSSLGAVVTNIAYASTGECLLVEAVVGPTTVGREKMQSCLELHAFPQTRTLHESMSTPFRKDASVKKSEKDNGWKLLVEAKERAEMERDEALAVLQEATDELEAMYEYQRQVEERRAKTPGLCDITALRDQKNSSVTSSTSQACTKVPIYVATAEEYEEVLAVMGKLERERDEVLQLLQKSQANSVSTTNKATSTSFIDSQHRQHREDTAASQTVSVNEYSRVVAEKEGAEAECREARRKLQKALHELESLQKLHLQAEEQRSRTRGLAGSTRLHGRKSTNESLLESREGTKVPIYVATAEEYEEVLAVMGKLERERDEVLQLLQKSQANSVSTTNKATSTSFIDSQHRQHREDTAASQTVSVNEYSRVVAEKEGAEAECREARRKLQKALHELESLQKLHLQAEEEWRKKLNSSGYSESSWRGGKKPLLSFYPDGDPTLRGLGSGEHVKTDDTDALLSGEEVADHRLRGGRRNPSKGSTTFGSSDRTASADQRRSRLLPTASDIDIATGHVTPGLGSYFHNLAAKEEYASAATQNLTRPVDVGALDLKTSKFSRYRCMLGEMWGPLVKRYRALVEDVFLMEVFRATSIPPNYVKGLEFGRGGLFVEVDIYDVHSCENVNLCLQRHKFSVLDKLIRLSQSCSATAHDPHQLGEETSASQRGPGCVAERNLGLNGESRKFFQQTSHCIDEAQAKELDAFRCRRAFANSLRRGEETLRSLLISQSEIDPKVPVDSLALQREPIYCVTLDEYRCVLRQLGAASRRVTQRQRDISGDEQTRLWNEHVVKQAEKERRFARRLSHPYPQFAKGSHTE
Protein: Mitochondrial transcription termination factor 1 (C9JNM8)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MAPGNLWHMRNNFLFGSRCWMTRFSAENIFKSVSFRLFGVKCHNTDSEPLKNEDLLKNLLTMGVDIDMARKRQPGVFHRMITNEQDLKMFLLSKGASKEVIASIISRYPRAITRTPENLSKRWDLWRKIVTSDLEIVNI
Protein: 2-phospho-L-lactate guanylyltransferase (LP guanylyltransferase) (EC 2.7.7.68) (Q58297)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Guanylyltransferase that catalyzes the activation of (2S)-2-phospholactate (2-PL) as (2S)-lactyl-2-diphospho-5'-guanosine, via the condensation of 2-PL with GTP. It is involved in the biosynthesis of coenzyme F420, a hydride carrier cofactor. Is able to utilize other purine nucleotides including ATP, dGTP and ITP as cosubstrates in place of GTP but with a lower activity. Does not display lactate kinase activity.
Interaction partners:
- 2-phospho-L-lactate transferase
- Coenzyme F420:L-glutamate ligase
- 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase
- Putative molybdopterin biosynthesis protein MJ0886
- 5-amino-6-
- 5,10-methylenetetrahydromethanopterin reductase
- Probable metallo-hydrolase MJ0888
- F420-dependent NADP reductase
- Homocitrate synthase AksA
- Coenzyme gamma-F420-2:alpha-L-glutamate ligase
Sequence:
MNCGIKMKVIIPVSPINSLKTRLSEFLSGEERKNLLLNMLKDIIKALDGLDIVIVSRDEEILDFAKNELKAETIKEKYKGLNNAIKQAFEEIEDKEVIIIPADIPLIKKKHIEDILKLSKNYDLIIAPSRGGGTNLLYLKSKDLIEIKYEGFSFLKHLEEAKKRNLRYYIYDSFLISVDINTPEDLGEIFIHGNDTYTKNYLKSLGIDVEPKHSSAGRFVVKRR
Protein: Pollux, isoform E (A0A0B4KGK7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKTRLVSLTFRGSASVDPRYSASMLPWTINDIRSTESYTKLSVGIENGILESYNSDFELQFSHPLKHIVGMCRIIHKPQAKSIGNGFLQLKSSAGQTSSSSAVASSMGGAASSSLTGNGLRHTLTASTSYGSLSSSAACAYQLQLQQSAEASAEQPQNFMEFQGPITGLVYLLKDPKDPLLHIYLFECEAVEEMAELMHQMRDPAHTLGGSVGSIPQTLIGGGGGSHGNSNGALNGIHATPATNLKMSEAMRNAQHDTSPNPVSSKMKASKSYTHGLSSSSGTVNIPTSTSAQSNLSLLADISPNHTHFFEVMYVGKIRVSQKRVPNTFIDDALPKFKAYDAQRLRLLQNRKMSLSSEGGVGIEAKPSSSLKSHDLKEEDEEEQEQHKGHDDSQDSQAKPLVQLQLTGAEEGAAPRPLEDNKENKSPEKRPLLRGQSQIELGHKEHIPKQRDRSASQGCIPPYVEQNRTMVFLVGRCDLRLISPDRKQVLLYKDFKDVASCVHGQKSLDHFGIICRELNNDGYIGYVFKCQSEHVCDDIVAAIAQAFDTCAEQKKKQDTQIFSCEHCPMLWYHKLCTDVEGLSEKKTQALILRRIETLSDDEQEIVWAKFCGSEKTNSPVAEQNQFLMMLLRAHCESRQQRHVHDTAENRSEFLNQYLGGSTIFMKAKRSLTNSFDNLLKRKPSKDDIAVPSHNLRDIREGSAEPLGTQSPPEGFRSRSNTVGASPSSKPTAEQLKSPMMDIFIKVGNSPKEAETHQGSWRQAILNSVVTPSKGLDSEVPTEFLSPMRKPAKRGKRDAAELRELWRTAIRQTIMLNRMETENAMLQARQNENELKRIKLDYEEIVPCDKQLIERWEQIIERNSTQIGNKKDPKVLGHAIRTGVPRSKRGDVWTFLAEQHSMNTAPVDTKRFPNFNTPYHMLLKHLTEHQHAIFIDLGRTFPNHQFYKDPLGLGQLSLFNLLKAYSILDPELGYCQGLGFICGVLLLHCDEANSFQLLKHLMFRRNMRTKYLPDMKKFQLQLYQLSRLVKDHLPDLYVWLDQNDVSPTLYAAPWILTVFSSQFPLGFVARVFDLLFLESSDVIFKFAIALLSVHKQQLLAKDNFEEIMDYLKTVVPKMEHTCMEQIMKLVFSMDIGKQLAEYKVEYNVLQEEITTTNHHLEMLNREKTQNQHLEQQLQFAQSSIAQLETTRSSQQAQITTLQSQVQSLELTIQTLGRYVGQLVEHNPDLELPNEVRRMLQQLDDLDRQRRKPIFTERKIGKSVSVNSHLGFPLKVLEELTERDELGSPQKQKKEKTPFFEQLRQQQQQHRLNGGGQSSNVGESGSPTPPSRPNRLLDNASARTVMQVKLDELKLPEHVDKFVANIKSPLEVDSGVGTPLSPPSTASNSSGGSIFSRMGYRTTPPALSPLAQRQSYGVAITTAPCPQHMEEVAPATTMAVMPQEDVEEPQPMHPLSMVGGDVNVRFKGTTQLKSIRPVHHMRAIPLGGVQHPSSTEPAVRVAPVPVELAPPAATATTGRS
Protein: Pre-mRNA-splicing factor 38A (Q8NAV1)
Organism: Homo sapiens (Human)
Function: Involved in pre-mRNA splicing as a component of the spliceosome.
Subcellular location: Nucleus {ECO:0000269|PubMed:28781166}.
Interaction partners:
- Microfibrillar-associated protein 1
- Zinc finger matrin-type protein 2
- Splicing factor 3A subunit 3
- WD40 repeat-containing protein SMU1
- Transcription elongation regulator 1
- Pre-mRNA-processing-splicing factor 8
- Pre-mRNA-processing factor 6
- U4/U6.U5 tri-snRNP-associated protein 1
- WW domain-binding protein 4
- Ubiquitin-like protein 5
Sequence:
MANRTVKDAHSIHGTNPQYLVEKIIRTRIYESKYWKEECFGLTAELVVDKAMELRFVGGVYGGNIKPTPFLCLTLKMLQIQPEKDIIVEFIKNEDFKYVRMLGALYMRLTGTAIDCYKYLEPLYNDYRKIKSQNRNGEFELMHVDEFIDELLHSERVCDIILPRLQKRYVLEEAEQLEPRVSALEEDMDDVESSEEEEEEDEKLERVPSPDHRRRSYRDLDKPRRSPTLRYRRSRSRSPRRRSRSPKRRSPSPRRERHRSKSPRRHRSRSRDRRHRSRSKSPGHHRSHRHRSHSKSPERSKKSHKKSRRGNE