ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q7NST5 | MPSITVRRLYQENQQKLNLTWVAGTGGSDNVIGNDDQRPTLALVGHLNFIHPNRVQVLGLAEVDYLNKLEQSAAKTALDQLFHKSMSVVMVANGQPVPRLLRDYCHSHNVPLMCSTLESPYLMDVLRIYLARALAVSTVLHGVFLDVFEIGVLIMGDSAMGKSELALELISRGHGMVADDAVELYRIGPDTLEGRCPPLLRDFLEVRGLGILNIRTIFGETAVRPKKVLKLIIHLVKANDQAMQALDRLNIQSETQDIIGVTVRKVVLPVAAGRNLAVLVEAAVRNYILQLRGIDSTREFIERHTNFLRDQENAPDID | Function: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation... |
P57291 | MKHTLQVIITEKELDIRVRELGQEITKKYRNSRNKMILIALLRGSFIFISDLCRRIHIEHEIDFMTTSSYGRGMLSSGDVKIIKDLDEDIYNKNVLIVEDIIDSGKTLSKVLDILKLRNPKSLSICTLLDKPECREVNINVDFIGFSILENFFIVGYGIDYAQSYRYLPNIGKVVFKK | Function: Purine salvage pathway enzyme which catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of hypoxanthine to yield IMP (inosine 5'-monophosphate). To a lesser extent, can also act on guanine leading to GMP, but shows a highly less efficie... |
Q54NJ8 | MSREVIFTEKEIKERVSELGRQITQDYKDSKNLVLVGILKGSFVFMSDLVRSIHLPNTNVSLEFMSISSYGAETSSSGVIRIMMDLRTSIEGKDVLIIEDIVDSGLTLKHLMELLNHRNPNSLHTAVLLRKKEGLKVEVPVKYMGFDIPMVFIIGYGLDFAENYRELPYLGELKEECYKK | Cofactor: Binds 2 magnesium ions per subunit. The magnesium ions are essentially bound to the substrate and have few direct interactions with the protein.
Function: Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosp... |
P45078 | MKKHHVDVLISENDVHARIAELGAQITKFYQEKQIDNLVVVGLLRGSFMFMADIVRQINLPVEIEFMTTSSYGTGMTTNHDVRITKDLDGDIKGKHVLIVEDIIDTGYTLEKVRDILNLREPASLTICTLLDKPSRREVEVPVEWVGFEIPDEFVVGYGIDYAQRHRNLGYIGKVVLEE | Function: Purine salvage pathway enzyme which catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of hypoxanthine to yield IMP (inosine 5'-monophosphate). To a lesser extent, can also act on guanine leading to GMP, but shows a highly less efficie... |
P00492 | MATRSPGVVISDDEPGYDLDLFCIPNHYAEDLERVFIPHGLIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKALNRNSDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVRQYNPKMVKVASLLVKRTPRSVGYKPDFVGFEIPDKFVVGYALDYNEYFRDLNHVCVISETGKAKYKA | Cofactor: Binds 2 magnesium ions per subunit. The magnesium ions are essentially bound to the substrate and have few direct interactions with the protein.
Function: Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosp... |
P43152 | MSNSAKSPSGPVGDEGRRNYPMSAHTLVTQEQVWAATAKCAKKIAEDYRSFKLTTDNPLYLLCVLKGSFIFTADLARFLADEGVPVKVEFICASSYGTGVETSGQVRMLLDVRDSVENRHILIVEDIVDSAITLQYLMRFMLAKKPASLKTVVLLDKPSGRKVEVLVDYPVITIPHAFVIGYGMDYAESYRELRDICVLKKEYYEKPESKV | Cofactor: Binds 2 magnesium ions per subunit. The magnesium ions are essentially bound to the substrate and have few direct interactions with the protein.
Function: Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosp... |
Q52374 | MSALRLRKVDALLAQATRALGAGRRLGFSSRGQHAELSLLPLLEDARIPADGVWLNTAVGPLLLSDAEALLSLLGEVPFTLGGEHQGWYWQLFNQRLSPVVADLLAPVAPFSDTPTELAIGCRVHVRLGSERLDTRLHAAPATLLRLLGSADWQVLNRNLDESWSVSTPLIVGELSLTREQIASLRPGDVVLPARCRFDSAGQGSVTLAGRQWAARTDQQAQHLFLQLSHEEHSHHEY | Function: Component of the type III secretion system, which is required for effector protein delivery, parasitism, and pathogenicity. Probably participates in the formation of a C-ring-like assembly along with hrcQb (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26034
Sequence Lengt... |
O85094 | MSTEDLYQEDVEMLDDYEDPSTEQHWSEEDGEPSGYATAEPDDHAAQEEQDEPPALDSLALDLTLRCGELRLTLAELRRLDAGTILEVTGISPGHATLCHGEQVVAEGELVDVEGRLGLQITRLVTRS | Function: Component of the type III secretion system, which is required for effector protein delivery, parasitism, and pathogenicity. Probably participates in the formation of a C-ring-like assembly along with HrcQa.
Sequence Mass (Da): 14077
Sequence Length: 128
Domain: The HrcQb-C domain interacts with the HrcQa C-te... |
Q60235 | MSTEDLYQDDVEMLDDYEEPVPEQADQQQRDDEYAEHAFGYADSDAEHEEQSGDHHESPMLDSLELDLTLRCGDLRLTLAELRRLDAGSILEVSGIAPGHATLCHGEQVVAEGELVDVEGRLGLQITRLVARS | Function: Component of the type III secretion system, which is required for effector protein delivery, parasitism, and pathogenicity. Probably participates in the formation of a C-ring-like assembly along with HrcQa (By similarity).
Sequence Mass (Da): 14793
Sequence Length: 133
Domain: The HrcQb-C domain interacts wit... |
Q46646 | MNTEQFDPMTFALFLGALSLIPMLMIVCTCFLKISMVLLITRNAIGVQQVPPNMALYGIALAATLFVMAPVFNQMQQQFSQVPADLSSMDNLKTSVTNGVAPLQKFMTHNTDPDILIHLQENSVRMWPKEMSDSVNKDNLLLVIPAFVLSELQAGFKIGFLIYIPFIVIDLIVSNVLLALGMQMVAPMTLSLPLKMLLFVLINGWTRLLDGLFYSYL | Function: Required for the secretion of harpin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24192
Sequence Length: 217
Subcellular Location: Cell membrane
|
Q52488 | MQNVEFASLIVMAVAIALLPFAAMVVTSYTKIVVVLGLLRNALGVQQVPPNMVLNGIAMIVSCFVMAPVGMEAMQRAHVQINAQGGTNITQVMPLLDAARDPFREFLNKHTNAREKAFFMRSAQQLWPPAKAAQLKDDDLIVLAPAFTLTELTSAFRIGFLLYLAFIVIDLVIANLLMALGLSQVTPSNVAIPFKLLLFVVMDGWSVLIHGLVNTYR | Function: Involved in the secretion of PopA, a proteinaceous elicitor of the hypersensitivity response in plants.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23739
Sequence Length: 217
Subcellular Location: Cell membrane
|
P35652 | MSDEKTEQPTDKKLEDAHRDGETAKSADLTAAAVLLSGCLLLALTASVFGERWRALLDLALDVDSSRHPLMTLKQTISHFALQLVLMTLPVGFVFALVAWIATWAQTGVVLSFKPVELKMSAINPASGLKRIFSVRSMIDLVKMIIKGVAVAAAVWKLILILMPSIVGAAYQSVMDIAEIGMTLLVRLLAAGGGLFLILGAADFGIQRWLFIRDHRMSKDEVKREHKNSEGDPHIKGERKKLARELADEAKPKQSVAGAQAVVVNPTHYAVAIRYAPEEYGLPRIIAKGVDDEALALREEAAALGIPIVGNPPLARSLYR... | Function: Involved in the secretion of PopA, a proteinaceous elicitor of the hypersensitivity response in plants.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38607
Sequence Length: 357
Subcellular Location: Cell membrane
|
P35656 | MAKKNAIQDFSGEIGIAALVVAVVALMVLPLPTMLIDALLGLNITLSVVLLMVTMYIPSATSLSAFPSLLLFTTLLRLSLNIASTKSILLHADAGHIIESFGKLVVGGNLVVGLVVFLIITTVQFIVIAKGSERVAEVGARFTLDAMPGKQMSIDADLRAGHLSPEEARKRRALLAMESQLHGGMDGAMKFVKGDAIAGLVITLVNILAGIVIGITYHNMTAGEAANRFAVLSIGDAMVSQIPSLLISVAAGVMITRVSDEEQAHKQSSLGMEIVRQLSTSARAMFTASALLMGFALVPGFPSFLFVALATLIFVFGYTL... | Function: Involved in the secretion of PopA, a proteinaceous elicitor of the hypersensitivity response in plants.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73991
Sequence Length: 690
Subcellular Location: Cell inner membrane
|
Q9SLJ2 | MAGLINKIGDALHIGGGNKEGEHKKEEEHKKHVDEHKSGEHKEGIVDKIKDKIHGGEGKSHDGEGKSHDGEKKKKKDKKEKKHHDDGHHSSSSDSDSD | Function: Intrinsically disordered and metal-binding protein. Binds to the divalent cations cobalt, nickel, copper and zinc, but not to magnesium, calcium, manganese or cadmium (Ref.8). Binding to metal ions decreases disordered state, decreases susceptibility to trypsin and promotes self-association. Can reduce the fo... |
Q9LW77 | MIRLRTYAGLSFMATLAVIYHAFSSRGQFYPATVYLSTSKISLVLLLNMCLVLMLSLWHLVKFVFLGSLREAEVERLNEQAWRELMEILFAITIFRQDFSSGFLPLVVTLLLIKALHWLAQKRVEYIETTPSVSKLSHFRIVSFMGFLLLVDSLFMYSSIRHLIQSRQASVSLFFSFEYMILATTTVAIFVKYVFYVTDMLMDGQWEKKPVYTFYLELIRDLLHLSMYICFFFVIFMNYGVPLHLLRELYETFRNFQIRVSDYLRYRKITSNMNDRFPDATPEELTASDATCIICREEMTNAKKLICGHLFHVHCLRSWL... | Function: Probable component of the HRD1 ubiquitin ligase complex that mediates the rapid degradation of misfolded endoplasmic reticulum (ER) proteins, a process called ER-associated degradation (ERAD). Targets the misfolded LRR receptor kinase BRI1. Functions redundantly with HRD3B.
Catalytic Activity: S-ubiquitinyl-[... |
Q6NPT7 | MIQLKVYAGLSTLATLVVIYHAFSSRGQFYPATVYLSTSKINLVVLLNMGLVLMLSLWNLVKIVFLGSLREAEVERLNEQAWRELMEILFAITIFRQDFSVGFISLVVTLLLIKGLHWMAQKRVEYIETTPSVTLLSHVRIVSFMVFLLILDCLLTYSSIQQLIQSRKASMSVFFTFEYMILATTTVSIIVKYAFYVTDMLKEGQWEGKPVYTFYLELVRDLLHLSMYLCFFLMIFMNYGLPLHLIRELYETFRNFKIRVTDYLRYRKITSNMNDRFPDATPEELSSNDATCIICREEMTSAKKLVCGHLFHVHCLRSWL... | Function: Probable component of the HRD1 ubiquitin ligase complex that mediates the rapid degradation of misfolded endoplasmic reticulum (ER) proteins, a process called ER-associated degradation (ERAD). Targets the misfolded LRR receptor kinase BRI1. Functions redundantly with HRD3A.
Catalytic Activity: S-ubiquitinyl-[... |
Q75CC8 | MPREVSWPMWAMFITATYALAGWSAYSCATSFDDPLSALFMASSGVHFVIWGNFLIVHYCLFVWAIIRVLFGQLTAIEYDHIFERLHVVLVTLASIVITMRKTYMAGHMTILFYTLCLVAHWVLRDRMDFVFQVHGTDSSLLGILCSRFMFSLLVLGMVDYKMLKFCVQNTNVDGKRHDLYLMLALSFAQLILDVLHVVLLTSLNLFEMVRSRRTRSANLVYEGGTTDDDADDEVFILEGKYIYETVFDLTITVLKVILDIIQEVFVPWSITVVYSIFVRSIKAGESFLLVYNYWKNNKKLYEKLSDVSEEQLDDTDSMC... | Function: E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of endoplasmic reticulum proteins (ERQC), also called ER-associated degradation (ERAD). Component of the HRD1 ... |
A8Y4B2 | MRVSAGLMIGGSCVATAATVLNAFVINKQFYPSIVYLSKSNASMAVLYFQGIVLVYLMFQLLKSILFGDLRAAEAEHLSERTWHAVLETCLAFTVFRDDFSAMFVMQFIGLLFIKCFHWLADDRVDMMERSPVITLRFHLRMMTVLAALGFADSYFVSSAYFSTITKGASSQIVFGFEYAILLALVLHVTIKYLLHMHDLRNPQSWDNKAVYLLYAELLINLIRCVLYGFFAVIMLRVHTFPLFSVRPFYQSVRALHKAFLDVILSRRAINAMNSQFPVVSNDELSAMDATCIICREEMTVESSPKRLPCSHVFHAHCLR... | Function: Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated ubc-7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system, which is also called the ER-associated degradatio... |
Q20798 | MRVSAGLMIGGSCVATAATILNAFLINKQFYPSIVYLSKSNASMAVIYVQGIVLVYLMFQLLKSILFGDLRAAEAEHLSERTWHAVLETCLAFTVFRDDFSAIFVMQFIGLLFIKCFHWLADDRVDMMERSPVITLRFHLRMMTVLAALGFADSYFVSSAYFTTITRGASAQIVFGFEYAILLALVLHVTIKYLLHMHDLRNPQSWDNKAVYLLYAELFINLIRCLLYGFFAVVMLRVHTFPLFSVRPFYQSVRALHKAFLDVILSRRAINAMNSQFPVVSAEDLAAMDATCIICREEMTVDASPKRLPCSHVFHAHCLR... | Function: Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated ubc-7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system, which is also called the ER-associated degradatio... |
Q95SP2 | MQLLLSSVCMALTSAVIGFAYYQKQQFYPAVVYITKSNASMGVIYIQFFVIVFMFGKLLSKIFLGTLRAAEFEHLLERFWYALTETCLAFTVFRDDFNPRFVALFTVLLFLKSFHWLAEERVDFMERSPVLGWLFHIRVGSLLTVLGILDYVLLIHAYNSTLVRGPTVQLVFGFEYAILLTVIASTAIKYVLHAAEMRTDTPWENKAVFLLYTELVIGLIKVVLYILFVVIMAKIYALPMFVFRPMFFTIRNFRKALNDVIMSRRAIRNMNTLYPDATPEELRQSDNICIICREDMVNHSKKLPCGHIFHTTCLRSWFQR... | Function: Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation. Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involv... |
Q5Z880 | MIRLQTYAAFSLMATATAVYYAFSSREQFYPAMVYLSTSKICFVLLLNTGLVAMCVAWQLVKRLFLGTLREAEVERLNEQAWREVVEILFAVTIFRQDFSVSFLAMVAALLLVKALHWLAQKRVEYIETTPSVPMLSHARIVSFMLFLLVVDCLFLSNSLRSLIHKREASVAIFFSFEYMILATSTVSTFVKYIFYVSDMLMEGQWEKKAVYTFYLELISDLVHLSLYMLFFIAIFLNYGVPLHLIRELYETFRNFRIRIADYVRYRKITSNMNERFPDATADELNASDATCIICREEMTTAKKLLCGHLFHVHCLRSWL... | Function: Probable component of the HRD1 ubiquitin ligase complex that mediates the rapid degradation of misfolded endoplasmic reticulum (ER) proteins, a process called ER-associated degradation (ERAD).
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ub... |
O74757 | MKFILYVLASLVLFGLSVLLSLYSSANVYSATVMISQSPVHITIGLNVCLCLFFAIANALKTLLFGSLQTFELELLYEQFWITLTEIMLAITVFREAISISFFMLLSTLMFARVFHSICSFRTERLQIQLTDQRFHIFSRLTCAYFVLSILDASLIYLCFTSEHLGDKSTRMLFVCEFSVLLLNLTIEASKLCIYLYEARHLDQVWDEKSTYLFRLEVCRDGLRLLAYSLLFMYQFPYVSVPIYSIRQMYTCFYSLFRRIREHARFRQATRDMNAMYPTATEEQLTNSDRTCTICREEMFHPDHPPENTDEMEPLPRGLD... | Function: E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of endoplasmic reticulum proteins (ERQC), also called ER-associated degradation (ERAD). Component of the hrd1 ... |
B5VL26 | MQYKKTLVASALAATTLAAYAPSEPWSTLTPTATYSGGVTDYASTFGIAVQPISTTSSASSAATTASSKAKRAASQIGDGQVQAATTTASVSTKSSAAAVSQIGDGQIQATTKTTAAASLKLVMVKIQATTKTTAAAVSQIGDGQVQATTKTTAAAVSQITDGQVQATTKTTQAASQVSDGQVQATSATSASAAATSTDPVDAVSCKTSGTLEMNLKGGILTDGKGRIGSIVANRQFQFDGPPPQAGAIYAAGWSITPDGNLAIGDNDVFYQCLSGTFYNLYDEHIGSQCTPVHLEAIDLIDC | Function: Component of the outer cell wall layer. Required for stability of the cell wall and for optimal growth. Required for resistance against several antifungal and cell wall-perturbing agents and for tolerance to heat shock (By similarity).
PTM: Covalently linked to beta-1,3-glucan of the inner cell wall layer via... |
P32478 | MQYKKTLVASALAATTLAAYAPSEPWSTLTPTATYSGGVTDYASTFGIAVQPISTTSSASSAATTASSKAKRAASQIGDGQVQAATTTASVSTKSTAAAVSQIGDGQIQATTKTTAAAVSQIGDGQIQATTKTTSAKTTAAAVSQISDGQIQATTTTLAPKSTAAAVSQIGDGQVQATTTTLAPKSTAAAVSQIGDGQVQATTKTTAAAVSQIGDGQVQATTKTTAAAVSQIGDGQVQATTKTTAAAVSQIGDGQVQATTKTTAAAVSQITDGQVQATTKTTQAASQVSDGQVQATTATSASAAATSTDPVDAVSCKTSG... | Function: Component of the outer cell wall layer. Required for stability of the cell wall and for optimal growth. Required for resistance against several antifungal and cell wall-perturbing agents and for tolerance to heat shock.
PTM: Covalently linked to beta-1,3-glucan of the inner cell wall layer via an alkali-sensi... |
Q6BNP6 | MFGGRQSNNKSNDSLEQLINRATDETLTNDNWQYILDVCDNISSNPEEGTKQGIKVVSSRLASKDANIILRTLSLLVAMAENCGSRMRQEIATTSFVQESLLKKFTDRRLHKTVKFRVAEVIKQLHDSFKTDPSLKPMTDAYNRLVNDYSQYSAETADGPAKPAKKERSRQDKKKEEDELQRVLKLSLQEYEREQTVKKSYLNNKPLPQAQNESQYQEQPRQQQQQQQVLQNQPMHSTPTGQQSTQSPAESQTIATVSKVRALYDLISYEPDELSFRKGDIITVIESVYRDWWRGSLVNGKTGIFPLNYVTPVVTKTPQE... | Function: Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 58084
Sequence Length: 512
Subcellular Location: Endosome membrane
|
Q6CVA8 | MSSHPKVKKAIERATDPGLRVDNWGYLIEVCDLVKVDAEDRGQYAMKIIEERLLKQDANMILRTLSLVVALAENCGSRLQQAISSKHFTGILYKIVDDSQVHVAVKREVLKVVHQLADSFKNDPSLKYMHDLESKIKISHPELISEPRVPKKKEMSKDREVEEEKELAEALRLSLLEFEKTGSRQQVQQPQQQQQQQQQQQQQQQQKLYPQNAEAQQQQAPTVIRKVRAMYDFNSTEQDELSFKKGDLICVVEQVYRDWWRGTLAGSVGIFPLNYVTPVTEPSQQELAAERAKDEQVFAQKDNVDRLQNKLREAGNADIT... | Function: Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 57400
Sequence Length: 508
Subcellular Location: Endosome membrane
|
A4RF61 | MFRAQATTPYDTAIAKATDENLTSEDWGAIMEVCDRVAGDDNGAKEAVQALIRRLAHRNANVQLYTLEVANALSQNCGKPMHRELASRAFTEALLKLANERNTHNQVKAKILEGTKEWSDMFKDDADLGIMYDAYYRLKQTNPQLQPPSAPQKNSLTDVDRQKEEEELQIALKLSLQEEERKKQQTPAGPSGAAGPSSSSAPDQAGTPSGQGADAGAGAAAVPLQPTGTGTTAATVSRVRALYDFVPSEDGELEFKKGDVIAVLESVYKDWWRGSLKGKTGIFPLNYVEKLADPTPDELQREAQMEAEVFSEIKNVEKLL... | Function: Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 76839
Sequence Length: 718
Subcellular Location: Endosome membrane
|
Q0U6X7 | MFRAQSNIFDDVVVKATDENLTSENWEYILDVCDKVGSSDTGAKDAVAAMIKRLAHRNANVQLYTLELANALSQNCGIQMHKELASRSFTDAMLRLANDRNTHQAVKAKILERMGEWSEMFSRDPDLGIMEGAYMKLKTQNPNLRAPSKPQKTQISDSDRQKEEEELQMALAMSIKESKGATPSAAKANAPQESNAGSSSQAAPAPQPVQPGTTAATVSRVRALFDFQPSEPGELQFKKGDIIAVLESVYKDWWKGSLRGNTGIFPLNYVEKLQDPTREELEKEAQTEAEVFAQIRNVEKLLALLSTNTQAGGGDGRDNE... | Function: Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 66902
Sequence Length: 618
Subcellular Location: Endosome membrane
|
A3LXQ8 | MYKAKKTTDSSLESLIKRATDETLTTNNWEYIIAVCDKVKSDPEVATKKAITILTTRLQSKDANVLLRTLSLIIALGENCGSRMQQEIASEAFLKPLTKKLKEKKLHETVKVEIAKLIEQLHQSFKSDPSLKPMSDAYNKIKQEHPRYLERNVPAKPEKHDVSSKTQSEEDELQRVINLSLQEYEREQFSKSLQKPLPDPKKTSPRNANIAQEDSDDKKPEISKVRAMFDLVSHEKDELSFRKGDLINVIEVVYRDWWRGSLPTGEVGIFPLNYVAPVYAKSSDQIEKELQIENRLLNVESKKIDKVLAMLSAATNGNEN... | Function: Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53698
Sequence Length: 475
Subcellular Location: Endosome membrane
|
O74749 | MFRGKPNSIETLILQATDEKNTKEKWDVIMDACDQLSSTSGDVGRNSIKFLNKRLDTANANIQLLALTLTDAIVKNCKTSIVREISSRTFTDSLLKIASDSTTHNRVRSRIAVLVNEWAEIMKKDPNMSLMQDICEKIRKLDIVDLRAPKKPEKEAMNELELKREEEELQYALALSLSESTAQSNKVENPQSTKDEPLQKTNQRQESNLATSPASTVSRVRALYDFAATEQGELSFKKGDIILVLESVYKDWWKGSCKNAVGIFPVNYVQRVVEPTIEQQRQSAHMEQQVFDALPQIDELLDTLSTTSPDAADDDALQGK... | Function: Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 42497
Sequence Length: 373
Subcellular Location: Endosome membrane
|
Q4P5J4 | MFTAKNPFEDIVLKATSDELTSENWELNLEVCDKVSSGGDTAARNCIAAIQKRLVHRNANVQLYALTLADAVAKNCGLAAHQEIASRSFTQTLARICLDRNTHSTVKKRCSALVKEWAGEFDDQSLGLMKETYESLKSQDAVAEDETPAEPPREPTSEQLRAEDEELRRALELSIQDQGGRNAWPSYNTEQAETSGSSAPAAASSSSSAYQPTSQSLAPAQQQQQQQHDANHTNGTSSSAHAQPLSAATPPAVASRVRALYDFSPTEPGELAFSRGEVIRVLDSVYEHWWRGEVRGEAGIFPVNYVEVLPDPTPDELQRE... | Function: Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 65613
Sequence Length: 593
Subcellular Location: Endosome membrane
|
Q6C2N2 | MFRSSEPVSPLDDVVTKATDENLTTENWQYILDVCDEVNNDPENGAKNVITSVTKRLNKKFANTQLYALTLVISLSSNCGSKMQQAIASKAFVKTLMKLANDSAVHKSVKSKVLEVLEQLTDEYKKDPSLRLIEEAYDELSRKKPDLKAPAKPEKHKITEQERQREEEELQMVLALSLSETNTSGSFQQHHQTNSQIQPPVNNSHFATDPHQQQQQQQQQHNQQDYGQQSNNANTNNNAPAVEDPTPTVATVSRVKALYDLNATEPGELSFRKGDIITVLESVFRDWWRGSLRGQVGIFPLNYVMPIAEPTPAEIEKEAQ... | Function: Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 73584
Sequence Length: 685
Subcellular Location: Endosome membrane
|
P38753 | MSSSAIKIRNALLKATDPKLRSDNWQYILDVCDLVKEDPEDNGQEVMSLIEKRLEQQDANVILRTLSLTVSLAENCGSRLRQEISSKNFTSLLYALIESHSVHITLKKAVTDVVKQLSDSFKDDPSLRAMGDLYDKIKRKAPYLVQPNVPEKHNMSTQADNSDDEELQKALKMSLFEYEKQKKLQEQEKESAEVLPQQQQQHQQQNQAPAHKIPAQTVVRRVRALYDLTTNEPDELSFRKGDVITVLEQVYRDWWKGALRGNMGIFPLNYVTPIVEPSKEEIEKEKNKEAIVFSQKTTIDQLHNSLNAASKTGNSNEVLQ... | Function: Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 51161
Sequence Length: 452
Subcellular Location: Endosome membrane... |
G5EFT5 | MQPTGNQIQQNQQQQQQLIMRVPKQEVSVSGAARRYVQQAPPNRPPRQNHQNGAIGGKKSSVTIQEVPNNAYLETLNKSGNNKVDDDKLPVFLIKLWNIVEDPNLQSIVHWDDSGASFHISDPYLFGRNVLPHFFKHNNMNSMVRQLNMYGFRKMTPLSQGGLTRTESDQDHLEFSHPCFVQGRPELLSQIKRKQSARTVEDKQVNEQTQQNLEVVMAEMRAMREKAKNMEDKMNKLTKENRDMWTQMGSMRQQHARQQQYFKKLLHFLVSVMQPGLSKRVAKRGVLEIDFCAANGTAGPNSKRARMNSEEGPYKDVCDL... | Function: Functions as a stress-inducible and DNA-binding transcription factor, playing a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones, heat shock proteins (HSPs), that protect cells from cellular insult damage . Upon... |
Q00613 | MDLPVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQGQFAKEVLPKYFKHNNMASFVRQLNMYGFRKVVHIEQGGLVKPERDDTEFQHPCFLRGQEQLLENIKRKVTSVSTLKSEDIKIRQDSVTKLLTDVQLMKGKQECMDSKLLAMKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSNRILGVKRKIPLMLNDSGSAHSMPKYSRQFSLEHVHGSGPYSAPSPAYSSSSLYAPDAVASSGPIISDITELAPASPMASPGGSIDERPLSSSPLVRVKEEPPSPPQSPRVEEASPGRPSS... | Function: Functions as a stress-inducible and DNA-binding transcription factor that plays a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones, heat shock proteins (HSPs), that protect cells from cellular insult damage . In... |
P22335 | MSQRTAPAPFLLKTYQLVDDAATDDVISWNEIGTTFVVWKTAEFAKDLLPKYFKHNNFSSFVRQLNTYGFRKIVPDKWEFANENFKRGQKELLTAIRRRKTVTSTPAGGKSVAAGASASPDNSGDDIGSSSTSSPDSKNPGSVDTPGKLSQFTDLSDENEKLKKDNQMLSSELVQAKKQCNELVAFLSQYVKVAPDMINRIMSQGTPSGSSLEELVKEVGGVKDLEEQGSYNDNDDKEDDDEKGDTLKLFGVLLKEKKKKRGPDENIETCGGRGKMMKTVDYNGPWMKMSSPAGESSKVCN | Function: DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription.
PTM: Exhibits temperature-dependent phosphorylation.
Sequence Mass (Da): 33195
Sequence Length: 301
Subcellular Location: Nucleus
|
O75031 | MGEAGAAEEACRHMGTKEEFVKVRKKDLERLTTEVMQIRDFLPRILNGEVLESFQKLKIVEKNLERKEQELEQLKMDCEHFKARLETVQADNIREKKEKLALRQQLNEAKQQLLQQAEYCTEMGAAACTLLWGVSSSEEVVKAILGGDKALKFFSITGQTMESFVKSLDGDVQELDSDESQFVFALAGIVTNVAAIACGREFLVNSSRVLLDTILQLLGDLKPGQCTKLKVLMLMSLYNVSINLKGLKYISESPGFIPLLWWLLSDPDAEVCLHVLRLVQSVVLEPEVFSKSASEFRSSLPLQRILAMSKSRNPRLQTAA... | Function: Meiotic recombination factor component of recombination bridges involved in meiotic double-strand break repair. Modulates the localization of recombinases DMC1:RAD51 to meiotic double-strand break (DSB) sites through the interaction with BRCA2 and its recruitment during meiotic recombination (By similarity) .... |
Q9D4G2 | MAATVGDGSGTEEACRNMESKEEFVKVRKKDLERLTTEVMQIRDFLPRILNGELLESFQKLKMVEKNLERKEQELEQLIMDREHFKARLETAQADSGREKKEKLALRQQLNEAKQQLLQQAEYCTQMGAVTCTLLWGVSSSEEVVKTILGGDKALKFFNITGQTMESFVKSLDGDVKEVDSDENQFVFALAGIVTNVAAIACGREFLVNSSRVLLDTMLQLLGDLKPGQCTKLKVLMLMSLYNVSINSKGLKYITESPGFIPLLWWLLSDPDAEVCLHTLRLIQSVVLEPDVFSKVASELQSSLPLQRILAMSKSRNSHL... | Function: Meiotic recombination factor component of recombination bridges involved in meiotic double-strand break repair. Modulates the localization of recombinases DMC1:RAD51 to meiotic double-strand break (DSB) sites through the interaction with BRCA2 and its recruitment during meiotic recombination. Indispensable fo... |
B3PI66 | MTTILSVRRDGQVVIGGDGQVSLGNTVMKGNARKVRRLYKNQVLAGFAGGTADAFTLFERFEAKLESHNGQLTRAAVELAKDWRTDRSLRRLEALLAVADKEASLIITGNGDVIQPEDDLIAIGSGGMYAQAAARALLENTQLDARNIVEKGLKIAGDICVYTNQNHTIEVLDY | Function: Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
Catalytic Activity: ATP-dependent cleavage of peptide bonds with broad specificity.
Sequence Mass (Da): 18874
Sequence Length: 174
Subcellular Location: Cytoplasm
EC: 3.4.25.2
|
P04553 | MARYRCCRSQSRSRYYRQRQRSRRRRRRSCQTRRRAMRCCRPRYRPRCRRH | Function: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex.
PTM: Phosphorylated by SRPK1.
Sequence Mass (Da): 6823
Sequence Length: 51
Subcellular Location: Nucleus
|
P36182 | EFISYPIYLWTEKTTEKEISDDEDDEPKKDEEGAVEEVDEDKEKEKGKKKKIKEVSHEWQLINKQKPIWLRKPEEITKDEYASFYKSLTNDWEEHLAVKHFSVEGQLEFKAILFVPKRAPFDLFDTRKKMNNIKLYVRRVFIMDNCEELIPEYLGFVKGVVDSDDLPLNISREMLQQNKILKVIRKNLVKKCIEMFNEIAENKEDYNKFYEAFSKNLKLGIHEDSQNRAKLADLLRYHSTKSGDEMTSLKDYVTRMKEGQKDIYYITGESKKAVENSPFLERLKKKGYEVLYMVDAIDEYAVGQLKEYDGKKLVSATKEG... | Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes... |
P02829 | MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVEKEVPIPEEEKKDEEKKDEEKKDEDDKKPKLEEVDEEEEKKPKTKKVKEEVQEIEELNKTKPLWTRNPSDITQEEYNAFYKSISNDWEDPLYVKHFSVEGQLEFRAI... | Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open confo... |
P02828 | MPEEAETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELYIKLIPNKTAGTLTIIDTGIGMTKSDLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVADKVTVTSKNNDDEQYVWESSAGGSFTVRADNSEPLGRGTKIVLYIKEDQTDYLEESKIKEIVNKHSQFIGYPIKLLVEKEREKEVSDDEADDEKKEGDEKKEMETDEPKIEDVGEDEDADKKDKDAKKKKTIKEKYTEDEELNKTKPIWTRNPDDISQEEYGEFYKSLTNDWEDHLAVKHFSVEGQL... | Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes... |
P51819 | MADVQMAEAETFAFQAEINQLLSLIINTFYSNKEIFLRELISNASDALDKIRFESLTDKSKLDAQPELFIRLVPDKTNKTLSIIDSGVGMAKADLVNNLGTIARSGTKEFMEALQAGADVSMIGQFGVGFYSAYLVAEKVIVTTKHNDDEQYIWESQAGGSFTVTRDVDGEQLGRGTKITLFLKEDQLEYLEERRIKDLVKKHSEFISYPIYLWTEKTTEKEISDDEDDEPKKEEEGDIEEVDEDKEKEGKKKKKIKEVSHEWQLINKQKPIWLRKPEEITKEEYASFYKSLTNDWEDHLAVKHFSVEGQLEFKAILFVP... | Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes... |
P27741 | MTETFAFQAEINQLMSLIINTFYSNKEIFLRDVISNASDACDKIRYQSLTDPSVLGDATRLCVRVVPDKENKTLTVEDNGIGMTKADLVNNLGTIARSGTKAFMEALEAGADMSMIGQFGVGFYSAYLVADRVTVTSKNNSDEVYVWESSAGGTFTITSAPESDMKLPARITLHLKEDQLEYLEARRLKELIKKHSEFIGYDIELMVEKTTEKEVTDEDEEEAKKADEDGEEPKVEEVTEGEEGKKKKTKKVKEVTKEYEVQNKHKPLWTRDPKDVTKEEYAAFYKAISNDWEDPPATKHFSVEGQLEFRAIMFVPKRAP... | Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes... |
P27890 | TKKVKEVTKEYEVQNKHKPLWTRDPKDVTKEEYAAFYKAISNDWEDPMATKHFSVEGQLEFRSIMFVPKRAPFDMFEPNKKRNNIKLYVRRVFIMDNCEDLCPDWLGFVKGVVDSEDLPLNISRENLQQNKILKVIRKNIVKKCLEMFDEVAENKEDYKQFYEQFGKNIKLGIHEDTANPKKLMEFLRFYSTESGLEMTTLKDYVTRMKEGQKSIYYITGDSKKKLESSPFIEQARRRGLEVLFMTEPIDEYVMQQVKDFEDKKFACLTKEGVHFEESEEEKQQREEEKAACEKRCKTMKEVLGDKVEKVTVSDRLSTSP... | Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes... |
Q07078 | MASETETFAFQAEINQLLSLIINTFYSNKEIFLRELISNSSDALDKIRFESLTDKSKLDAQPELFIHIVPDKASNTLSIIDSGVGMTKSDLVNNLGTIARSGTKEFMEALAAGADVSMIGQFGVGFYSAYLVAERVVVTTKHNDDEQYVWESQAGGSFTVTRDTSGEQLGRGTKITLYLKDDQLEYLEERRLKDLVKKHSEFISYPISLWTEKTTEKEISDDEDEEEKKDAEEGKVEDVDEEKEEKEKKKKKIKEVSHEWNVMNKQKPIWLRKPEEITKEEYAAFYKSLTNDWEEHLAVKHFSVEGQLEFKAILFVPKRA... | Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes... |
P12861 | MTETFAFQAEINQLMSLIINTFYSNKEIFLRELISNSSDACDKIRYQSLTNQSVLGDEPHLRIRVIPDRVNKTLTVEDSGIGMTKADLVNNLGTIARSGTKSFMEALEAGGDMSMIGQFGVGFYSAYLVADRVTVVSKNNEDDAYTWESSAGGTFTVTSTPDCDLKRGTRIVLHLKEDQQEYLEERRLKDLIKKHSEFIGYDIELMVENTTEKEVTDEDEDEEAAKKAEEGEEPKVEEVKDGVDADAKKKKTKKVKEVKQEFVVQNKHKPLWTRDPKDVTKEEYASFYKAISNDWEEQLSTKHFSVEGQLEFRAILFLPK... | Function: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes... |
Q49ZT8 | MTTCLIVDDDPKILEYVSKYIEREHFETIVQSSAENALSYLETHQVDIAIVDVMMGKMSGFELCKILKEDFDIPVIMLTARDALSDKEQAYLTGTDDYVTKPFEVKELMFRIKAVLKRYNVNINNEVSIGNLTLNQSYLEIQSSSKSMNLPNKEFQLLFLLASNPRQVFNRDALIEKIWGFDYEGDERTVDVHIKRLRKRLEKIDASVTIHTVRGLGYKVDDHV | Function: Member of the two-component regulatory system HssS/HssR involved in intracellular heme homeostasis and tempering of staphylococcal virulence. Phosphorylated HssR binds to a direct repeat sequence within hrtAB promoter and activates the expression of hrtAB, an efflux pump, in response to extracellular heme, he... |
A5FUZ5 | MPNLIRTGLLMAALTALFVAIGYWIGRGAGAAIALAFAAAGNFVAYWVSDRAVLAMYGAQPANQAAFPRLVAQVDRLASKAGLPPPRVYVIDNDQPNAFATGRNPQHAAIAVTTGLLGALDEAELAGVIAHELSHIRHRDTLTMTVTATLAGAIGMISNLAIFFGGSDERRSSPFAGIAGLLLLLLAPLTATLVQLAISRTREYAADARAASLTGQPLALARALMRIDEMARWVPNDDAERNPATASLFIVNPLSGTTFDTLFATHPPIRERVARLRHMAQFDVSKN | Cofactor: Binds 1 zinc ion per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30460
Sequence Length: 287
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
|
Q9YD67 | MGLTVLALIGGYIVVLGVAAWALDAFTGLSGTGVAFMLSLLALAMVLVQWLFSPYIINMVYRTREPLPGEEWIVAEVEQLARRSGLKPPKVVVSEMNMPNAFAYGSPIAGSYVAVTRGLLRLLPKDEVRAVLAHEVGHLKHRDVTVILALSLIPIAAFLIGRTLVWAGILGGGGGERRGNPMALVAVGAALLAAGMVFQLIVSHFNRLREYYADAHSALVTGSPRSLQRALARIHAAYEHNPHLVEEARSNEMASMLFIVAPLTSLTASPLVDVDYLVERLKEQETNPLVELFSTHPPVSKRLRFLDRLASRIGGIEHY | Cofactor: Binds 1 zinc ion per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34671
Sequence Length: 319
Subcellular Location: Cell membrane
EC: 3.4.24.-
|
Q8UBM5 | MNMMRTAMLLAFMTALFMGVGFLIGGKGGMMIALLIAAGMNLFSYWNSDKMVLSAYRAREIDEANAPEFFHMIRDLSQNAGLPMPKVYIYDSPQPNAFATGRNPENAAVAASTGLLERLTPEEVAGVMAHELAHVQNRDTLTMTITATLAGAISMLGNFAFFFGGNRENNNNPLGFIGVLVAMIVAPLAAMLVQMAISRTREYSADRRGAEICGNPLWLASALQKISGMAQQIHNDDAERNPATAHMFIINPLSGERMDNLFSTHPNTENRVAALHAMAQEFSPRASTPPPSGDRPVRKSGSVPTTGWRRGNENERKGPW... | Cofactor: Binds 1 zinc ion per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34932
Sequence Length: 321
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
|
Q9K006 | MKRIFLFLATNIAVLVVINIVLAVLGINSRGGTGSLLAYSAVVGFTGSIISLLMSKFIAKQSVGAEVIDTPRTEEEAWLLNTVEAQARQWNLKTPEVAIYHSPEPNAFATGASRNSSLIAVSTGLLDHMTRDEVEAVLAHEMAHVGNGDMVTLTLIQGVVNTFVVFLSRIIANLIARNNDGSQSQGTYFLVSMVFQILFGFLASLIVMWFSRQREYRADAGAAKLVGAPKMISALQRLKGNPVDLPEEMNAMGIAGDTRDSLLSTHPSLDNRIARLKSL | Cofactor: Binds 1 zinc ion per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30202
Sequence Length: 279
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
|
Q3JE43 | MIKRVILFLATNLAVLLVLSISMRLLGIESLLNQQGTDLNLNALLIFAAIIGFSGSLISLAISKFTAKRLTGAQVIERPRSTTEVWLLETVQRHARMAGIGMPEVAIYASPEPNAFATGWNRNAALVAVSSGLLEQMNQNEVEAVLGHEISHVANGDMVTLALIQGVVNTFVIFLARIIGHLVDRVVFKTERGYGPAFFITTLIAQTVLAILASLIVLWFSRQREFRADAGGAQLAGKEKMIAALERLGRMAQEGLPEQLQAFGIAGGERSQGWKRLFMSHPPIEERIAALRAEH | Cofactor: Binds 1 zinc ion per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32175
Sequence Length: 295
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
|
B2J204 | MGNQVKTAALLAALSGLLIAISYWVIGGSSGLIIGIGLAAVTNLFSWYQSDKIALAVYQAQPVSEGEAPGLYRMVQRLSDRANIPMPRVYIVPSQGANAFATGRDPEHAAVAVTEGILNILPDDELEGVIAHELTHIINRDTLTQAVAATVAGAISFLAQMVSYSLWFGGGSRDDNRGANPLGVLLTVMLAPLAATIIQLAISRTREFSADAGSARLTGNPRALARALQRLEALAKQIPLNANPAFEPLLIINSISGQFLGNLFSSHPATEARVAALLKLEQQLPTKAY | Cofactor: Binds 1 zinc ion per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30546
Sequence Length: 289
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
|
A1R944 | MHKHNNGLKTAALFGVLWAVLLGLGAIIAAGTRSTTPIWIMALIGVATTAYGYWNSDKIAIRSMAAYPVTEAQAPQLYQIVRELSVRANKPMPRIYLSPTMTPNAFATGRNPKNAAVCCTEGILHLLDARELRGVLGHELMHVYNRDILTSSVVAAVAGVITSVGQMLLIFGSGDRRNANPLATIAMALLAPFAASLIQMAISRTREFDADEDGAELTGDPLALASALRKIESGVSQLPLPPDQRLVNASHLMIANPFRGGGIRRMFSTHPPMKERISRLERMAGRPLL | Cofactor: Binds 1 zinc ion per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31184
Sequence Length: 289
Subcellular Location: Cell membrane
EC: 3.4.24.-
|
A1AZW2 | MTGNLRTFILMAALTALVMGMGGLIGGRGGAVIALAIAGAGNLFAWWNSDKMVLRQQGAHLVTRQQAPELVDMVAALAQRANLPMPKVYVLETEQPNAFATGRNPENAAVAVTQGIMRVLNRDELAGVIAHELAHIKHRDTLTMTVTATMAGAIAMLGNMLMFSSMFGGRDDNRGSGLAAILAMIFAPMAAGLVQMAISRTREYEADRMGAEICGRPMALAGALAKISRAAGQVVNIPAERNPASASMFIVNPLHALRMDRLFATHPPTEERIARLQAMASGAPASGPWGAR | Cofactor: Binds 1 zinc ion per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30852
Sequence Length: 292
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
|
A7HSR4 | MNTVKTGMLLAAMTALFMGLGFLIGGPKGAMIAFFIAAAMNLFAYWNSDKMVLRMYKARQVDETTAPNYVGIVRQLAQNAGIPMPATYIIDNPQPNAFATGRDPEHAAVAATTGLIKMLTPEELAGVMAHELSHIKNRDTLIMTVTATIAGAISMLANFALFFGGNRNNAGGLIGTLALAILAPMAAALVQMAISRTREYSADAGGAEISGNPLWLASALQRIDEAARRAPNEAAEANPATAHMFIINPLNGRGRDNLFSTHPATGNRIDALRRIAETMGSRSRPWG | Cofactor: Binds 1 zinc ion per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30512
Sequence Length: 287
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
|
B2T1K8 | MFNWVKTAMLMAAITALFIVIGGMIGGSRGMTIALVIALGMNFFSYWFSDKMVLRMYNAQEVDETSAPQFYRMVRELSTRAGLPMPRVYLINEDAPNAFATGRNPEHAAVAATTGILRVLSEREMRGVMAHELSHVKHRDILISTISATMAGAISALANFAMFFGSRDENGRSTNPIAGIAVALLAPIAGALIQMAISRAREFEADRGGAQISGDPQALASALDKIHRYASGIPFPTAEQHPATAQMMIMNPLSGGGIANLFSTHPATEERIARLMEMARTGRFE | Cofactor: Binds 1 zinc ion per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30838
Sequence Length: 285
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
|
B0R4N9 | MTGPDNSLTDPSASPSTPVASLRPTAEQLLPQQRDQLHAFIERVLADHPDHIVDCCVEYYTNTLPNGTAAYGDLLALLAATSADADAFTAAVTAIQSPLLSGDGPTDGPPAQESVTAHARVVAEDMSALRGRVAADDATATGSEATADEAAAVAELIERAREMNQNMEEIDRLAAQQSDNTDNLKAEISDISSAIEQIAASATEVNDRSDEAQSLATDGYERAVAVVEQVEAIHDGVTEVRHQTATLQDHTEAIDDIVEVINDIADQTNLLALNASIEAARADAGGEGFAVVADEVKSLAEESKTQAEEIEERVENIQVE... | Function: Potentially involved in chemo- or phototactic signal transduction.
PTM: Methylated by CheR.
Sequence Mass (Da): 45015
Sequence Length: 423
Subcellular Location: Cytoplasm
|
B0R474 | MALGTYVPTAIRTSLLRKAAVVIVTIMLVLVGVGVFTTQAVSTQVTEQRDTELLTSTEQEAEALEEWIGRQRSATQYLSQDNAIQSAPQADKSEVLSTRISGLTETAAALHYVNLSTDTIRASTDAAVEGDTYTSYSIPWRGEGLSFYGGGDVITSSVFNYRGTPVMAFASKQPGSDNAVFVFHSVETRGEAFSRNIDGSYTQVVDIEGTVQIAADESAISSAYGAGRDAPVIATGLTTNSGIETRDGLLVGHAKVEGTDWVLLKHAPTSNAYALEGDVQRNIVVLIVTAVAGLGALVLVIGRDALTALTDMSDRAEAIA... | Function: Potentially involved in chemo- or phototactic signal transduction.
PTM: Methylated by CheR.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87061
Sequence Length: 816
Subcellular Location: Cell membrane
|
Q6GMI0 | MILVTLFCICALVTSLQADARLSKRYVIGGCPSHCDKSMCPTMPKDCSTGQVMDHCNCCLVCASGEGEACGGVGKLGDPVCGESLECSVTGGVSYSATVRRRGKQGVCVCKSSDPVCGSDGVSYRDICELKRVSNRAQSLQQPPVLFIQRGACGTSLHDNPNSLRYKYNFIADVVEKIAPAVVHIELYRKMVYSKREMAVASGSGFVVSDDGLIVTNAHVVANKNRVKVELKNGASYDAKIKDVDEKADIALIKIDLPNKLPVLLLGRSADLRPGEFVVAIGSPFSLQNTVTTGIVSTTQRGGKELGLRNSDMDYIQTDA... | Function: Serine protease with a variety of targets, including extracellular matrix proteins and proteoglycans. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Regulates the availability of insulin-lik... |
A9JRB3 | MRLLILCASIILVPLLCDARIIKRYVIGCPERCDKSLCPPIPPDCLAGDILDQCDCCPVCAAGEGESCGGTGKLGDPECGEGLECAVSDGVGATTTVRRRGKTGVCVCKSSEPVCGSDGVSYRNICELKRVSNRAQKLQQPPIIFIQRGACGKGHEENPDSLRHRYNFIADVVEKIAPAVVHIELFRKNVFNREVAVASGSGFVVSEDGLIVTNAHVVANKHRVKVELKTGTTYDAKIKDVDEKADIALIKIDAPMKLPVLLLGRSADLRPGEFVVAIGSPFSLQNTVTTGIVSTTQRGGKELGLRNSDMDYIQTDAIIN... | Function: Serine protease with a variety of targets, including extracellular matrix proteins and proteoglycans. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Regulates the availability of insulin-lik... |
B0R632 | MTIAWARRRYGVKLGLGYIATAGLLVGVGVTTNDVPSTIVAGIAGLLTLGSINAAETVASIKEIAAQTERVANGNLEQEVTSTRTDEFGSLADSIEQMRQSLRGRLNEMERTRADLEETQAEAETAREEAEQAKQEAQAAEREARELAATYQDTAKRYGETMEAAATGDLTQRVDVDTDHEAMETVGTAFNQMMDDLQATVRTVTTVADEIEAKTERMSETSADIEASAGDTVEAVSKIESQANDQRTELDSAADDVQQVSASAEEIAATIDDLASRSEDVATASDAARDSSKSALDEMSSIETEVDDAVGQVEQLRDQV... | Function: Transduces signals from the phototaxis receptor sensory rhodopsin I (SR-I) to the flagellar motor. Responds to light changes through the variation of the level of methylation.
PTM: Methylated by CheR.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56675
Sequence Length: 536
Subcellular Loc... |
Q5V5V4 | MDSNRDSPLPSFIAGSYAARLGVALSFAILVIIAAGVLTSVQASATLEEDVADDITALSETQAVQLDDWLTTSRRNVRSTSRLPVFTDGTDTEKQQRLEELRSNEELPPGVVAVHYFDTETSEIRASSNQDFIGVNAAEQGAPFATDPPQFDGPDDTHVTEPFSVSVVDHPIVAVVSPVPGDEDRALVYMIDLREKADQISSHREGSFTTVVNTDGEFVSHPNHSMIGSTAPISQMESDPLGTLEPGQRMFHETDSMLMGLTRLESHDWVVMVHSDREAAYALSDQINSDLIGLILLAVVNLGLIGVTIGGNTIASLRRL... | Function: Transduces signals from the phototaxis receptor sensory rhodopsin II (Sop2).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 82593
Sequence Length: 773
Subcellular Location: Membrane
|
B0R6B1 | MGSGLVARIRGSYGTKLTLALVVVVVLSVGVGTFVYQQTTTQLETDVRADLTGSADARADHLDAWLSNARGQTQLASRHPVLASGNDTAITRYLEGLAASDERPDGVVAAHVYNTSTTTIEASSADAFTGVNPREQGAPFATDPPSFATTSDVVVAAPFTVPAADFPVLSVLSPIPGTTDKALIYMVNVNTLTDDFGQNVAGSTTTVVSADGTYVSHPDQDRVLTGHDGPSRLLNQSRTQPAYIDANGTVTAAAPVDGAPWSVLVRAPHDRAFALGDFVASSLVGLVLITIVSLSLIGVTVGSTTVTALRQFSRRADEMA... | Function: Transduces signals from the phototaxis receptor sensory rhodopsin II (SR-II) to the flagellar motor. Responds to light changes through the variation of the level of methylation. Also acts as a chemotransducer (By similarity).
PTM: Methylated by CheR.
Location Topology: Multi-pass membrane protein
Sequence Mas... |
P42259 | MSLNVSRLLLPSRVRHSYTGKMGAVFIFVGALTVLFGAIAYGEVTAAAATGDAAAVQEAAVSAILGLIILLGINLGLVAATLGGDTAASLSTLAAKASRMGDGDLDVELETRREDEIGDLYAAFDEMRQSVRTSLEDAKNAREDAEQAQKRAEEINTELQAEAERFGEVMDRCADGDFTQRLDAETDNEAMQSIEGSFNEMMDGIEALVGRIERFADAVSEDAEAVRANAESVMEASEDVNRAVQNISDAAGDQTETVQQIALEMDDVSATTEEVAASADDIAKTARQAAETGEAGRETAETAITEMNEVESRTEQAVAS... | Function: Transduces signals from the phototaxis receptor sensory rhodopsin II (SR-II) to the flagellar motor. Responds to light changes through the variation of the level of methylation. Also acts as a chemotransducer.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56622
Sequence Length: 534
Subcel... |
B0R470 | MSIRSFAHRILRRALPGFVRRSYLAKFGVALLAVVVCISAAGGVMYLNTSEHLQQSSRTELKKAAELSSSAVDNWHDERTNNARMLAQYGVFDNDNATEVQQFFTDEQHHLPSDVRDIHYVSLTDARVITSTDAGLRNASFGSEAAPWSRQQLTPGDDGVFVSQPYVNDGITEVAYVARVSSTPGRRTAVVMTASLAAISSSFWDPTPHSFTQLVDGTGSVIADDSKRATRQPYVENATSPIVGARAVGFQPAAQAAKEMDQAHETAYAPVDGTPWVVTLHVPTSEAYGLASNMAENVLLILGIALAGLVFIALTLGRGT... | Function: Potentially involved in chemo- or phototactic signal transduction.
PTM: Methylated by CheR.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 82077
Sequence Length: 778
Subcellular Location: Cell membrane
|
P27650 | MKYSKITTTLAALALPSIAHAHVGLHADGTLAGLNHPFSGLDHILAMVAVGFWASTLGGKAVWIVPSAFVIVMAGGGVLGIEGIALPMVETAIALTVAMLGLLVAFEVKIPTPVAAIVVGICALFHGHVHGIELPTMSNATGYVAGFLAATVILHVLGIGLASLRFGKAGQVVARVAGGAVALAGAALLVG | Function: Needed for full hydrogenase activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19022
Sequence Length: 191
Subcellular Location: Cell inner membrane
|
Q4A173 | MTLQLNGEMLTINDIKTFLNKEDTVEVTQEALERVKKSRQTVEHIIENKETIYGITTGFGLFSDVRIDKDEYNQLQVNLIRSHACGVGKPFSEEVALVMMVLRLNTLLKGHSGTTVALVEQLVYYINNRIVPVIPQQGSLGASGDLAPLSHLALALIGEGNVFFKGEEVDSRYVLNQLNRNPIQLQAKEGLALINGTQAMTAQGVINYIEAEALGYQAEWIAALTHQALNGITDAYNEKVHKARNFQEQIDVAARMLDWLDGSELTTTQGDIRVQDAYTLRCIPQIHGASFQVFNYVKEKLEFEMNAANDNPLIFDEGDE... | PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.
Catalytic Activity: L-histidine = NH4(+) + trans-urocanate
Sequence Mass (Da): 55479
Sequence Length: 499
Pathway: Amino-acid degradation; L-histidine degradation in... |
P24221 | MHTVVVGTSGTTAEDVVAVARHGARVELSAAAVEALAAARLIVDALAAKPEPVYGVSTGFGALASRHIGTELRAQLQRNIVRSHAAGMGPRVEREVVRALMFLRLKTVASGHTGVRPEVAQTMADVLNAGITPVVHEYGSLGCSGDLAPLSHCALTLMGEGEAEGPDGTVRPAGELLAAHGIAPVELREKEGLALLNGTDGMLGMLVMALADLRNLYTSADITAALSLEALLGTDKVLAPELHAIRPHPGQGVSADNMSRVLAGSGLTGHHQDDAPRVQDAYSVRCAPQVNGAGRDTLDHAALVAGRELASSVDNPVVLP... | PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Cys-Ser-Gly.
Catalytic Activity: L-histidine = NH4(+) + trans-urocanate
Sequence Mass (Da): 53111
Sequence Length: 514
Pathway: Amino-acid degradation; L-histidine degradation in... |
A3CL24 | MTHVINLDGEHLTLEDVIAVARHGATCEIDQEAKKAVEASRKIVDDIVREKRVVYGVTTGFGSLCNVSISPEDTTQLQENLIRTHSSGYGDPLPEDAVRAIMLIRINSLVKGYSGIRLSTVEKLLELLNKGVVPYIPEKGSLGASGDLAPLAHMVLPMLGLGRAYYQGQLLSGQEALDKAGIEKIALAAKEGLALINGTTVLTGIGALATYDAIQLLKLSDVAGALSMEVHNGITSPFEEDLHTIRPQSGQLATARNIRNLLEGSGNTTVATQQRVQDPYTLRCIPQIHGASKDSIAYVKTKVEIEINSVTDNPIITKEG... | PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.
Catalytic Activity: L-histidine = NH4(+) + trans-urocanate
Sequence Mass (Da): 55643
Sequence Length: 513
Pathway: Amino-acid degradation; L-histidine degradation in... |
Q67JH4 | MEAVELGAHLTLPEVVAVARHGARVVLTPEVRQRVARASEMVERLVRERRPVYGITTGFGKFSDVPISAEQTEALQRNLLMSHACAVGEPLAAEVVRAMLLLRAQALSRGHSGIRAETLEMLVAFLNLGLTPVVPEQGSLGASGDLAPLAHMSLPLIGLGEAVVNGERLSGAEALQRVGLRPLTLTAKEGLALINGTQAMTALGSLGLHDAQVLLKTADIAAAMTAEALGAIPAAWDPRVQALRLHTGQQAAARNLRRLTEGSRLTTRPGQMRTQDPYTLRCLPQVHGASRTAIEHVAQVLDWEMNAVTDNPLLFPDDDE... | PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.
Catalytic Activity: L-histidine = NH4(+) + trans-urocanate
Sequence Mass (Da): 53709
Sequence Length: 507
Pathway: Amino-acid degradation; L-histidine degradation in... |
Q9HLI6 | MIEIDGRSLRVEDVYAVAVEYDRVSISDDTLKAVEEKHEAFLKLINSGKTVYGVNTGFGSLLNVHIERDQEIELQKNLIRSHSSGVGDYLENRYVRAIMAVRLNSLAAGYSAVSADLLNMMVEMLNRDVIPAVPKYGSVGASGDLAPLAHIGLAMMGEGKAFFEGRLMDSARALEKAGLKPYQFKEKEGVALINGTSFMSGILSIAVMDAHDILENAIRSALLSFEALGGTSKAFTPWILGARPHLGQVAIGNRFREYLTGSDIVKRADSVKVQDAYTLRCIPQVYGSVADVIDYVENVLSVEINSATDNPLFNGEEVVS... | PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.
Catalytic Activity: L-histidine = NH4(+) + trans-urocanate
Sequence Mass (Da): 54149
Sequence Length: 496
Pathway: Amino-acid degradation; L-histidine degradation in... |
Q73Q56 | MKVKPVTVTGSSLTIEDVVAVARHGAEVKLSADAKKRIKDSKKIVDDIVKSGKPTYGISTGFGELSTVTITKDQNGALQRNLILSHACGVGNPFPEDIVRAIMLLRLNTHASGFSGVTPSVPDILVDMLNKGVIPYVPEKGSLGASGDLANLAHIALVMIGEGKAYYEGKLMEGKAALAKAGLKPVVLSGKDGLGIINGTPVMSGIGALALHDAEQLLKAANMGASLVFEAFRGITAALDPRIHKSRPHKGQIDTAAFILKMLKGSSSINTRENDVQDPYTLRCVPQVHGASADAIAYVRKVLEIEINAVTDNPLVFPDN... | PTM: Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly.
Catalytic Activity: L-histidine = NH4(+) + trans-urocanate
Sequence Mass (Da): 54038
Sequence Length: 507
Pathway: Amino-acid degradation; L-histidine degradation in... |
Q6L2W1 | MIIKNAGQIITFDSEGNFKLIKDKSIVIENNIISDITDNKNNDDAIDASNMVVMPGFIDSHTHLAYAGTRENELYMRSHGQSYLDILNLGGGIHKTMNDTESSGEDKIFNETIKRVDESILNGTTYLEIKSGYGKTINGERRLINAIKRIKSIYRNVKITLLAHAVPDNINEYDYAGYFINNMIPAFKNDVDFLDVFCDAGAFSRKSTEMILEAGVSSRLKLKIHADELKNIGCIDLCKRFNFTSVDHLLNTRNDQLNYIKDSGAVATILPVTAFSLDSDYVNAQRFINKKIDVAIASDASPASYNSNMIFAIYLAVRYC... | Cofactor: Binds 1 zinc or iron ion per subunit.
Function: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
Catalytic Activity: 4-imidazolone-5-propanoate + H2O = N-formimidoy... |
Q9HU91 | MKRLWQHCHAATLKGGKYSIVEDAALVTDGPLIHWIGPRAELPPGDYAERIDLGGAWLTPGLIDCHTHAVFGGNRSGEFEQRLEGVSYAEIAAAGGGIASTVRATREASEEELLASARKRLEPLLRDGVTALEIKSGYGLDLASERKMLRVIRRLGERLPATVRSTCLAAHALPPEYAGRADDYIEHICSTMLPALAGEGLVDAVDAFCEHLAFSPAQVERVFIAARELGLPVKLHAEQLSSLHGSSLAARYRALSADHLEYMTEDDARAMGEAGTVAVLLPGAFYLLRETQLPPIDALRRHGVAMAIASDLNPGTSPAL... | Cofactor: Binds 1 zinc or iron ion per subunit.
Function: Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
Catalytic Activity: 4-imidazolone-5-propanoate + H2O = N-formimidoy... |
P25503 | MTDVKKSIRANRGTELECLGWEQEAVLRMLRNNLDPEVAEKPEDLIVYGGIGKAARDWDAFHAIEHSLKTLKNDETLLVQSGKPVGMFRTHPQAPRVLLANSVLVPKWADWEHFHELEKKGLMMYGQMTAGSWIYIGSQGILQGTYETFAELARQHFGGSLKGTLTLTAGLGGMGGAQPLSVTMNEGVVIAVEVDEKRIDKRIETKYCDRKTASIEEALAWAEEAKLAGKPLSIALLGNAAEVHHTLLNRGVKIDIVTDQTSAHDPLIGYVPEGYSLDEADRLRQDTPELYVRLAKQSMKKHVEAMLAFQQKGSIVFDYG... | Cofactor: Binds 1 NAD(+) per subunit.
Function: Catalyzes the conversion of urocanate to 4-imidazolone-5-propionate.
Catalytic Activity: 4-imidazolone-5-propanoate = H2O + trans-urocanate
Sequence Mass (Da): 60600
Sequence Length: 552
Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimid... |
Q1JV40 | MEGDNCNKSRHKSHNMINPNYASVRCTQPLPSVIQLRSRNKMIGITEDPSSDSEPVSSNQPLLLTNLSYEVHTFNDNNNHERPAPQEQSTQNTMISMQSEQKSDRFTASNLGMFQYMKFEIGEDGDDHEEEAILTNREKLRHILHSKPIHVAIIVLVVLDSFLVVGELLIDLKVIIVPHGNPAPEILHGFSLSILSIFMVEIALKIIADHRHFIHHKVEVLDAVVVVISFGVDIALIFVGESEALAAIGLLVILRLWRVFRIINGIIVTVKTKADDRVHEIKKKNSELELQIHNLEEKLSQKEQDMSRLHEILRCNNIDI... | Function: Mediates the voltage-dependent proton permeability of excitable membranes. Forms a proton-selective channel through which protons may pass in accordance with their electrochemical gradient (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38501
Sequence Length: 342
Domain: Th... |
Q6DHQ1 | MSRYLKHFTAVGDNKSAVPTWHEEDTSHHVTTLHDAPDGLEVSTGQHLGQLSFRDSLRKLYSTERFQIVVVCLVVLDAIFVLCELLIDLSIIEADHHRIAPQVFHYLSLALLTFFMVELAGKIFAYRLEFLHHKFEVFDGIVVVVSFILDIIYISKEDAFDAMGLLILLRLWRVARIINGILVSVQNRANHRVEKLKEINESLVHQVNELKEQNTKMDQENVRLRALLKDHSIDF | Function: Mediates the voltage-dependent proton permeability of excitable membranes. Forms a proton-selective channel through which protons may pass in accordance with their electrochemical gradient (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27110
Sequence Length: 235
Domain: Th... |
Q96D96 | MATWDEKAVTRRAKVAPAERMSKFLRHFTVVGDDYHAWNINYKKWENEEEEEEEEQPPPTPVSGEEGRAAAPDVAPAPGPAPRAPLDFRGMLRKLFSSHRFQVIIICLVVLDALLVLAELILDLKIIQPDKNNYAAMVFHYMSITILVFFMMEIIFKLFVFRLEFFHHKFEILDAVVVVVSFILDIVLLFQEHQFEALGLLILLRLWRVARIINGIIISVKTRSERQLLRLKQMNVQLAAKIQHLEFSCSEKEQEIERLNKLLRQHGLLGEVN | Function: Mediates the voltage-dependent proton permeability of excitable membranes. Forms a proton-selective channel through which protons may pass in accordance with their electrochemical gradient. Proton efflux, accompanied by membrane depolarization, facilitates acute production of reactive oxygen species in phagoc... |
Q3U2S8 | MTSHDPKAVTRRTKVAPTKRMSRFLKHFTVVGDDYHTWNVNYKKWENEEEEEEPAPTSAEGEGNAEGPDAEAGSASTPRQSLDFRSRLRKLFSSHRFQVIIICLVVLDALLVLAELLLDLKIIEPDEQDYAVTAFHYMSFAILVFFMLEIFFKIFVFRLEFFHHKFEILDAFVVVVSFVLDLVLLFKSHHFEALGLLILLRLWRVARIINGIIISVKTRSERQILRLKQINIQLATKIQHLEFSCSEKEQEIERLNKLLKQNGLLGDVN | Function: Mediates the voltage-dependent proton permeability of excitable membranes. Forms a proton-selective channel through which protons may pass in accordance with their electrochemical gradient. Proton efflux, accompanied by membrane depolarization, facilitates acute production of reactive oxygen species in phagoc... |
Q5M8L8 | MAGCLRHFTSVGDDTKKKAWKEEDVEVAHEEEPKNTPHPFIASYSFRGALKWLFSSHKFQIVIICLVILDALFVLVEVLLDLELLAEKVDHIIPEIFHYLSISVLSFFILEIAGKLYAFRLEFFHHKFEVFDAAIVVISFIIDIVYISREDIFNAVGLLILLRLWRVARIVNGIIVSVKTQAEDKIHRLKENQESLLEKVAHLEQQCAQQEQEIVRLQTLLQQHNVFPAS | Function: Mediates the voltage-dependent proton permeability of excitable membranes. Forms a proton-selective channel through which protons may pass in accordance with their electrochemical gradient (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26575
Sequence Length: 230
Domain: Th... |
Q12891 | MRAGPGPTVTLALVLAVSWAMELKPTAPPIFTGRPFVVAWDVPTQDCGPRLKVPLDLNAFDVQASPNEGFVNQNITIFYRDRLGLYPRFDSAGRSVHGGVPQNVSLWAHRKMLQKRVEHYIRTQESAGLAVIDWEDWRPVWVRNWQDKDVYRRLSRQLVASRHPDWPPDRIVKQAQYEFEFAAQQFMLETLRYVKAVRPRHLWGFYLFPDCYNHDYVQNWESYTGRCPDVEVARNDQLAWLWAESTALFPSVYLDETLASSRHGRNFVSFRVQEALRVARTHHANHALPVYVFTRPTYSRRLTGLSEMDLISTIGESAAL... | Function: Hydrolyzes high molecular weight hyaluronic acid to produce an intermediate-sized product which is further hydrolyzed by sperm hyaluronidase to give small oligosaccharides. Displays very low levels of activity. Associates with and negatively regulates MST1R.
Catalytic Activity: Random hydrolysis of (1->4)-lin... |
O35632 | MRAGLGPIITLALVLEVAWAGELKPTAPPIFTGRPFVVAWNVPTQECAPRHKVPLDLRAFDVKATPNEGFFNQNITTFYYDRLGLYPRFDAAGTSVHGGVPQNGSLCAHLPMLKESVERYIQTQEPGGLAVIDWEEWRPVWVRNWQEKDVYRQSSRQLVASRHPDWPSDRVMKQAQYEFEFAARQFMLNTLRYVKAVRPQHLWGFYLFPDCYNHDYVQNWESYTGRCPDVEVARNDQLAWLWAESTALFPSVYLDETLASSVHSRNFVSFRVREALRVAHTHHANHALPVYVFTRPTYTRGLTGLSQVDLISTIGESAAL... | Function: Hydrolyzes high molecular weight hyaluronic acid to produce an intermediate-sized product which is further hydrolyzed by sperm hyaluronidase to give small oligosaccharides. Displays very low levels of activity. Associates with and negatively regulates MST1R (By similarity).
Catalytic Activity: Random hydrolys... |
Q8SQG7 | MWTGLGPAVTLALVLVVAWATELKPTAPPIFTGRPFVVAWDVPTQDCGPRHKMPLDPKDMKAFDVQASPNEGFVNQNITIFYRDRLGMYPHFNSVGRSVHGGVPQNGSLWVHLEMLKGHVEHYIRTQEPAGLAVIDWEDWRPVWVRNWQDKDVYRRLSRQLVASHHPDWPPERIVKEAQYEFEFAARQFMLETLRFVKAFRPRHLWGFYLFPDCYNHDYVQNWETYTGRCPDVEVSRNDQLSWLWAESTALFPSVYLEETLASSTHGRNFVSFRVQEALRVADVHHANHALPVYVFTRPTYSRGLTGLSEMDLISTIGES... | Function: Hydrolyzes high molecular weight hyaluronic acid to produce an intermediate-sized product which is further hydrolyzed by sperm hyaluronidase to give small oligosaccharides. Displays very low levels of activity. Associates with and negatively regulates MST1R (By similarity).
Catalytic Activity: Random hydrolys... |
O43820 | MTTQLGPALVLGVALCLGCGQPLPQVPERPFSVLWNVPSAHCEARFGVHLPLNALGIIANRGQHFHGQNMTIFYKNQLGLYPYFGPRGTAHNGGIPQALPLDRHLALAAYQIHHSLRPGFAGPAVLDWEEWCPLWAGNWGRRRAYQAASWAWAQQVFPDLDPQEQLYKAYTGFEQAARALMEDTLRVAQALRPHGLWGFYHYPACGNGWHSMASNYTGRCHAATLARNTQLHWLWAASSALFPSIYLPPRLPPAHHQAFVRHRLEEAFRVALVGHRHPLPVLAYVRLTHRRSGRFLSQDDLVQSIGVSAALGAAGVVLWG... | Function: Facilitates sperm penetration into the layer of cumulus cells surrounding the egg by digesting hyaluronic acid. Involved in induction of the acrosome reaction in the sperm. Involved in follicular atresia, the breakdown of immature ovarian follicles that are not selected to ovulate. Induces ovarian granulosa c... |
Q8VEI3 | MIMHLGLMMVVGLTLCLMHGQALLQVPEHPFSVVWNVPSARCKAHFGVHLPLDALGIVANHGQHFHGQNISIFYKNQFGLYPYFGPRGTAHNGGIPQAVSLDHHLARAAHQILHSLGSSFAGLAVLDWEEWYPLWAGNWGPHRQVYLAASWVWTQQMFPGLDPQEQLHKAHTSFEQAARALMEYTLQLGRTLRPSGLWGFYRYPACGNGWHKMASNYTGHCHAAITTRNTQLRWLWAASSALFPSIYLPPRLPLAYRQAFVRHRLEEAFRVALLEHSHPLPVLAYSRLTHRSSGRFLSLDDLMQTIGVSAALGTAGVVLW... | Function: Facilitates sperm penetration into the layer of cumulus cells surrounding the egg by digesting hyaluronic acid. Involved in induction of the acrosome reaction in the sperm . Involved in follicular atresia, the breakdown of immature ovarian follicles that are not selected to ovulate. Induces ovarian granulosa ... |
Q6RHW2 | MTMQLGLALVLGVAMCLGCGQPLLRAPERPFCVLWNVPSARCKARFGVHLPLEALGITANHGQRFHGQNITIFYKSQLGLYPYFGPRGTAHNGGIPQAVSLDHHLARAAYQIHRSLRPGFTGLAVLDWEEWCPLWAGNWGRRQAYQAASCAWAQRVYPNLDPQEQLCKARAGFEEAARALMEDTLRLGRMLRPHGLWGFYHYPACGNGWHGTASNYTGHCHAAALARNTQLYWLWAASSALFPSIYLPPGLPPAYHQAFVRYRLEEAFRVALVGHPHPLPVLAYARLTHRNSGRFLSQDELVQTIGVSAALGASGVVLWG... | Function: Facilitates sperm penetration into the layer of cumulus cells surrounding the egg by digesting hyaluronic acid. Involved in induction of the acrosome reaction in the sperm. Involved in follicular atresia, the breakdown of immature ovarian follicles that are not selected to ovulate. Induces ovarian granulosa c... |
Q2M3T9 | MKVLSEGQLKLCVVQPVHLTSWLLIFFILKSISCLKPARLPIYQRKPFIAAWNAPTDQCLIKYNLRLNLKMFPVIGSPLAKARGQNVTIFYVNRLGYYPWYTSQGVPINGGLPQNISLQVHLEKADQDINYYIPAEDFSGLAVIDWEYWRPQWARNWNSKDVYRQKSRKLISDMGKNVSATDIEYLAKVTFEESAKAFMKETIKLGIKSRPKGLWGYYLYPDCHNYNVYAPNYSGSCPEDEVLRNNELSWLWNSSAALYPSIGVWKSLGDSENILRFSKFRVHESMRISTMTSHDYALPVFVYTRLGYRDEPLFFLSKQD... | Function: Endo-hyaluronidase that degrades hyaluronan to smaller oligosaccharide fragments. Has also chondroitin sulfate hydrolase activity, The best substrate being the galactosaminidic linkage in the sequence of a trisulfated tetrasaccharide.
Catalytic Activity: Random hydrolysis of (1->4)-linkages between N-acetyl-b... |
Q812F3 | MRVLYFKHSFFRSLLKSNGLPQTLLVFLLIPCYLTVDFRAPPLIPDVPFLWAWNAPTESCFTRFNQPLDLGLFSLVGSPRKSATGQPVTIFYSDRLGLYPYIDDSQLIFNGGLPQLVSLKSHLEVAKTDILHYMPIDNVGLAVIDWEEWRPTWARNWKPKDIYRNKSIELVQQQNILLNFTEAVKWAKEEFEEAARHFMEETLRLGKSLRPNHLWGFYLFPDCYNNKFQVADYKGECPDIEKHRNDALFWIWEESTALYPSIYLKSSLKSSPQAALYVRNRVQEAIRVSKVKDPRNPLPIFVYFRIVFTDLTYQYLYEDD... | Function: Catalyzes the hydrolysis of hyaluronan into smaller oligosaccharide fragments . Does not appear to be essential for fertilization .
Catalytic Activity: Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.
Location Topology: Lipid-anchor
Sequence M... |
P23613 | MGAFTFKHSFFGSFVECSGVLQTVFIFLLIPCCLADKRAPPLIPNVPLLWVWNAPTEFCIGGTNQPLDMSFFSIVGTPRKNITGQSITLYYVDRLGYYPYIDPHTGAIVHGGLPQLMNLQQHLRKSRQDILFYMPTDSVGLAVIDWEEWRPTWTRNWRPKDIYRNKSIELVKSQHPQYNHSYAVAVAKRDFERTGKAFMLETLKLGKSLRPSSLWGYYLFPDCYNTHFTKPNYDGHCPPIELQRNNDLQWLWNDSTALYPSVYLTSRVRSSQNGALYVRNRVHESIRVSKLMDDKNPLPIYVYIRLVFTDQTTTFLELDD... | Function: Involved in sperm-egg adhesion. Upon fertilization sperm must first penetrate a layer of cumulus cells that surrounds the egg before reaching the zona pellucida. The cumulus cells are embedded in a matrix containing hyaluronic acid which is formed prior to ovulation. This protein aids in penetrating the layer... |
P38567 | MGVLKFKHIFFRSFVKSSGVSQIVFTFLLIPCCLTLNFRAPPVIPNVPFLWAWNAPSEFCLGKFDEPLDMSLFSFIGSPRINATGQGVTIFYVDRLGYYPYIDSITGVTVNGGIPQKISLQDHLDKAKKDITFYMPVDNLGMAVIDWEEWRPTWARNWKPKDVYKNRSIELVQQQNVQLSLTEATEKAKQEFEKAGKDFLVETIKLGKLLRPNHLWGYYLFPDCYNHHYKKPGYNGSCFNVEIKRNDDLSWLWNESTALYPSIYLNTQQSPVAATLYVRNRVREAIRVSKIPDAKSPLPVFAYTRIVFTDQVLKFLSQDE... | Function: Involved in sperm-egg adhesion. Upon fertilization sperm must first penetrate a layer of cumulus cells that surrounds the egg before reaching the zona pellucida. The cumulus cells are embedded in a matrix containing hyaluronic acid which is formed prior to ovulation. This protein aids in penetrating the layer... |
P38568 | MGVLKFKHIFFRSFVKSSGVSQIVFTFLLIPCCLTLNFRAPPIIPNVPFLWAWNAPSEFCLGKFNEPLDMSLFTLMGSPRINVTGQGVTIFYVDRLGYYPYIDLTTGVTVHGGIPQKVSLQDHLDKSKQDILFYMPVDNLGMAVIDWEEWRPTWARNWKPKDVYKNRSIELVQQQNVQLSLPQATDKAKQEFEKAGKDFMLETIKLGRSLRPNHLWGYYLFPDCYNHHYRKPGYNGSCFDVEIKRNDDLSWLWNESTALYPSIYLNTQQSVVVATLYVRNRVREAIRVSKIPDAKNPLPVFVYARLVFTDQVLKFLSREE... | Function: Involved in sperm-egg adhesion. Upon fertilization sperm must first penetrate a layer of cumulus cells that surrounds the egg before reaching the zona pellucida. The cumulus cells are embedded in a matrix containing hyaluronic acid which is formed prior to ovulation. This protein aids in penetrating the layer... |
P48794 | MGELRFKHLFWGSFVESGGTFQTVLIFLLIPCSLTVDYRAAPILSNTTFLWIWNVPTERCVGNVNDPIDLSFFSLIGSPRKTATGQPVTLFYVDRLGLYPHIDANQAEHYGGIPQRGDYQAHLRKAKTDIEHYIPDDKLGLAIIDWEEWRPTWLRNWKPKDNYRNKSIELVQSTNPGLSITEATQKAIQQFEEAGRKFMEGTLHLGKFLRPNQLWGYYLFPDCYNNKFQDPKYDGQCPAVEKKRNDNLKWLWKASTGLYPSVYLKKDLKSNRQATLYVRYRVVEAIRVSKVGNASDPVPIFVYIRLVFTDRTSEYLLEDD... | Function: Involved in sperm-egg adhesion. Upon fertilization sperm must first penetrate a layer of cumulus cells that surrounds the egg before reaching the zona pellucida. The cumulus cells are embedded in a matrix containing hyaluronic acid which is formed prior to ovulation. This protein aids in penetrating the layer... |
P52754 | MKFFAIAALFAAAAVAQPLEDRSNGNGNVCPPGLFSNPQCCATQVLGLIGLDCKVPSQNVYDGTDFRNVCAKTGAQPLCCVAPVAGQALLCQTAVGA | Function: Contributes to surface hydrophobicity, which is important for processes such as association of hyphae in reproductive structures, dispersal of aerial spores and adhesion of pathogens to host structures.
PTM: Four disulfide bonds may be present.
Sequence Mass (Da): 9874
Sequence Length: 97
Subcellular Location... |
P79073 | MQFFAVALFATSALAAVCPTGLFSNPLCCATNVLDLIGVDCKTPTIAVDTGAIFQAHCASKGSKPLCCVAPVADQALLCQKAIGTF | Function: Responsible for spore hydrophobicity and protection.
PTM: Four disulfide bonds may be present.
Sequence Mass (Da): 8766
Sequence Length: 86
Subcellular Location: Spore wall
|
M9PFN0 | MDATSIITQVSRDDEQLNVYPSYPNDKDAWLGFSGSVWLPDCPADHAQLTHDVDRLKPQKRGLFHSLLCCWRRNRTKTNQNGTQIDGSTTPPPLPDQQRYLLPQVRLTDMHRKCMVIDLDETLVHSSFKPIPNADFIVPVEIDGTVHQVYVLKRPHVDEFLQKMGELYECVLFTASLAKYADPVADLLDKWNVFRARLFRESCVYYRGNYIKDLNRLGRDLQKIVIVDNSPASYIFHPDNAVPVKSWFDDVTDCELRELIPLFEKLSKVDSVYSVLCNSNQPLNNQTNQQQHPQELQQAPNQLHQQLQQQQQQQTISATT... | Function: Prion-like membrane-associated phosphatase . Phosphatase activity depends on amyloid-like assembly at the membrane . Might have a role in establishment of segment polarity in embryos .
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Location Topology: Peripheral membrane ... |
Q1Q0T2 | MGKRKLGVIASAFVAGALVCGSTLVNAEPVMTGGPVQGKALWTDYSGMSKEVQGPVSQILFTQSPRTAKGDPYQNYPHYIPEGSRIVLFDLNTKELKVLTNDFATAFDPCTYWDGKKFAFAGVHKKGGGCQIWEMNIDGSGLRQMTDLKGTCRSPIYYAAGSIEEGEGRIIWRDRYFEGDWKEHGMVEKTGMIIFSGSPEGVMDEFHNPYAYNLYRLDTQGGKIIQRITGHVLSGIEFPHLNTTIDQITYNLSSNFDPWLTPDGNILFSSVQANGSRAGGEGRVMICVDNWDGAYPRPIYGNCDGEIGGTSGRSQAKITF... | Cofactor: Binds two heme c groups per subunit.
Function: Component of the hydrazine synthase complex that catalyzes the condensation of nitric oxide (NO) with ammonium to form hydrazine . The alpha subunit catalyzes the second half-reaction, i.e. the condensation of hydroxylamine formed in the active site of the gamma ... |
Q1Q0T4 | MVIRRKMNKMIRKGMIGAVMLGAAVAISGGVATAGYIQGTHVKTDLPGPFHITMSPDGSTLFISNQSGHSVTFVDARTQKVTGEVAVRVQPEASAVTPDGAFLYVCNAESDSVSVVDIQRKQEIKEIKVGDWPSGIKISPDGKTAYVACSGCMWNAIDVIDTGRMEKVRSIYTSDYGPRMVEISPDGKTLVAILDTVGSINRSVDFIDIASGRVVENRVIHESSNLRDVVYTPDGKYIAVTHQTPKNWLPVCEAENGQVFTNNVTIIETKAGGKVARLPLDDLNNYDGNPYGMAMDPKGKYLYIGVRGMHRVTILDMDKV... | Function: Component of the hydrazine synthase complex that catalyzes the condensation of nitric oxide (NO) with ammonium to form hydrazine . The beta subunit may play a role in modulating transport of the hydroxylamine intermediate through a tunnel between the gamma and alpha subunit's active site . Is involved in anae... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.