{"metadata":{"accession":"Q7SZN0","id":"FA5V_PSETE","source_organism":{"taxId":"8673","scientificName":"Pseudonaja textilis","fullName":"Pseudonaja textilis (Eastern brown snake)"},"name":"Venom prothrombin activator pseutarin-C non-catalytic subunit","description":["Snake prothrombin activator that attacks the hemostatic system of prey. This non-catalytic subunit is functionally similar to blood coagulation factor V (PubMed:12362232, PubMed:23869089). It serves as a critical cofactor for the prothrombinase activity of the catalytic subunit, which is similar to the blood coagulation factor X (PubMed:12362232, PubMed:23869089). The complex converts prothrombin to thrombin by sequential cleavage at two positions, Arg-320 followed by Arg-271 (PubMed:23869089). Cleavage at Arg-320 produces an active intermediate known as meizothrombin (PubMed:23869089). Meizothrombin is the 'second' substrate for prothrombinase, and it docks in an altered manner to present the second cleavage site (271) (PubMed:23869089). Cleavage at Arg-271 releases active thrombin from its pro-fragment (PubMed:23869089). This order of events is reversed if the protease component of prothrombinase is used on its own, suggesting that the 271 site is inherently more accessible to proteolysis (PubMed:23869089). The complex converts prothrombin to thrombin in presence but also in the absence of membrane (PubMed:23869089)"],"length":1460,"sequence":"MGRYSVSPVPKCLLLMFLGWSGLKYYQVNAAQLREYHIAAQLEDWDYNPQPEELSRLSESDLTFKKIVYREYELDFKQEEPRDALSGLLGPTLRGEVGDSLIIYFKNFATQPVSIHPQSAVYNKWSEGSSYSDGTSDVERLDDAVPPGQSFKYVWNITAEIGPKKADPPCLTYAYYSHVNMVRDFNSGLIGALLICKEGSLNANGSQKFFNREYVLMFSVFDESKNWYRKPSLQYTINGFANGTLPDVQACAYDHISWHLIGMSSSPEIFSVHFNGQTLEQNHYKVSTINLVGGASVTADMSVSRTGKWLISSLVAKHLQAGMYGYLNIKDCGNPDTLTRKLSFRELMKIKNWEYFIAAEEITWDYAPEIPSSVDRRYKAQYLDNFSNFIGKKYKKAVFRQYEDGNFTKPTYAIWPKERGILGPVIKAKVRDTVTIVFKNLASRPYSIYVHGVSVSKDAEGAIYPSDPKENITHGKAVEPGQVYTYKWTVLDTDEPTVKDSECITKLYHSAVDMTRDIASGLIGPLLVCKHKALSVKGVQNKADVEQHAVFAVFDENKSWYLEDNIKKYCSNPSAVKKDDPKFYKSNVMYTLNGYASDRTEVLRFHQSEVVQWHLTSVGTVDEIVPVHLSGHTFLSKGKHQDILNLFPMSGESATVTMDNLGTWLLSSWGSCEMSNGMRLRFLDANYDDEDEGNEEEEEDDGDIFADIFIPSEVVKKKEEVPVNFVPDPESDALAKELGLIDDEGNPIIQPRREQTEDDEEQLMKASMLGLRSFKGSVAEEELKHTALALEEDAHASDPRIDSNSARNPDDIAGRYLRTINRGNKRRYYIAAEEVLWDYSPIGKSQVRSRAAKTTFKKAIFRSYLDDTFQTPSTGGEYEKHLGILGPIIRAEVDDVIEIQFKNLASRPYSLHAHGLLYEKSSEGRSYDDKSPELFKKDDAIMPNGTYTYVWQVPPRSGPTDNTEKCKSWAYYSGVNPEKDIHSGLIGPILICQKGMIDKYNRTIDIREFVLFFMVFDEEKSWYFPKSDKSTCEEKLIGVQSLHTFPAINGIPYQLQGLTMYKDENVHWHLLNMGGPKDIHVVNFHGQTFTEEGREDNQLGVLPLLPGTFASIKMKPSKIGTWLLETEVGENQERGMQALFTVIDKDCKLPMGLASGIIQDSQISASGHVGYWEPKLARLNNTGKYNAWSIIKKEHEHPWIQIDLQRQVVITGIQTQGTVQLLQHSYTVEYFVTYSEDGQNWITFKGRHSETQMHFEGNSDGTTVKENHIDPPIIARYIRLHPTKFYNRPTFRIELLGCEVEGCSVPLGMESGAIKNSEITASSYKKTWWSSWEPSLARLNLEGGTNAWQPEVNNKDQWLQIDLQHLTKITSIITQGATSMTTSMYVKTFSIHYTDDNSTWKPYLDVRTSMEKVFTGNINSDGHVKHFFKPPILSRFIRIIPKTWNQYIALRIELFGCEVF","proteome":"UP000472273","gene":null,"go_terms":[{"identifier":"GO:0005507","name":"copper ion binding","category":{"code":"F","name":"molecular_function"}}],"protein_evidence":1,"source_database":"reviewed","is_fragment":false,"in_alphafold":true,"in_bfvd":false,"ida_accession":"646f5e9a260b46ae4a010b420737a969945f9f16","counters":{"domain_architectures":120,"entries":26,"isoforms":0,"proteomes":1,"sets":4,"structures":1,"taxa":1,"dbEntries":{"ssf":2,"cathgene3d":2,"cdd":6,"pfam":2,"smart":1,"profile":1,"pirsf":1,"panther":1,"prosite":3,"interpro":7},"proteome":1,"taxonomy":1,"similar_proteins":120}}}