Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P03567 | REP_TGMVY | MPSHPKRFQINAKNYFLTYPQCSLSKEESLSQLQALNTPINKKFIKICRELHEDGQPHLHVLIQFEGKYCCQNQRFFDLVSPTRSAHFHPNIQRAKSSSDVKTYIDKDGDTLVWGEFQVDGRSARGGCQTSNDAAAEALNASSKEEALQIIREKIPEKYLFQFHNLNSNLDRIFDKTPEPWLPPFHVSSFTNVPDEMRQWAENYFGKSSAARPERPISIIIEGDSRTGKTMWARSLGPHNYLSGHLDLNSRVYSNKVEYNVIDDVTPQYLKLKHWKELIGAQRDWQTNCKYGKPVQIKGGIPSIVLCNPGEGASYKVFLD... | 2.7.7.-; 3.1.21.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU01364}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU01364}; Note=Divalent metal cations, possibly Mg(2+) or Mn(2+). {ECO:0000255|PROSITE-ProRule:PRU01364}; | DNA replication [GO:0006260]; rolling circle single-stranded viral DNA replication [GO:0039684] | host cell nucleus [GO:0042025] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; endodeoxyribonuclease activity, producing 5'-phosphomonoesters [GO:0016888]; helicase activity [GO:0004386]; metal ion binding [GO:0046872]; nucleotidyltransferase activity [GO:0016779]; structural molecule activity [GO:0005198] | PF00799;PF08283; | 3.40.1310.20; | Geminiviridae Rep protein family | null | SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Essential for the replication of viral ssDNA. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep binds a specific region at the genome origin of replication. It introduces an endonucleolytic nick within the conserved sequence 5'-TAATATTAC-3' in the intergenic region of the genome... | Tomato golden mosaic virus (strain Yellow vein) (TGMV) |
P03586 | RDRP_TMV | MAYTQTATTSALLDTVRGNNSLVNDLAKRRLYDTAVEEFNARDRRPKVNFSKVISEEQTLIATRAYPEFQITFYNTQNAVHSLAGGLRSLELEYLMMQIPYGSLTYDIGGNFASHLFKGRAYVHCCMPNLDVRDIMRHEGQKDSIELYLSRLERGGKTVPNFQKEAFDRYAEIPEDAVCHNTFQTMRHQPMQQSGRVYAIALHSIYDIPADEFGAALLRKNVHTCYAAFHFSENLLLEDSYVNLDEINACFSRDGDKLTFSFASESTLNYCHSYSNILKYVCKTYFPASNREVYMKEFLVTRVNTWFCKFSRIDTFLLYK... | 2.1.1.-; 2.7.7.-; 2.7.7.48; 3.6.4.13 | null | DNA-templated transcription [GO:0006351]; RNA processing [GO:0006396]; viral RNA genome replication [GO:0039694]; virus-mediated perturbation of host defense response [GO:0019049] | null | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; mRNA methyltransferase activity [GO:0008174]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968] | PF00978;PF20896;PF01443;PF01660; | 3.30.450.420;3.40.50.300; | SsRNA positive-strand viruses RNA-directed RNA polymerase family | null | null | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=ATP + H2... | null | null | null | null | FUNCTION: [Replicase large subunit]: Is an RNA-dependent RNA polymerase active in viral RNA replication. {ECO:0000269|PubMed:17634237}.; FUNCTION: [Replicase small subunit]: Is a methyltransferase active in RNA capping and an RNA helicase. Methyltransferase displays a cytoplasmic capping enzyme activity. This function ... | Tobacco mosaic virus (strain vulgare) (TMV) (Tobacco mosaic virus (strain U1)) |
P03587 | RDRP_TOML | MAYTQTATSSALLETVRGNNTLVNDLAKRRLYDTAVDEFNARDRRPKVNFSKVVSEEQTLIATKAYPEFQITFYNTQNAVHSLAGGLRSLELEYLMMQIPYGSLTYDIGGNFASHLFKGRAYVHCCMPNLDVRDIMRHEGQKDSIELYLSRLERGNKHVPNFQKEAFDRYAEMPNEVVCHDTFQTCRHSQECYTGRVYAIALHSIYDIPADEFGAALLRKNVHVCYAAFHFSENLLLEDSHVNLDEINACFQRDGDRLTFSFASESTLNYSHSYSNILKYVCKTYFPASNREVYMKEFLVTRVNTWFCKFSRIDTFLLYK... | 2.1.1.-; 2.7.7.-; 2.7.7.48; 3.6.4.13 | null | DNA-templated transcription [GO:0006351]; RNA processing [GO:0006396]; viral RNA genome replication [GO:0039694]; virus-mediated perturbation of host defense response [GO:0019049] | null | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; mRNA methyltransferase activity [GO:0008174]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968] | PF00978;PF01443;PF01660; | 3.30.450.420;3.40.50.300; | SsRNA positive-strand viruses RNA-directed RNA polymerase family | null | null | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=ATP + H2... | null | null | null | null | FUNCTION: [Replicase large subunit]: Is an RNA-dependent RNA polymerase active in viral RNA replication. {ECO:0000269|PubMed:14512550}.; FUNCTION: [Replicase small subunit]: Is a methyltransferase active in RNA capping and an RNA helicase. Methyltransferase displays a cytoplasmic capping enzyme activity. This function ... | Tomato mosaic virus (strain L) (ToMV) (TMV strain tomato) |
P03588 | 1A_BMV | MSSSIDLLKLIAEKGADSQSAQDIVDNQVAQQLSAQIEYAKRSKKINVRNKLSIEEADAFRDRYGGAFDLNLTQQYHAPHSLAGALRVAEHYDCLDSFPPEDPVIDFGGSWWHHFSRRDKRVHSCCPVLGVRDAARHEERMCRMRKILQESDDFDEVPNFCLNRAQDCDVQADWAICIHGGYDMGFQGLCDAMHSHGVRVLRGTVMFDGAMLFDREGFLPLLKCHWQRDGSGADEVIKFDFENESTLSYIHGWQDLGSFFTESVHCIDGTTYLLEREMLKCNIMTYKIIATNLRCPRETLRHCVWFEDISKYVGVSIPED... | 2.1.1.-; 3.6.4.- | null | positive stranded viral RNA replication [GO:0039690]; RNA processing [GO:0006396] | host cell cytoplasm [GO:0030430]; host cell endoplasmic reticulum membrane [GO:0044167]; membrane [GO:0016020] | ATP binding [GO:0005524]; helicase activity [GO:0004386]; hydrolase activity, acting on acid anhydrides [GO:0016817]; mRNA methyltransferase activity [GO:0008174]; RNA binding [GO:0003723] | PF12503;PF01443;PF01660; | 3.40.50.300; | Bromoviridae replication protein 1a family | null | SUBCELLULAR LOCATION: Host endoplasmic reticulum membrane {ECO:0000269|PubMed:19325881}; Peripheral membrane protein {ECO:0000269|PubMed:19325881}. | null | null | null | null | null | FUNCTION: Involved in the virus replication. Contains a helicase domain and a methyltransferase domain. The methyltransferase domain is probably involved in viral RNA capping. Involved in the formation of ER membrane spherular invaginations in which RNA replication complexes form. {ECO:0000269|PubMed:19325881}. | Brome mosaic virus (BMV) |
P03599 | POL2_CPMVS | MFSFTEAKSKISLWTRSAAPLNNVYLSYSCRCGLGKRKLAGGCCSAPYITCYDSADFRRVQYLYFCLTRYCCLYFFLLLLADWFYKKSSIFFETEFSRGFRTWRKIVKLLYILPKFEMESIMSRGIPSGILEEKAIQFKRAKEGNKPLKDEIPKPEDMYVSHTSKWNVLRKMSQKTVDLSKAAAGMGFINKHMLTGNILAQPTTVLDIPVTKDKTLAMASDFIRKENLKTSAIHIGAIEIIIQSFASPESDLMGGFLLVDSLHTDTANAIRSIFVAPMRGGRPVRVVTFPNTLAPVSCDLNNRFKLICSLPNCDIVQGSQ... | null | null | transport of virus in host, cell to cell [GO:0046740]; virus-mediated perturbation of host defense response [GO:0019049] | host cell nucleus [GO:0042025]; host cell plasmodesma [GO:0044219]; T=3 icosahedral viral capsid [GO:0039617] | DNA binding [GO:0003677]; GTP binding [GO:0005525]; RNA binding [GO:0003723]; structural molecule activity [GO:0005198] | PF02247;PF02248; | 2.60.120.20; | null | PTM: [RNA2 polyprotein]: Specific enzymatic cleavages by picornain 3C-like protease in vivo yield mature proteins. {ECO:0000269|PubMed:16789216}.; PTM: [Small capsid protein precursor]: The C-terminal 24 amino acids of the small capsid protein are specifically cleaved by the RNA1 encoded picornain 3C-like protease duri... | SUBCELLULAR LOCATION: [VP58]: Host nucleus {ECO:0000269|PubMed:8497075}.; SUBCELLULAR LOCATION: [Movement protein]: Host cell junction, host plasmodesma {ECO:0000269|PubMed:14579172, ECO:0000269|PubMed:27339685}. Note=Assembles in tubules that are embedded within modified plasmodesmata. {ECO:0000269|PubMed:10864669, EC... | null | null | null | null | null | FUNCTION: [VP58]: Responsible for viral RNA2 accumulation. May function by recruiting the RNA1-encoded polyprotein that contains the replication protein to RNA2 and enable its replication. {ECO:0000250|UniProtKB:P23009}.; FUNCTION: [Movement protein]: Transports the viral genome to neighboring plant cells directly thro... | Cowpea mosaic virus (strain SB) (CPMV) |
P03600 | POL1_CPMVS | MGLPEYEADSEALLSQLTIEFTPGMTVSSLLAQVTTNDFHSAIEFFAAEKAVDIEGVHYNAYMQQIRKNPSLLRISVVAYAFHVSDMVAETMSYDVYEFLYKHYALFISNLVTRTLRFKELLLFCKQQFLEKMQASIVWAPELEQYLQVEGDAVAQGVSQLLYKMVTWVPTFVRGAVDWSVDAILVSFRKHFEKMVQEYVPMAHRVCSWLSQLWDKIVQWISQASETMGWFLDGCRDLMTWGIATLATCSALSLVEKLLVAMGFLVEPFGLSGIFLRTGVVAAACYNYGTNSKGFAEMMALLSLAANCVSTVIVGGFFPG... | 2.7.7.48; 3.4.22.-; 3.6.4.- | null | DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; viral RNA genome replication [GO:0039694] | host cell endoplasmic reticulum [GO:0044165]; host cell membrane [GO:0033644]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968] | PF00548;PF00680;PF00910; | 3.30.70.270;2.40.10.10; | null | PTM: [RNA1 polyprotein]: Specific enzymatic cleavages by picornain 3C-like protease in vivo yield mature proteins (PubMed:1431806, PubMed:16789216, PubMed:16789257, PubMed:7964626). Picornain 3C-like protease is autocatalytically processed. {ECO:0000269|PubMed:1431806, ECO:0000269|PubMed:16789216, ECO:0000269|PubMed:16... | SUBCELLULAR LOCATION: [Putative helicase]: Host membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:12021362}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host endoplasmic reticulum {ECO:0000269|PubMed:10864669}.; SUBCELLULAR LOCATION... | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; | null | null | null | null | FUNCTION: [Picornain 3C-like protease]: Thiol protease that cleaves the RNA1 and RNA2 polyproteins. {ECO:0000269|PubMed:16453750, ECO:0000269|PubMed:16789216, ECO:0000269|PubMed:8811039}.; FUNCTION: [Viral genome-linked protein]: Plays a role in RNA replication. It is covalently linked to the 5'terminus of both viral s... | Cowpea mosaic virus (strain SB) (CPMV) |
P03607 | CAPSD_SCPMV | MSGLFHHRTKPREIRAFVMATRLTKKQLAQAIQNTLPNPPRRKRRAKRRAAQVPKPTQAGVSMAPIAQGTMVKLRPPMLRSSMDVTILSHCELSTELAVTVTIVVTSELVMPFTVGTWLRGVAQNWSKYAWVAIRYTYLPSCPTTTSGAIHMGFQYDMADTLPVSVNQLSNLKGYVTGPVWEGQSGLCFVNNTKCPDTSRAITIALDTNEVSEKRYPFKTATDYATAVGVNANIGNILVPARLVTAMEGGSSKTAVNTGRLYASYTIRLIEPIAAALNL | null | null | null | T=3 icosahedral viral capsid [GO:0039617] | calcium ion binding [GO:0005509]; lipid binding [GO:0008289]; RNA binding [GO:0003723]; structural constituent of virion [GO:0039660] | PF00729; | 2.60.120.20; | Icosahedral plant coat protein family | null | SUBCELLULAR LOCATION: Virion {ECO:0000305}. | null | null | null | null | null | null | Southern cowpea mosaic virus (SCPMV) (Southern bean mosaic virus (strain cowpea)) |
P03612 | CAPSD_BPMS2 | MASNFTQFVLVDNGGTGDVTVAPSNFANGVAEWISSNSRSQAYKVTCSVRQSSAQNRKYTIKVEVPKVATQTVGGVELPVAAWRSYLNMELTIPIFATNSDCELIVKAMQGLLKDGNPIPSAIAANSGIY | null | null | negative regulation of viral translation [GO:1904972]; regulation of translation [GO:0006417] | T=3 icosahedral viral capsid [GO:0039617] | identical protein binding [GO:0042802]; RNA binding [GO:0003723]; structural molecule activity [GO:0005198] | PF01819; | 3.30.380.10; | Leviviricetes capsid protein family | null | SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:8254664}. Note=The shell is composed of 178 copies of the capsid protein and 1 copy of the maturation protein. {ECO:0000269|PubMed:23810697, ECO:0000305|PubMed:8254664}. | null | null | null | null | null | FUNCTION: Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins) (PubMed:18662904, PubMed:8254664). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the m... | Escherichia phage MS2 (Bacteriophage MS2) |
P03615 | CAPSD_BPQBE | MAKLETVTLGNIGKDGKQTLVLNPRGVNPTNGVASLSQAGAVPALEKRVTVSVSQPSRNRKNYKVQVKIQNPTACTANGSCDPSVTRQAYADVTFSFTQYSTDEERAFVRTELAALLASPLLIDAIDQLNPAY | null | null | null | T=3 icosahedral viral capsid [GO:0039617] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; translation repressor activity [GO:0030371] | PF01819; | 3.30.380.10; | Leviviricetes capsid protein family | null | SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:27671640, ECO:0000269|PubMed:29078304}. Note=The shell is composed of 89 dimers of the capsid protein, one of them being sequestered inside the virion, and 1 copy of the maturation protein. {ECO:0000269|PubMed:27671640, ECO:0000269|PubMed:29078304}. | null | null | null | null | null | FUNCTION: Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins) (PubMed:19913556, PubMed:27671640). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the ... | Escherichia virus Qbeta (Bacteriophage Q-beta) |
P03630 | CAPSD_BPPP7 | MSKTIVLSVGEATRTLTEIQSTADRQIFEEKVGPLVGRLRLTASLRQNGAKTAYRVNLKLDQADVVDCSTSVCGELPKVRYTQVWSHDVTIVANSTEASRKSLYDLTKSLVATSQVEDLVVNLVPLGR | null | null | regulation of translation [GO:0006417] | T=3 icosahedral viral capsid [GO:0039617] | identical protein binding [GO:0042802]; RNA binding [GO:0003723] | PF09063; | 3.30.380.10; | Leviviricetes capsid protein family | null | SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:109813}. Note=The shell is composed of 178 copies of the capsid protein and 1 copy of the maturation protein. {ECO:0000250|UniProtKB:P03612}. | null | null | null | null | null | FUNCTION: Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins) (PubMed:10739912). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packagin... | Pseudomonas phage PP7 (Bacteriophage PP7) |
P03631 | REPA_BPPHS | MVRSYYPSECHADYFDFERIEALKPAIEACGISTLSQSPMLGFHKQMDNRIKLLEEILSFRMQGVEFDNGDMYVDGHKAASDVRDEFVSVTEKLMDELAQCYNVLPQLDINNTIDHRPEGDEKWFLENEKTVTQFCRKLAAERPLKDIRDEYNYPKKKGIKDECSRLLEASTMKSRRGFAIQRLMNAMRQAHADGWFIVFDTLTLADDRLEAFYDNPNALRDYFRDIGRMVLAAEGRKANDSHADCYQYFCVPEYGTANGRLHFHAVHFMRTLPTGSVDPNFGRRVRNRRQLNSLQNTWPYGYSMPIAVRYTQDAFSRSG... | 3.1.21.-; 6.5.1.1 | null | DNA replication [GO:0006260]; rolling circle single-stranded viral DNA replication [GO:0039684] | null | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA ligase (ATP) activity [GO:0003910]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872] | PF05840; | null | Microviridae Rep protein family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.; EC=6.5.1.1; | null | null | null | null | FUNCTION: Plays an essential role in viral DNA replication. Binds the origin of replication and cleaves the dsDNA replicative form I (RFI) and becomes covalently bound to it via phosphotyrosine bond, generating the dsDNA replicative form II (RFII). In turn, viral DNA replication initiates in the presence of host Rep an... | Enterobacteria phage phiX174 (Isolate Sanger) (Bacteriophage phi-X174) |
P03661 | G3P_BPFD | MKKLLFAIPLVVPFYSHSAETVESCLAKPHTENSFTNVWKDDKTLDRYANYEGCLWNATGVVVCTGDETQCYGTWVPIGLAIPENEGGGSEGGGSEGGGSEGGGTKPPEYGDTPIPGYTYINPLDGTYPPGTEQNPANPNPSLEESQPLNTFMFQNNRFRNRQGALTVYTGTVTQGTDPVKTYYQYTPVSSKAMYDAYWNGKFRDCAFHSGFNEDPFVCEYQGQSSDLPQPPVNAGGGSGGGSGGGSEGGGSEGGGSEGGGSEGGGSGGGSGSGDFDYEKMANANKGAMTENADENALQSDAKGKLDSVATDYGAAIDGF... | null | null | adhesion receptor-mediated virion attachment to host cell [GO:0098671]; entry receptor-mediated virion attachment to host cell [GO:0098670]; viral extrusion [GO:0099045]; virion attachment to host cell pilus [GO:0039666] | host cell membrane [GO:0033644]; membrane [GO:0016020]; viral capsid [GO:0019028] | null | PF05357; | 2.30.27.10; | Inovirus G3P protein family | null | SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Prior to assembly, G3P is found associated with the bacterial host inner membrane. There are about five copies of this protein per mature phage that are located on the head side of the filame... | null | null | null | null | null | FUNCTION: Plays essential roles both in the penetration of the viral genome into the bacterial host via pilus retraction and in the extrusion process. During the initial step of infection, G3P mediates adsorption of the phage to its primary receptor, the tip of host F-pilus. Subsequent interaction with the host entry r... | Enterobacteria phage fd (Bacteriophage fd) |
P03679 | GP1_BPPH2 | MGKIFDQEKRLEGTWKNSKWGNQGIIAPVDGDLKMIDLELEKKMTKLEHENKLMKNALYELSRMENNDYATWVIKVLFGGAPHGAK | null | null | DNA replication [GO:0006260]; viral DNA genome replication [GO:0039693] | host cell membrane [GO:0033644]; membrane [GO:0016020] | RNA binding [GO:0003723] | null | null | Phi29likevirus DNA replication protein 1 family | null | SUBCELLULAR LOCATION: Host membrane {ECO:0000269|PubMed:11032825, ECO:0000269|PubMed:12904294}; Peripheral membrane protein {ECO:0000269|PubMed:12904294}. | null | null | null | null | null | FUNCTION: Protein that assembles into highly ordered structures and provides a specific site for viral DNA replication. Probably anchors the viral DNA replisome to the host membrane. {ECO:0000269|PubMed:11032825, ECO:0000269|PubMed:12904294, ECO:0000269|PubMed:9193003, ECO:0000269|PubMed:9774353}. | Bacillus phage phi29 (Bacteriophage phi-29) |
P03680 | DPOL_BPPH2 | MKHMPRKMYSCDFETTTKVEDCRVWAYGYMNIEDHSEYKIGNSLDEFMAWVLKVQADLYFHNLKFDGAFIINWLERNGFKWSADGLPNTYNTIISRMGQWYMIDICLGYKGKRKIHTVIYDSLKKLPFPVKKIAKDFKLTVLKGDIDYHKERPVGYKITPEEYAYIKNDIQIIAEALLIQFKQGLDRMTAGSDSLKGFKDIITTKKFKKVFPTLSLGLDKEVRYAYRGGFTWLNDRFKEKEIGEGMVFDVNSLYPAQMYSRLLPYGEPIVFEGKYVWDEDYPLHIQHIRCEFELKEGYIPTIQIKRSRFYKGNEYLKSSG... | 2.7.7.7; 3.1.11.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:1310035, ECO:0000269|PubMed:15608377, ECO:0000269|PubMed:17611604, ECO:0000269|PubMed:9784372}; | DNA replication [GO:0006260]; viral DNA genome replication [GO:0039693] | null | DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exonuclease activity [GO:0004527]; metal ion binding [GO:0046872]; nucleoside binding [GO:0001882]; nucleotide binding [GO:0000166] | PF03175; | 1.10.287.690;3.90.1600.10;3.30.420.10;3.30.1770.10; | DNA polymerase type-B family | null | null | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000269|PubMed:3863101}; | null | null | null | null | FUNCTION: Polymerase responsible for protein-primed viral DNA replication by strand displacement with high processivity and fidelity (PubMed:2498321, PubMed:3863101). To start replication, the DNA polymerase forms a heterodimer with a free primer terminal protein (TP), recognizes the replication origins at both 5' ends... | Bacillus phage phi29 (Bacteriophage phi-29) |
P03681 | TERM_BPPH2 | MARSPRIRIKDNDKAEYARLVKNTKAKIARTKKKYGVDLTAEIDIPDLDSFETRAQFNKWKEQASSFTNRANMRYQFEKNAYGVVASKAKIAEIERNTKEVQRLVDEKIKAMKDKEYYAGGKPQGTIEQRIAMTSPAHVTGINRPHDFDFSKVRSYSRLRTLEESMEMRTDPQYYEKKMIQLQLNFIKSVEGSFNSFDAADELIEELKKIPPDDFYELFLRISEISFEEFDSEGNTVENVEGNVYKILSYLEQYRRGDFDLSLKGF | null | null | DNA replication, synthesis of RNA primer [GO:0006269]; symbiont entry into host cell via disruption of host cell envelope [GO:0098994]; symbiont entry into host cell via disruption of host cell wall peptidoglycan [GO:0098932]; viral DNA genome packaging [GO:0019073]; viral DNA genome replication [GO:0039693] | host cell nucleus [GO:0042025]; viral terminase complex [GO:0043493]; virion component [GO:0044423] | DNA binding [GO:0003677]; hydrolase activity [GO:0016787] | PF05435; | 6.10.250.960;1.20.1270.230; | Phi29likevirus DNA terminal protein family | null | SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:14763988}. Host nucleus {ECO:0000269|PubMed:23091024}. Note=Associates with the host bacterial nucleoid through its N-terminal region. {ECO:0000269|PubMed:20823229}. | null | null | null | null | null | FUNCTION: Acts as a primer for DNA elongation during viral genomic replication (PubMed:6813861). Acts as the small terminase protein during packaging (PubMed:18674782). Recruits the phage DNA polymerase to the bacterial nucleoid (PubMed:20823229). Primer terminal protein (TP) is covalently linked to the 5'-ends of both... | Bacillus phage phi29 (Bacteriophage phi-29) |
P03685 | NP_BPPH2 | MAKMMQREITKTTVNVAKMVMVDGEVQVEQLPSETFVGNLTMEQAQWRMKRKYKGEPVQVVSVEPNTEVYELPVEKFLEVATVRVEKDEDQEEQTEAPEEQVAE | null | null | chromosome condensation [GO:0030261]; DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; regulation of viral transcription [GO:0046782]; viral DNA genome replication [GO:0039693] | transcription repressor complex [GO:0017053] | DNA binding [GO:0003677]; DNA-binding transcription repressor activity [GO:0001217] | PF17548; | null | Phi29likevirus histone-like protein p6 family | null | null | null | null | null | null | null | FUNCTION: Histone-like nucleoprotein that binds to the viral dsDNA and responsible for wrapping and compacting the viral DNA about 4-fold. Forms a nucleoprotein complex in which the DNA adopts a right-handed toroidal conformation winding around a protein core. Binds ito most, if not all, the viral genome, although with... | Bacillus phage phi29 (Bacteriophage phi-29) |
P03692 | HELIC_BPT7 | MDNSHDSDSVFLYHIPCDNCGSSDGNSLFSDGHTFCYVCEKWTAGNEDTKERASKRKPSGGKPMTYNVWNFGESNGRYSALTARGISKETCQKAGYWIAKVDGVMYQVADYRDQNGNIVSQKVRDKDKNFKTTGSHKSDALFGKHLWNGGKKIVVTEGEIDMLTVMELQDCKYPVVSLGHGASAAKKTCAANYEYFDQFEQIILMFDMDEAGRKAVEEAAQVLPAGKVRVAVLPCKDANECHLNGHDREIMEQVWNAGPWIPDGVVSALSLRERIREHLSSEESVGLLFSGCTGINDKTLGARGGEVIMVTSGSGMGKST... | 2.7.7.-; 3.6.4.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_04154, ECO:0000269|PubMed:12769857}; Note=Binds 2 Mg(2+), one of which is catalytic. {ECO:0000255|HAMAP-Rule:MF_04154, ECO:0000269|PubMed:12769857, ECO:0000269|PubMed:30679383}; | viral DNA genome replication [GO:0039693] | null | 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA helicase activity [GO:0003678]; DNA primase activity [GO:0003896]; identical protein binding [GO:0042802]; single-stranded DNA binding [GO:0003697]; zinc ion binding [GO:0008270] | PF03796;PF21268;PF08273;PF13155; | 2.20.25.10;2.20.25.180;3.40.1360.10;3.40.50.300; | Teseptimavirus DNA helicase/primase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000255|HAMAP-Rule:MF_04154, ECO:0000269|PubMed:2829184, ECO:0000269|PubMed:9185573}; | null | null | null | null | FUNCTION: ATP-dependent DNA helicase and primase essential for viral DNA replication and recombination (PubMed:21606333, PubMed:22977246, PubMed:32009150). The helicase moves 5' -> 3' on the lagging strand template, unwinding the DNA duplex ahead of the leading strand polymerase at the replication fork and generating s... | Escherichia phage T7 (Bacteriophage T7) |
P03705 | HOLIN_LAMBD | MKMPEKHDLLAAILAAKEQGIGAILAFAMAYLRGRYNGGAFTKTVIDATMCAIIAWFIRDLLDFAGLSSNLAYITSVFIGYIGTDSIGSLIKRFAAKKAGVEDGRNQ | null | null | negative regulation of cytolysis [GO:0045918]; viral release from host cell by cytolysis [GO:0044659] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | pore-forming activity [GO:0140911] | PF05106; | null | Lambdavirus holin family | null | SUBCELLULAR LOCATION: Host cell inner membrane {ECO:0000269|PubMed:2137120}; Multi-pass membrane protein {ECO:0000269|PubMed:19897658}. Note=Classified as a class I holin. {ECO:0000305}. | null | null | null | null | null | FUNCTION: [Isoform Holin]: Accumulates harmlessly in the cytoplasmic membrane until it reaches a critical concentration that triggers the formation of micron-scale pores (holes) causing host cell membrane disruption and endolysin escape into the periplasmic space (PubMed:18788120, PubMed:21187415). Determines the preci... | Escherichia phage lambda (Bacteriophage lambda) |
P03706 | ENLYS_LAMBD | MVEINNQRKAFLDMLAWSEGTDNGRQKTRNHGYDVIVGGELFTDYSDHPRKLVTLNPKLKSTGAGRYQLLSRWWDAYRKQLGLKDFSPKSQDAVALQQIKERGALPMIDRGDIRQAIDRCSNIWASLPGAGYGQFEHKADSLIAKFKEAGGTVREIDV | 4.2.2.n2 | null | cell wall macromolecule catabolic process [GO:0016998]; defense response to bacterium [GO:0042742]; peptidoglycan catabolic process [GO:0009253]; viral release from host cell by cytolysis [GO:0044659] | host cell cytoplasm [GO:0030430] | lysozyme activity [GO:0003796]; lytic transglycosylase activity [GO:0008933] | PF00959; | 1.10.530.10; | Glycosyl hydrolase 24 family | null | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04109}. Note=The endolysin is cytoplasmic, but can reach the periplasmic space with the help of the holins which disrupt the host cell membrane. {ECO:0000255|HAMAP-Rule:MF_04109, ECO:0000305|PubMed:24113139}. | CATALYTIC ACTIVITY: Reaction=Endolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n2; Evidence={ECO:0000255|HAMAP-Rule:MF_04109, ECO:00002... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.6. {ECO:0000269|PubMed:6448076}; | null | FUNCTION: Endolysin with transglycosylase activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can ... | Escherichia phage lambda (Bacteriophage lambda) |
P03707 | TERS_LAMBD | MEVNKKQLADIFGASIRTIQNWQEQGMPVLRGGGKGNEVLYDSAAVIKWYAERDAEIENEKLRREVEELRQASEADLQPGTIEYERHRLTRAQADAQELKNARDSAEVVETAFCTFVLSRIAGEIASILDGLPLSVQRRFPELENRHVDFLKRDIIKAMNKAAALDELIPGLLSEYIEQSG | 3.6.4.- | null | viral DNA genome packaging [GO:0019073] | host cell cytoplasm [GO:0030430]; viral terminase, small subunit [GO:0097710] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; sequence-specific DNA binding, bending [GO:0044374] | PF07471; | 1.10.10.10; | Terminase small subunit family | null | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}. Note=The terminase lies at a unique vertex of the procapsid during viral DNA packaging. {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:2965248, ECO:0000269|PubMed:8611586}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=469 uM for ATP {ECO:0000269|PubMed:8611586}; | null | null | null | FUNCTION: The small subunit is responsible for the binding to multiple recognition elements within the packaging initiation site cos (PubMed:15755448, PubMed:16618107, PubMed:2989542). The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA... | Escherichia phage lambda (Bacteriophage lambda) |
P03708 | TERL_LAMBD | MNISNSQVNRLRHFVRAGLRSLFRPEPQTAVEWADANYYLPKESAYQEGRWETLPFQRAIMNAMGSDYIREVNVVKSARVGYSKMLLGVYAYFIEHKQRNTLIWLPTDGDAENFMKTHVEPTIRDIPSLLALAPWYGKKHRDNTLTMKRFTNGRGFWCLGGKAAKNYREKSVDVAGYDELAAFDDDIEQEGSPTFLGDKRIEGSVWPKSIRGSTPKVRGTCQIERAASESPHFMRFHVACPHCGEEQYLKFGDKETPFGLKWTPDDPSSVFYLCEHNACVIRQQELDFTDARYICEKTGIWTRDGILWFSSSGEEIEPPD... | 3.1.21.4; 3.6.4.-; 3.6.4.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_04144, ECO:0000269|PubMed:8175794, ECO:0000269|PubMed:8428984}; Note=Probably binds 2 Mg(2+) ions per subunit (By similarity). Necessary for the ATPase activity (PubMed:8175794, PubMed:8428984). Zn(2+) Co(2+), Cd(2+), Cu(2+), Ca(2+), Sr(... | viral DNA genome packaging [GO:0019073] | host cell cytoplasm [GO:0030430]; viral terminase, large subunit [GO:0098009] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA helicase activity [GO:0003678]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; type II site-specific deoxyribonuclease activity [GO:0009036] | PF05876;PF20454; | 3.40.50.300; | Lambdavirus large terminase family | null | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04144}. Note=The terminase lies at a unique vertex of the procapsid during viral DNA packaging. {ECO:0000255|HAMAP-Rule:MF_04144}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4; Evidence={ECO:0000255|HAMAP-Rule:MF_04144, ECO:0000269|PubMed:1534952, ECO:0000269|PubMed:17870092, ECO:0000269|PubMed:23134123, ECO:0000269|PubMed:2970303, ECO:0000269|PubM... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.6 uM for ATP for the high affinity ATPase {ECO:0000269|PubMed:8428984, ECO:0000269|PubMed:8611586, ECO:0000269|PubMed:8794874}; KM=23 uM for ATP for helicase {ECO:0000269|PubMed:8175794}; Note=The high affinity ATPase activity corresponds to the packaging ATPase ... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-9.0 for the ATPase and helicase. {ECO:0000269|PubMed:8175794}; | null | FUNCTION: The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome from the concetamer to initiate and to end the packaging reaction (PubMed:11866517, PubMed:23134123). The terminase lies at a unique vert... | Escherichia phage lambda (Bacteriophage lambda) |
P03711 | SCAF_LAMBD | MTAELRNLPHIASMAFNEPLMLEPAYARVFFCALAGQLGISSLTDAVSGDSLTAQEALATLALSGDDDGPRQARSYQVMNGIAVLPVSGTLVSRTRALQPYSGMTGYNGIIARLQQAASDPMVDGILLDMDTPGGMVAGAFDCADIIARVRDIKPVWALANDMNCSAGQLLASAASRRLVTQTARTGSIGVMMAHSNYGAALEKQGVEITLIYSGSHKVDGNPYSHLPDDVRETLQSRMDATRQMFAQKVSAYTGLSVQVVLDTEAAVYSGQEAIDAGLADELVNSTDAITVMRDALDARKSRLSGGRMTKETQSTTVSA... | 3.4.21.- | null | proteolysis [GO:0006508]; viral procapsid maturation [GO:0046797] | host cell cytoplasm [GO:0030430]; viral capsid [GO:0019028] | identical protein binding [GO:0042802]; serine-type peptidase activity [GO:0008236] | PF01343; | 6.20.330.10; | Peptidase S49 family | null | SUBCELLULAR LOCATION: [Isoform Capsid assembly protease C]: Virion. Host cytoplasm.; SUBCELLULAR LOCATION: [Isoform Capsid scaffolding protein Nu3]: Host cytoplasm. | null | null | null | null | null | FUNCTION: Assembly protease promotes icosahedral procapsid assembly. Autocatalytic cleavage may release the capsid scaffolding protein. The protease domain catalyzes the cleavage of the capsid scaffolding protein after complete procapsid formation. Assembly protease and cleavages products are evicted from the capsid be... | Escherichia phage lambda (Bacteriophage lambda) |
P03726 | EXLYS_BPT7 | MDKYDKNVPSDYDGLFQKAADANGVSYDLLRKVAWTESRFVPTAKSKTGPLGMMQFTKATAKALGLRVTDGPDDDRLNPELAINAAAKQLAGLVGKFDGDELKAALAYNQGEGRLGNPQLEAYSKGDFASISEEGRNYMRNLLDVAKSPMAGQLETFGGITPKGKGIPAEVGLAGIGHKQKVTQELPESTSFDVKGIEQEATAKPFAKDFWETHGETLDEYNSRSTFFGFKNAAEAELSNSVAGMAFRAGRLDNGFDVFKDTITPTRWNSHIWTPEELEKIRTEVKNPAYINVVTGGSPENLDDLIKLANENFENDSRAA... | 4.2.2.n1 | null | defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640]; peptidoglycan metabolic process [GO:0000270]; symbiont entry into host [GO:0044409]; symbiont entry into host cell via disruption of host cell envelope [GO:0098994]; symbiont entry into host cell via disruption of host cell w... | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | hydrolase activity [GO:0016787]; lytic transglycosylase activity [GO:0008933] | PF01464; | 1.10.530.10; | Transglycosylase Slt family | null | SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04121, ECO:0000269|PubMed:23884409}. Host cell inner membrane {ECO:0000255|HAMAP-Rule:MF_04121, ECO:0000269|PubMed:23306440}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04121}. Note=The gp15-gp16 complex spans the periplasm and the cytoplasmic membran... | CATALYTIC ACTIVITY: Reaction=Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the Mur... | null | null | null | null | FUNCTION: Component of the cylindrical core that assembles on the inner surface of the capsid during capsid formation and plays a role in viral DNA ejection into the host cell. The inner core is composed of stacked rings of gp14, gp15 and gp16 proteins. Following binding to the host cell surface, the internal core is d... | Escherichia phage T7 (Bacteriophage T7) |
P03763 | TARGB_BPMU | MNISDIRAGLRTLVENEETTFKQIALESGLSTGTISSFINDKYNGDNERVSQMLQRWLEKYHAVAELPEPPRFVETQTVKQIWTSMRFASLTESIAVVCGNPGVGKTEAAREYRRTNNNVWMITITPSCASVLECLTELAFELGMNDAPRRKGPLSRALRRRLEGTQGLVIIDEADHLGAEVLEELRLLQESTRIGLVLMGNHRVYSNMTGGNRTVEFARLFSRIAKRTAINKTKKADVKAIADAWQINGEKELELLQQIAQKPGALRILNHSLRLAAMTAHGKGERVNEDYLRQAFRELDLDVDISTLLRN | 3.6.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:23776210}; | DNA integration [GO:0015074]; DNA replication [GO:0006260]; DNA transposition [GO:0006313]; viral DNA genome replication [GO:0039693] | host cell cytoplasm [GO:0030430] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; metal ion binding [GO:0046872] | PF13401;PF09077; | 1.10.1180.10;1.10.260.40;3.40.50.300; | AAA ATPase family | null | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:23776210}; | null | null | null | null | FUNCTION: Selects the target DNA sites for transposition. Recruits DDE-recombinase A to the target sites and catalytically activates it. Displays non-specific DNA-binding properties. Polymerizes as helical filaments around the DNA. Coating of the DNA by the target DNA activator B might play a role in favoring target-pr... | Escherichia phage Mu (Bacteriophage Mu) |
P03819 | KEFC_ECOLI | MDSHTLIQALIYLGSAALIVPIAVRLGLGSVLGYLIAGCIIGPWGLRLVTDAESILHFAEIGVVLMLFIIGLELDPQRLWKLRAAVFGCGALQMVICGGLLGLFCMLLGLRWQVAELIGMTLALSSTAIAMQAMNERNLMVTQMGRSAFAVLLFQDIAAIPLVAMIPLLATSSASTTMGAFALSALKVAGALVLVVLLGRYVTRPALRFVARSGLREVFSAVALFLVFGFGLLLEEVGLSMAMGAFLAGVLLASSEYRHALESDIEPFKGLLLGLFFIGVGMSIDFGTLLENPLRIVILLLGFLIIKIAMLWLIARPLQV... | null | null | intracellular pH elevation [GO:0051454]; potassium ion transport [GO:0006813]; proton transmembrane transport [GO:1902600]; regulation of intracellular pH [GO:0051453]; regulation of pH [GO:0006885]; response to hydrogen peroxide [GO:0042542]; response to methylglyoxal [GO:0051595]; response to toxic substance [GO:0009... | membrane [GO:0016020]; plasma membrane [GO:0005886]; potassium:proton antiporter complex [GO:1903103] | antiporter activity [GO:0015297]; enzyme binding [GO:0019899]; glutathione-regulated potassium exporter activity [GO:0015503]; nucleotide binding [GO:0000166]; protein homodimerization activity [GO:0042803]; toxic substance binding [GO:0015643] | PF00999;PF02254; | 1.20.1530.20;3.40.50.720; | Monovalent cation:proton antiporter 2 (CPA2) transporter (TC 2.A.37) family, KefC subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01413, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2046548}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01413, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2046548}. | null | null | null | null | null | FUNCTION: Pore-forming subunit of a potassium efflux system that confers protection against electrophiles. Catalyzes K(+)/H(+) antiport. Can also export rubidium, lithium and sodium. {ECO:0000255|HAMAP-Rule:MF_01413, ECO:0000269|PubMed:17679694, ECO:0000269|PubMed:21041667, ECO:0000269|PubMed:9023177}. | Escherichia coli (strain K12) |
P03870 | FLP_YEAST | MPQFGILCKTPPKVLVRQFVERFERPSGEKIALCAAELTYLCWMITHNGTAIKRATFMSYNTIISNSLSFDIVNKSLQFKYKTQKATILEASLKKLIPAWEFTIIPYYGQKHQSDITDIVSSLQLQFESSEEADKGNSHSKKMLKALLSEGESIWEITEKILNSFEYTSRFTKTKTLYQFLFLATFINCGRFSDIKNVDPKSFKLVQNKYLGVIIQCLVTETKTSVSRHIYFFSARGRIDPLVYLDEFLRNSEPVLKRVNRTGNSSSNKQEYQLLKDNLVRSYNKALKKNAPYSIFAIKNGPKSHIGRHLMTSFLSMKGL... | null | null | plasmid recombination [GO:0042150] | null | DNA binding, bending [GO:0008301]; double-stranded DNA binding [GO:0003690]; single-stranded DNA binding [GO:0003697]; site-specific recombinase activity [GO:0009009] | PF05202;PF03930; | 3.30.300.80;1.10.443.10; | 'phage' integrase family | null | null | null | null | null | null | null | FUNCTION: Part of the plasmid amplification system, which corrects any decrease in copy number caused by a rare missegregation event. Catalyzes the recombination between the large inverted repetitions of the 2-micron plasmid during plasmid replication. This recombination event changes the direction of one of the two re... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P03871 | REP1_YEAST | MNGERLLACIKQCIMQHFQPMVYDESRCVIETTRGTFPVPDNYKKYKTLAFAFVGHVLNTDDTPVIEKELDWPDPALVYNTIVDRIINHPELSQFISVAFISQLKATIGEGLDINVKGTLNRRGKGIRRPKGVFFRYMESPFVNTKVTAFFSYLRDYNKIASEYHNNTKFILTFSCQAYWASGPNFSALKNVIRCSIIHEYISKFVEREQDKGHIGDQELPPEEDPSRELNNVQHEVNSLTEQDAEADEGLWGEIDSLCEKWQSEAEDQTEAEIIADRIIGNSQRMANLKIRRTKFKSVLYHILKELIQSQGTVKVYRGS... | null | null | 2-micrometer plasmid partitioning [GO:0030543]; protein localization [GO:0008104] | nucleus [GO:0005634] | identical protein binding [GO:0042802] | PF05797; | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10791970, ECO:0000269|PubMed:9393716, ECO:0000269|PubMed:9819432}. Note=Colocalizes with the STB locus of the 2-micron plasmid as foci in the nucleus near the spindle pole body. Is expelled from STB during a short interval between late G1 and early S phases. | null | null | null | null | null | FUNCTION: Part of the plasmid partitioning system, which ensures the equal distribution of replicated plasmid molecules to daughter cells. The plasmids exist as well-organized plasmid foci within the nucleus that stay together throughout the cell-cycle and act as entity during segregation, effetively reducing copy numb... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P03873 | MBI2_YEAST | MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVIIFILTIATAFLGYCCVYGQMSHWGNMNIASNMFNMMKTIYMMMLMLLIYIFYTIMMRQMMKTKEYTMLIKSMDYINKNKYMINLNMTNKKDMNNNIGPLNMNILSIIYGSMLGDGHAEKRKGGKGTRIVFQQEYCNINYLYYLHSLLANLGYCNTNLPLIKTRLGKKGKIRQYLKFNTWTYDSFNMIYSEWYIKNMSGKGN... | null | null | mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; mRNA processing [GO:0006397]; RNA splicing [GO:0008380] | mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739] | endonuclease activity [GO:0004519]; nuclease activity [GO:0004518]; ubiquinol-cytochrome-c reductase activity [GO:0008121] | PF00033;PF03161; | 3.10.28.10; | Cytochrome b family; LAGLIDADG endonuclease family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: This protein is responsible for splicing and maturation of cytochrome b mRNA. Specifically, it may be responsible for the splicing specificity of the second intron. {ECO:0000269|PubMed:11016843, ECO:0000269|PubMed:7004642, ECO:0000269|PubMed:8670880}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P03877 | SCE3_YEAST | MVQRWLYSTNAKDIAVLYFMLAIFSGMAGTAMSLIIRLELAAPGSQYLHGNSQLFNVLVVGHAVLMIFFLVMPALIGGFGNQKRYESNNNNNQVMENKEYNLKLNYDKLGPYLAGLIEGDGTITVQNSSSMKKSKYRPLIVVVFKLEDLELANYLCNLTKCGKVYKKINRNYVLWTIHDLKGVYTLLNIINGYMRTPKYEAFVRGAEFMNNYINSTTITHNKLKNMDNIKIKPLDTSDIGSNAWLAGMTDADGNFSINLMNGKNRSSRAMPYYCLELRQNYQKNSNNNNINFSYFYIMSAIATYFNVNLYSRERNLNLLV... | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:8367285}; | electron transport coupled proton transport [GO:0015990]; intron homing [GO:0006314]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mRNA processing [GO:0006397]; RNA splicing [GO:0008380] | mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739] | cytochrome-c oxidase activity [GO:0004129]; endonuclease activity [GO:0004519]; heme binding [GO:0020037] | PF00115;PF00961; | 1.20.210.10;3.10.28.10; | LAGLIDADG endonuclease family | PTM: The mature protein may arise from proteolytic cleavage of an in-frame translation of some COX1 exons plus the intron containing the aI3 open reading frame. {ECO:0000269|PubMed:7797552, ECO:0000269|PubMed:8367285}. | SUBCELLULAR LOCATION: Mitochondrion. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:8367285}; | null | FUNCTION: Mitochondrial DNA endonuclease involved in intron homing. It introduces a specific double-strand break in the DNA of the COX1 gene and thus mediates the insertion of an intron, containing its own coding sequence (group I intron), into an intronless gene. Recognizes with high specificity and cleaves the sequen... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P03878 | SCE2_YEAST | MVQRWLYSTNAKDIAVLYFMLAIFSGMAGTAMSLIIRLELAAPGSQYLHGNSQLFNVLVVGHAVLMIFFLVMPALIGGFGNYLLPLMIGATDTAFPRINNIAFWVLPMGLVCLVTSTLVESGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAINFIVTTLNMRTNGMTMHKLPLFVWSIFITAFLLLLSLPVLSAGITMLLLDRNFNTSFFEVSGGGDPILYEHLFWFFGQTVATIIMLMMYNDMHFSKCWKLLKKWITNIMSTLFKALFVKMFMSYNNQQDKMMNNTMLKKDNIKRSSETTRKMLNNSM... | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:2172241}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:2172241}; | electron transport coupled proton transport [GO:0015990]; intron homing [GO:0006314]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; mRNA processing [GO:0006397]; RNA splicing [GO:0008380] | mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739] | cytochrome-c oxidase activity [GO:0004129]; endonuclease activity [GO:0004519]; heme binding [GO:0020037] | PF00115;PF00961; | 1.20.210.10;3.10.28.10; | LAGLIDADG endonuclease family; Heme-copper respiratory oxidase family | PTM: The mature protein may arise from proteolytic cleavage of an in-frame translation of COX1 exons 1 to 4 plus intron 4, containing the aI4 open reading frame. Cleavage would take place close to the Met-299 resulting in an active endonuclease of about 30 kDa. {ECO:0000269|PubMed:2172241, ECO:0000269|PubMed:2216759, E... | SUBCELLULAR LOCATION: Mitochondrion. | null | null | null | null | null | FUNCTION: Mitochondrial DNA endonuclease involved in intron homing. It introduces a specific double-strand break at the junction of the two exons a4-a5 of the COX1 gene and thus mediates the insertion of an intron, containing its own coding sequence (group I intron), into an intronless gene. Recognizes with limited spe... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P03879 | MBI4_YEAST | MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVIIFILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMALHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLILALFVFYSPNTLGQNMALLLITYVINILCAVCWKSLFIKYQWKIYNKTTYYFIIQNILNTKQLNNFVLKFNWTKQYNKMNI... | 3.1.-.- | null | Group I intron splicing [GO:0000372]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; mitochondrial mRNA processing [GO:0090615]; mRNA processing [GO:0006397]; proton transmembrane transport [GO:1902600] | mitochondrion [GO:0005739] | endonuclease activity [GO:0004519]; RNA binding [GO:0003723] | PF00033;PF00961; | 3.10.28.10; | LAGLIDADG endonuclease family | PTM: The mature protein may arise from proteolytic cleavage of an in-frame translation of COB exons 1 to 4 plus intron 4, containing the bI4 open reading frame. Cleavage would take place close to the Met-385 resulting in an active maturase of about 30 kDa. {ECO:0000269|PubMed:8352597}. | SUBCELLULAR LOCATION: Mitochondrion. | null | null | null | null | null | FUNCTION: Mitochondrial mRNA maturase required for splicing of intron 4 of the cytochrome b (COB) gene, containing its own coding sequence, and intron 4 in COX1, coding for the related homing endonuclease aI4. In vivo splicing requires in addition the imported mitochondrial leucyl-tRNA synthetase NAM2. Both proteins se... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P03886 | NU1M_HUMAN | MPMANLLLLIVPILIAMAFLMLTERKILGYMQLRKGPNVVGPYGLLQPFADAMKLFTKEPLKPATSTITLYITAPTLALTIALLLWTPLPMPNPLVNLNLGLLFILATSSLAVYSILWSGWASNSNYALIGALRAVAQTISYEVTLAIILLSTLLMSGSFNLSTLITTQEHLWLLLPSWPLAMMWFISTLAETNRTPFDLAEGESELVSGFNIEYAAGPFALFFMAEYTNIIMMNTLTTTIFLGTTYDALSPELYTTYFVTKTLLLTSLFLWIRTAYPRFRYDQLMHLLWKNFLPLTLALLMWYVSMPITISSIPPQT | 7.1.1.2 | null | aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]; response to hydroperoxide [GO:0033194]; response to hypoxia [GO:0001666]; response to... | dendrite [GO:0030425]; mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex I [GO:0005747]; neuronal cell body [GO:0043025] | NADH dehydrogenase (ubiquinone) activity [GO:0008137] | PF00146; | null | Complex I subunit 1 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P03887}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000269|PubMed:1959619}; | null | null | null | null | FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:1959619). Essential for the catalytic activity and assembly of complex I (PubMed:1959619, PubM... | Homo sapiens (Human) |
P03887 | NU1M_BOVIN | MFMINILMLIIPILLAVAFLTLVERKVLGYMQLRKGPNVVGPYGLLQPIADAIKLFIKEPLRPATSSASMFILAPIMALGLALTMWIPLPMPYPLINMNLGVLFMLAMSSLAVYSILWSGWASNSKYALIGALRAVAQTISYEVTLAIILLSVLLMSGSFTLSTLITTQEQMWLILPAWPLAMMWFISTLAETNRAPFDLTEGESELVSGFNVEYAAGPFALFFMAEYANIIMMNIFTAILFLGTSHNPHMPELYTINFTIKSLLLTMSFLWIRASYPRFRYDQLMHLLWKNFLPLTLALCMWHVSLPILTSGIPPQT | 7.1.1.2 | null | aerobic respiration [GO:0009060]; mitochondrial respiratory chain complex I assembly [GO:0032981] | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747] | NADH dehydrogenase (ubiquinone) activity [GO:0008137] | PF00146; | null | Complex I subunit 1 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:17060615, ECO:0000269|PubMed:25209663}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000269|PubMed:3141400}; | null | null | null | null | FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:3141400). Essential for the catalytic activity of complex I (PubMed:3141400). Essential for th... | Bos taurus (Bovine) |
P03891 | NU2M_HUMAN | MNPLAQPVIYSTIFAGTLITALSSHWFFTWVGLEMNMLAFIPVLTKKMNPRSTEAAIKYFLTQATASMILLMAILFNNMLSGQWTMTNTTNQYSSLMIMMAMAMKLGMAPFHFWVPEVTQGTPLTSGLLLLTWQKLAPISIMYQISPSLNVSLLLTLSILSIMAGSWGGLNQTQLRKILAYSSITHMGWMMAVLPYNPNMTILNLTIYIILTTTAFLLLNLNSSTTTLLLSRTWNKLTWLTPLIPSTLLSLGGLPPLTGFLPKWAIIEEFTKNNSLIIPTIMATITLLNLYFYLRLIYSTSITLLPMSNNVKMKWQFEHT... | 7.1.1.2 | null | aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]; reactive oxygen species metabolic process [GO:0072593]; response to hypoxia [GO:00016... | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747] | ionotropic glutamate receptor binding [GO:0035255]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]; protein kinase binding [GO:0019901] | PF06444;PF00361; | null | Complex I subunit 2 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P03892}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000269|PubMed:16996290}; | null | null | null | null | FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:16996290). Essential for the catalytic activity and assembly of complex I (PubMed:16996290). {... | Homo sapiens (Human) |
P03892 | NU2M_BOVIN | MNPIIFIIILLTIMLGTIIVMISSHWLLVWIGFEMNMLAIIPIMMKNHNPRATEASTKYFLTQSTASMLLMMAVIINLMFSGQWTVMKLFNPMASMLMTMALAMKLGMAPFHFWVPEVTQGIPLSSGLILLTWQKLAPMSVLYQIFPSINLNLILTLSVLSILIGGWGGLNQTQLRKIMAYSSIAHMGWMTAVLPYNPTMTLLNLIIYIIMTSTMFTMFMANSTTTTLSLSHTWNKTPIMTVLILATLLSMGGLPPLSGFMPKWMIIQEMTKNNSIILPTFMAITALLNLYFYMRLTYSTTLTMFPSTNNMKMKWQFPLM... | 7.1.1.2 | null | mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981] | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747] | NADH dehydrogenase (ubiquinone) activity [GO:0008137] | PF06444;PF00361; | null | Complex I subunit 2 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:17060615, ECO:0000269|PubMed:25209663}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000250|UniProtKB:P03891}; | null | null | null | null | FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I. {ECO:0000250|UniProtKB:P03891}. | Bos taurus (Bovine) |
P03897 | NU3M_HUMAN | MNFALILMINTLLALLLMIITFWLPQLNGYMEKSTPYECGFDPMSPARVPFSMKFFLVAITFLLFDLEIALLLPLPWALQTTNLPLMVMSSLLLIIILALSLAYEWLQKGLDWTE | 7.1.1.2 | null | aerobic respiration [GO:0009060]; cellular response to glucocorticoid stimulus [GO:0071385]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]; response to light intensity [GO:0009642]; response to oxidative stress [GO:0006979] | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747] | NADH dehydrogenase (ubiquinone) activity [GO:0008137] | PF00507; | 1.20.58.1610; | Complex I subunit 3 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P03898}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000269|PubMed:25118196}; | null | null | null | null | FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:25118196). Essential for the catalytic activity of complex I (PubMed:25118196). {ECO:0000269|P... | Homo sapiens (Human) |
P03898 | NU3M_BOVIN | MNLMLALLTNFTLATLLVIIAFWLPQLNVYSEKTSPYECGFDPMGSARLPFSMKFFLVAITFLLFDLEIALLLPLPWASQTANLNTMLTMALFLIILLAVSLAYEWTQKGLEWTE | 7.1.1.2 | null | mitochondrial electron transport, NADH to ubiquinone [GO:0006120] | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747] | NADH dehydrogenase (ubiquinone) activity [GO:0008137] | PF00507; | 1.20.58.1610; | Complex I subunit 3 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:17060615, ECO:0000269|PubMed:25209663}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000250|UniProtKB:P03897}; | null | null | null | null | FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I. {ECO:0000250|UniProtKB:P03897}. | Bos taurus (Bovine) |
P03901 | NU4LM_HUMAN | MPLIYMNIMLAFTISLLGMLVYRSHLMSSLLCLEGMMLSLFIMATLMTLNTHSLLANIVPIAMLVFAACEAAVGLALLVSISNTYGLDYVHNLNLLQC | 7.1.1.2 | null | aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776] | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747] | NADH dehydrogenase (ubiquinone) activity [GO:0008137] | PF00420; | 1.10.287.3510; | Complex I subunit 4L family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P03902}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000305|PubMed:28844695}; Physiolog... | null | null | null | null | FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:28844695). Part of the enzyme membrane arm which is embedded in the lipid bilayer and involved... | Homo sapiens (Human) |
P03902 | NU4LM_BOVIN | MSMVYMNIMMAFTVSLVGLLMYRSHLMSSLLCLEGMMLSLFVMAALTILNSHFTLASMMPIILLVFAACEAALGLSLLVMVSNTYGTDYVQNLNLLQC | 7.1.1.2 | null | ATP synthesis coupled electron transport [GO:0042773] | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747] | NADH dehydrogenase (ubiquinone) activity [GO:0008137] | PF00420; | 1.10.287.3510; | Complex I subunit 4L family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:17060615, ECO:0000269|PubMed:18721790, ECO:0000269|PubMed:25209663}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000305|PubMed:18721790, ECO:000030... | null | null | null | null | FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:18721790, PubMed:25209663). Part of the enzyme membrane arm which is embedded in the lipid bil... | Bos taurus (Bovine) |
P03905 | NU4M_HUMAN | MLKLIVPTIMLLPLTWLSKKHMIWINTTTHSLIISIIPLLFFNQINNNLFSCSPTFSSDPLTTPLLMLTTWLLPLTIMASQRHLSSEPLSRKKLYLSMLISLQISLIMTFTATELIMFYIFFETTLIPTLAIITRWGNQPERLNAGTYFLFYTLVGSLPLLIALIYTHNTLGSLNILLLTLTAQELSNSWANNLMWLAYTMAFMVKMPLYGLHLWLPKAHVEAPIAGSMVLAAVLLKLGGYGMMRLTLILNPLTKHMAYPFLVLSLWGMIMTSSICLRQTDLKSLIAYSSISHMALVVTAILIQTPWSFTGAVILMIAHG... | 7.1.1.2 | null | aerobic respiration [GO:0009060]; cerebellum development [GO:0021549]; electron transport coupled proton transport [GO:0015990]; in utero embryonic development [GO:0001701]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive ... | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747] | NADH dehydrogenase (ubiquinone) activity [GO:0008137]; ubiquinone binding [GO:0048039] | PF01059;PF00361; | null | Complex I subunit 4 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P03910}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000269|PubMed:15250827, ECO:000026... | null | null | null | null | FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:15250827, PubMed:8344246, PubMed:8644732). Essential for the catalytic activity and assembly o... | Homo sapiens (Human) |
P03910 | NU4M_BOVIN | MLKYIIPTIMLMPLTWLSKNNMIWVNSTAHSLLISFTSLLLMNQFGDNSLNFSLLFFSDSLSTPLLILTMWLLPLMLMASQHHLSKENLTRKKLFITMLISLQLFLIMTFTAMELILFYILFEATLVPTLIIITRWGNQTERLNAGLYFLFYTLAGSLPLLVALIYIQNTVGSLNFLMLQYWVQPVHNSWSNVFMWLACMMAFMVKMPLYGLHLWLPKAHVEAPIAGSMVLAAVLLKLGGYGMLRITLILNPMTDFMAYPFIMLSLWGMIMTSSICLRQTDLKSLIAYSSVSHMALVIVAILIQTPWSYMGATALMIAHG... | 7.1.1.2 | null | aerobic respiration [GO:0009060]; electron transport coupled proton transport [GO:0015990]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981] | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747] | NADH dehydrogenase (ubiquinone) activity [GO:0008137]; ubiquinone binding [GO:0048039] | PF01059;PF00361; | null | Complex I subunit 4 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:17060615}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000250|UniProtKB:P03905}; | null | null | null | null | FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I. {ECO:0000250|UniProtKB:P03905}. | Bos taurus (Bovine) |
P03915 | NU5M_HUMAN | MTMHTTMTTLTLTSLIPPILTTLVNPNKKNSYPHYVKSIVASTFIISLFPTTMFMCLDQEVIISNWHWATTQTTQLSLSFKLDYFSMMFIPVALFVTWSIMEFSLWYMNSDPNINQFFKYLLIFLITMLILVTANNLFQLFIGWEGVGIMSFLLISWWYARADANTAAIQAILYNRIGDIGFILALAWFILHSNSWDPQQMALLNANPSLTPLLGLLLAAAGKSAQLGLHPWLPSAMEGPTPVSALLHSSTMVVAGIFLLIRFHPLAENSPLIQTLTLCLGAITTLFAAVCALTQNDIKKIVAFSTSSQLGLMMVTIGIN... | 7.1.1.2 | null | aerobic respiration [GO:0009060]; electron transport coupled proton transport [GO:0015990]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]; response to hydrogen peroxi... | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747] | NADH dehydrogenase (ubiquinone) activity [GO:0008137]; NADH dehydrogenase activity [GO:0003954] | PF06455;PF00361;PF00662; | null | Complex I subunit 5 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P03920}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000269|PubMed:15250827}; | null | null | null | null | FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:15250827). Essential for the catalytic activity and assembly of complex I (PubMed:15250827). {... | Homo sapiens (Human) |
P03920 | NU5M_BOVIN | MNMFSSLSLVTLLLLTMPIMMMSFNTYKPSNYPLYVKTAISYAFITSMIPTMMFIHSGQELIISNWHWLTIQTLKLSLSFKMDYFSMMFIPVALFVTWSIMEFSMWYMYSDPNINKFFKYLLLFLITMLILVTANNLFQLFIGWEGVGIMSFLLIGWWYGRADANTAALQAILYNRIGDIGFILAMAWFLTNLNTWDLQQIFMLNPSDSNMPLIGLALAATGKSAQFGLHPWLPSAMEGPTPVSALLHSSTMVVAGIFLLIRFYPLTENNKYIQSITLCLGAITTLFTAMCALTQNDIKKIIAFSTSSQLGLMMVTIGIN... | 7.1.1.2 | null | electron transport coupled proton transport [GO:0015990]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981] | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747] | NADH dehydrogenase (ubiquinone) activity [GO:0008137]; NADH dehydrogenase activity [GO:0003954] | PF06455;PF00361;PF00662; | null | Complex I subunit 5 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:17060615}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000250|UniProtKB:P03915}; | null | null | null | null | FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I. {ECO:0000250|UniProtKB:P03915}. | Bos taurus (Bovine) |
P03923 | NU6M_HUMAN | MMYALFLLSVGLVMGFVGFSSKPSPIYGGLVLIVSGVVGCVIILNFGGGYMGLMVFLIYLGGMMVVFGYTTAMAIEEYPEAWGSGVEVLVSVLVGLAMEVGLVLWVKEYDGVVVVVNFNSVGSWMIYEGEGSGLIREDPIGAGALYDYGRWLVVVTGWTLFVGVYIVIEIARGN | 7.1.1.2 | null | aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]; response to cocaine [GO:0042220]; response to hydrogen peroxide [GO:0042542]; respons... | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739] | NADH dehydrogenase (ubiquinone) activity [GO:0008137] | PF00499; | null | Complex I subunit 6 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P03924}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000269|PubMed:14595656, ECO:000026... | null | null | null | null | FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:14595656, PubMed:8644732). Essential for the catalytic activity and assembly of complex I (Pub... | Homo sapiens (Human) |
P03928 | ATP8_HUMAN | MPQLNTTVWPTMITPMLLTLFLITQLKMLNTNYHLPPSPKPMKMKNYNKPWEPKWTKICSLHSLPPQS | null | null | proton motive force-driven ATP synthesis [GO:0015986]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776] | mitochondrial inner membrane [GO:0005743]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) [GO:0000276] | proton transmembrane transporter activity [GO:0015078] | PF00895; | null | ATPase protein 8 family | null | SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein. | null | null | null | null | null | FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... | Homo sapiens (Human) |
P03945 | COX1_NEUCR | MSSISIWTERWFLSTNAKDIGVLYLIFALFSGLLGTAFSVLIRMELSGPGVQYIADNQLYNAIITAHAILMIFFMVMPALIGGFGNFLLPLLVGGPDMAFPRLNNISFWLLPPSLLLLVFSACIEGGAGTGWTIYPPLSGVQSHSGPSVDLAIFALHLSGVSSLLGSINFITTIVNMRTPGIRLHKLALFGWAVVITAVLLLLSLPVLAGAITMLLTDRNFNTSFFETAGGGDPILFQHLFWFFGHPEVYILIIPGFGIISTTISAYSNKSVFGYIGMVYAMMSIGILGFIVWSHHMYTVGLDVDTRAYFTAATLIIAVP... | 7.1.1.9 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P00401}; Note=Binds 2 heme A groups non-covalently per subunit. {ECO:0000250|UniProtKB:P00401}; COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P00401}; Note=Binds a copper B center. {ECO:0000250|UniProtKB:P00... | electron transport coupled proton transport [GO:0015990]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123] | mitochondrial respiratory chain complex IV [GO:0005751] | cytochrome-c oxidase activity [GO:0004129]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00115; | 1.20.210.10; | Heme-copper respiratory oxidase family | PTM: The amino end of the mature protein may be Ser-3. {ECO:0000305|PubMed:6327266}. | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:31316820}; Multi-pass membrane protein {ECO:0000269|PubMed:31316820}. | CATALYTIC ACTIVITY: Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=7.1.1.9; Evidence={ECO:0000250|UniP... | null | PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000250|UniProtKB:P00401}. | null | null | FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
P03946 | SODC_XIPGL | MVLKAVCVLRGAGETTGTVYFEQEGNANAVGKGIILKGLTPGEHGFHVHGFGDNTNGCISAGPHFNPASKKHAGPKDEDRHVGDLGNVTADANGVAKIDITDKISLTGPYSIIGRTMVIHEKADDLGRGGNEESLKTGNAGSRLACGVIGTE | 1.15.1.1 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Note=Binds 1 copper ion per subunit.; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; | null | cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; peroxisome [GO:0005777] | copper ion binding [GO:0005507]; superoxide dismutase activity [GO:0004784] | PF00080; | 2.60.40.200; | Cu-Zn superoxide dismutase family | null | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; | null | null | null | null | FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | Xiphias gladius (Swordfish) (Tetrapterus imperator) |
P03949 | ABL1_CAEEL | MGHSHSTGKEINDNELFTCEDPVFDQPVASPKSEISSKLAEEIERSKSPLILEVSPRTPDSVQMFRPTFDTFRPPNSDSSTFRGSQSREDLVACSSMNSVNNVHDMNTVSSSSSSSAPLFVALYDFHGVGEEQLSLRKGDQVRILGYNKNNEWCEARLYSTRKNDASNQRRLGEIGWVPSNFIAPYNSLDKYTWYHGKISRSDSEAILGSGITGSFLVRESETSIGQYTISVRHDGRVFHYRINVDNTEKMFITQEVKFRTLGELVHHHSVHADGLICLLMYPASKKDKGRGLFSLSPNAPDEWELDRSEIIMHNKLGGG... | 2.7.10.2 | null | defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; DNA damage checkpoint signaling [GO:0000077]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell migration [GO:0030336]; negative regulation of DNA damage response, signal transduction by p... | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713] | PF08919;PF07714;PF00017;PF00018; | 1.20.120.330;3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, ABL subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27780040}. Cytoplasm {ECO:0000269|PubMed:27780040}. Note=Enriched at the leading edge compared to cytoplasm. Targeted to the leading edge of Q neuroblasts by mig-13. {ECO:0000269|PubMed:27780040}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Functions downstream of migratory protein mig-13 and is involved in Q neuroblast migration during larval development (PubMed:27780040). Recruited by mig-13 to the leading edge of Q neuroblasts and their descendents to signal downstream, likely to the wve-1 pathway, and direct migration along the anteroposteri... | Caenorhabditis elegans |
P03950 | ANGI_HUMAN | MVMGLGVLLLVFVLGLGLTPPTLAQDNSRYTHFLTQHYDAKPQGRDDRYCESIMRRRGLTSPCKDINTFIHGNKRSIKAICENKNGNPHRENLRISKSSFQVTTCKLHGGSPWPPCQYRATAGFRNVVVACENGLPVHLDQSIFRRP | 3.1.27.- | null | actin filament polymerization [GO:0030041]; activation of phospholipase A2 activity [GO:0032431]; activation of phospholipase C activity [GO:0007202]; activation of protein kinase B activity [GO:0032148]; angiogenesis [GO:0001525]; antibacterial humoral response [GO:0019731]; antimicrobial humoral immune response media... | actin cytoskeleton [GO:0015629]; angiogenin-PRI complex [GO:0032311]; basement membrane [GO:0005604]; chromosome [GO:0005694]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; growth cone [GO:0030426]; neuronal cell body [GO:0043025]; nucleolus... | actin binding [GO:0003779]; copper ion binding [GO:0005507]; DNA binding [GO:0003677]; endonuclease activity [GO:0004519]; heparin binding [GO:0008201]; peptide binding [GO:0042277]; protein homodimerization activity [GO:0042803]; RNA endonuclease activity [GO:0004521]; RNA nuclease activity [GO:0004540]; rRNA binding ... | PF00074; | 3.10.130.10; | Pancreatic ribonuclease family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000250|UniProtKB:Q3TMQ6}. Secreted {ECO:0000250|UniProtKB:P10152}. Nucleus {ECO:0000269|PubMed:12051708, ECO:0000269|PubMed:25372031, ECO:0000269|PubMed:8127865}. Nucleus, nucleolus {ECO:0000269|PubMed:7945327}. Note=Rapidly endocytosed by target ... | null | null | null | null | null | FUNCTION: Ribonuclease that cleaves tRNA within anticodon loops to produce tRNA-derived stress-induced fragments (tiRNAs) which inhibit protein synthesis and triggers the assembly of stress granules (SGs) (PubMed:1400510, PubMed:21855800). Binds to actin on the surface of endothelial cells; once bound, angiogenin is en... | Homo sapiens (Human) |
P03951 | FA11_HUMAN | MIFLYQVVHFILFTSVSGECVTQLLKDTCFEGGDITTVFTPSAKYCQVVCTYHPRCLLFTFTAESPSEDPTRWFTCVLKDSVTETLPRVNRTAAISGYSFKQCSHQISACNKDIYVDLDMKGINYNSSVAKSAQECQERCTDDVHCHFFTYATRQFPSLEHRNICLLKHTQTGTPTRITKLDKVVSGFSLKSCALSNLACIRDIFPNTVFADSNIDSVMAPDAFVCGRICTHHPGCLFFTFFSQEWPKESQRNLCLLKTSESGLPSTRIKKSKALSGFSLQSCRHSIPVFCHSSFYHDTDFLGEELDIVAAKSHEACQKL... | 3.4.21.27 | null | blood coagulation [GO:0007596]; plasminogen activation [GO:0031639]; positive regulation of fibrinolysis [GO:0051919] | extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; plasma membrane [GO:0005886] | heparin binding [GO:0008201]; identical protein binding [GO:0042802]; serine-type aminopeptidase activity [GO:0070009]; serine-type endopeptidase activity [GO:0004252] | PF00024;PF00089; | 3.50.4.10;2.40.10.10; | Peptidase S1 family, Plasma kallikrein subfamily | PTM: N-glycosylated on both chains. N-glycosylated sites mainly consist of nonfucosylated sialylated biantennary (in high abundance) and/or triantennary (in low abundance) complex structures. Glycosylation at Asn-163 uses a rare non-canonical Asn-X-Cys glycosite. {ECO:0000269|PubMed:25092234}.; PTM: Activated by factor... | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Ala and Arg-|-Val bonds in factor IX to form factor IXa.; EC=3.4.21.27; | null | null | null | null | FUNCTION: Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX. | Homo sapiens (Human) |
P03952 | KLKB1_HUMAN | MILFKQATYFISLFATVSCGCLTQLYENAFFRGGDVASMYTPNAQYCQMRCTFHPRCLLFSFLPASSINDMEKRFGCFLKDSVTGTLPKVHRTGAVSGHSLKQCGHQISACHRDIYKGVDMRGVNFNVSKVSSVEECQKRCTSNIRCQFFSYATQTFHKAEYRNNCLLKYSPGGTPTAIKVLSNVESGFSLKPCALSEIGCHMNIFQHLAFSDVDVARVLTPDAFVCRTICTYHPNCLFFTFYTNVWKIESQRNVCLLKTSESGTPSSSTPQENTISGYSLLTCKRTLPEPCHSKIYPGVDFGGEELNVTFVKGVNVCQE... | 3.4.21.34 | null | blood coagulation [GO:0007596]; Factor XII activation [GO:0002542]; fibrinolysis [GO:0042730]; plasminogen activation [GO:0031639]; positive regulation of fibrinolysis [GO:0051919]; proteolysis [GO:0006508]; zymogen activation [GO:0031638] | extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | serine-type endopeptidase activity [GO:0004252] | PF00024;PF00089; | 3.50.4.10;2.40.10.10; | Peptidase S1 family, Plasma kallikrein subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Cleaves selectively Arg-|-Xaa and Lys-|-Xaa bonds, including Lys-|-Arg and Arg-|-Ser bonds in (human) kininogen to release bradykinin.; EC=3.4.21.34; | null | null | null | null | FUNCTION: Participates in the surface-dependent activation of blood coagulation. Activates, in a reciprocal reaction, coagulation factor XII/F12 after binding to negatively charged surfaces. Releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin... | Homo sapiens (Human) |
P03953 | CFAD_MOUSE | MHSSVYFVALVILGAAVCAAQPRGRILGGQEAAAHARPYMASVQVNGTHVCGGTLLDEQWVLSAAHCMDGVTDDDSVQVLLGAHSLSAPEPYKRWYDVQSVVPHPGSRPDSLEDDLILFKLSQNASLGPHVRPLPLQYEDKEVEPGTLCDVAGWGVVTHAGRRPDVLHQLRVSIMNRTTCNLRTYHDGVVTINMMCAESNRRDTCRGDSGSPLVCGDAVEGVVTWGSRVCGNGKKPGVYTRVSSYRMWIENITNGNMTS | 3.4.21.46 | null | complement activation, alternative pathway [GO:0006957]; Notch signaling pathway [GO:0007219]; proteolysis [GO:0006508]; response to bacterium [GO:0009617] | extracellular space [GO:0005615] | endopeptidase activity [GO:0004175]; serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family | PTM: N-glycosylated. {ECO:0000269|PubMed:16944957, ECO:0000269|PubMed:17330941}. | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Lys bond in complement factor B when in complex with complement subcomponent C3b or with cobra venom factor.; EC=3.4.21.46; | null | null | null | null | FUNCTION: Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway. | Mus musculus (Mouse) |
P03954 | PEPA1_MACFU | MKWLLLLGLVALSECIIYKVPLVRKKSLRRNLSEHGLLKDFLKKHNLNPASKYFPQAEAPTLIDEQPLENYLDVEYFGTIGIGTPAQDFTVIFDTGSSNLWVPSVYCSSLACTNHNLFNPQDSSTYQSTSGTLSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISSSGATPVFDNIWDQGLVSQDLFSVYLSADDQSGSVVIFGGIDSSYYTGSLNWVPVSVEGYWQISVDSITMNGEAIACAEGCQAIVDTGTSLLTGPTSPIANIQSDIGASENSDGEMVVSCSAISSLPDI... | 3.4.23.1 | null | digestion [GO:0007586]; proteolysis [GO:0006508] | extracellular exosome [GO:0070062] | aspartic-type endopeptidase activity [GO:0004190] | PF07966;PF00026; | 6.10.140.60;2.40.70.10; | Peptidase A1 family | PTM: Each pepsinogen is converted to corresponding pepsin at pH 2.0 in part as a result of the release of a 47 AA activation segment and in part as a result of stepwise proteolytic cleavage via an intermediate form(s). | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.; EC=3.4.... | null | null | null | null | FUNCTION: Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent. | Macaca fuscata fuscata (Japanese macaque) |
P03956 | MMP1_HUMAN | MHSFPPLLLLLFWGVVSHSFPATLETQEQDVDLVQKYLEKYYNLKNDGRQVEKRRNSGPVVEKLKQMQEFFGLKVTGKPDAETLKVMKQPRCGVPDVAQFVLTEGNPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQAIYGRSQNPVQPIGPQTPKACDSKLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVF... | 3.4.24.7 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754, ECO:0000269|PubMed:8090713, ECO:0000269|PubMed:8278810, ECO:0000269|PubMed:9484219}; Note=Binds 4 Ca(2+) ions per subunit. {ECO:0000269|PubMed:7656013, ECO:0000269|PubMed:8031754, ECO:0000269|PubMed:8090713,... | cellular response to UV-A [GO:0071492]; collagen catabolic process [GO:0030574]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; positive regulation of protein-containing complex assembly [GO:0031334]; protein metabolic process [GO:0019538]; proteolysis [GO:0006508] | extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | endopeptidase activity [GO:0004175]; metalloendopeptidase activity [GO:0004222]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]; zinc ion binding [GO:0008270] | PF00045;PF00413;PF01471; | 3.40.390.10;2.110.10.10; | Peptidase M10A family | PTM: Undergoes autolytic cleavage to two major forms (22 kDa and 27 kDa). A minor form (25 kDa) is the glycosylated form of the 22 kDa form. The 27 kDa form has no activity while the 22/25 kDa form can act as activator for collagenase. {ECO:0000269|PubMed:10092871}.; PTM: Tyrosine phosphorylated in platelets by PKDCC/V... | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305|PubMed:2167156}. | CATALYTIC ACTIVITY: Reaction=Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.; EC=3.4.24.7; Evidence={ECO:000... | null | null | null | null | FUNCTION: Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X (PubMed:1645757, PubMed:2153297, PubMed:2557822). In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicit... | Homo sapiens (Human) |
P03957 | MMP3_RAT | MKGLPVLLWLCTAVCSSYPLHGSEEDAGMEVLQKYLENYYGLEKDVKQFTKKKDSSPVVKKIQEMQKFLGLKMTGKLDSNTMELMHKPRCGVPDVGGFSTFPGSPKWRKNHISYRIVNYTLDLPRESVDSAIERALKVWEEVTPLTFSRISEGEADIMISFAVEEHGDFIPFDGPGMVLAHAYAPGPGTNGDAHFDDDERWTDDVTGTNLFLVAAHELGHSLGLFHSANAEALMYPVYKSSTDLARFHLSQDDVDGIQSLYGPPTESPDVLVVPTKSNSLDPETLPMCSSALSFDAVSTLRGEVLFFKDRHFWRKSLRTP... | 3.4.24.17 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:1963430}; Note=Binds 4 Ca(2+) ions per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; | cellular response to amino acid stimulus [GO:0071230]; cellular response to cell-matrix adhesion [GO:0071460]; cellular response to interleukin-1 [GO:0071347]; cellular response to reactive oxygen species [GO:0034614]; cellular response to UV-A [GO:0071492]; collagen catabolic process [GO:0030574]; extracellular matrix... | cell body [GO:0044297]; cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; protein-containing complex [GO:0032991] | endopeptidase activity [GO:0004175]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; peptidase activity [GO:0008233]; protein-containing complex binding [GO:0044877]; zinc ion binding [GO:0008270] | PF00045;PF00413;PF01471; | 3.40.390.10;2.110.10.10; | Peptidase M10A family | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:1963430, ECO:0000269|PubMed:1988438, ECO:0000269|PubMed:2841336}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage where P1', P2' and P3' are hydrophobic residues.; EC=3.4.24.17; Evidence={ECO:0000269|PubMed:1963430, ECO:0000269|PubMed:1988438, ECO:0000269|PubMed:2841336}; | null | null | null | null | FUNCTION: Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase. {ECO:0000269|PubMed:1963430}.; FUNCTION: Metalloproteinase with a rather broad substrate specificity that can degrade fibronectin, laminin, gelatins of typ... | Rattus norvegicus (Rat) |
P03958 | ADA_MOUSE | MAQTPAFNKPKVELHVHLDGAIKPETILYFGKKRGIALPADTVEELRNIIGMDKPLSLPGFLAKFDYYMPVIAGCREAIKRIAYEFVEMKAKEGVVYVEVRYSPHLLANSKVDPMPWNQTEGDVTPDDVVDLVNQGLQEGEQAFGIKVRSILCCMRHQPSWSLEVLELCKKYNQKTVVAMDLAGDETIEGSSLFPGHVEAYEGAVKNGIHRTVHAGEVGSPEVVREAVDILKTERVGHGYHTIEDEALYNRLLKENMHFEVCPWSSYLTGAWDPKTTHAVVRFKNDKANYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEE... | 3.5.4.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8634299, ECO:0000269|PubMed:9622483}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:1925539, ECO:0000269|PubMed:8634299, ECO:0000269|PubMed:9622483}; | adenosine catabolic process [GO:0006154]; adenosine metabolic process [GO:0046085]; allantoin metabolic process [GO:0000255]; alpha-beta T cell differentiation [GO:0046632]; amide catabolic process [GO:0043605]; AMP catabolic process [GO:0006196]; AMP salvage [GO:0044209]; apoptotic process [GO:0006915]; B cell prolife... | anchoring junction [GO:0070161]; cytoplasm [GO:0005737]; cytoplasmic vesicle lumen [GO:0060205]; cytosol [GO:0005829]; dendrite cytoplasm [GO:0032839]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lysosome [GO:0005764]; neuronal cell body [GO:0043025] | 2'-deoxyadenosine deaminase activity [GO:0046936]; adenosine deaminase activity [GO:0004000]; purine nucleoside binding [GO:0001883]; zinc ion binding [GO:0008270] | PF00962; | 3.20.20.140; | Metallo-dependent hydrolases superfamily, Adenosine and AMP deaminases family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P00813}; Peripheral membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}. Cell junction {ECO:0000250|UniProtKB:P00813}. Cytoplasmic vesicle lumen {ECO:0000269|PubMed:8783262}. Cytoplasm {ECO:0000250}. Lysosome {ECO:0000250|UniProtKB:P00813}. Note=Co... | CATALYTIC ACTIVITY: Reaction=adenosine + H(+) + H2O = inosine + NH4(+); Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; Evidence={ECO:0000269|PubMed:10720488, ECO:0000269|PubMed:8634299, ECO:0000269|PubMed:8672487, ECO:0000269|PubMed:89426... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 uM for adenosine {ECO:0000269|PubMed:8634299, ECO:0000269|PubMed:8672487}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-8.5. {ECO:0000269|PubMed:8634299, ECO:0000269|PubMed:8672487}; | null | FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine (PubMed:10720488, PubMed:8634299, PubMed:8672487, PubMed:8942668, PubMed:9272950). Plays an important role in purine metabolism and in adenosine homeostasis (PubMed:10720488, PubMed:9272950). Modulates signaling by extracellular adenosine,... | Mus musculus (Mouse) |
P03959 | KDPA_ECOLI | MAAQGFLLIATFLLVLMVLARPLGSGLARLINDIPLPGTTGVERVLFRALGVSDREMNWKQYLCAILGLNMLGLAVLFFMLLGQHYLPLNPQQLPGLSWDLALNTAVSFVTNTNWQSYSGETTLSYFSQMAGLTVQNFLSAASGIAVIFALIRAFTRQSMSTLGNAWVDLLRITLWVLVPVALLIALFFIQQGALQNFLPYQAVNTVEGAQQLLPMGPVASQEAIKMLGTNGGGFFNANSSHPFENPTALTNFVQMLAIFLIPTALCFAFGEVMGDRRQGRMLLWAMSVIFVICVGVVMWAEVQGNPHLLALGTDSSINM... | null | null | monoatomic cation transmembrane transport [GO:0098655]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813] | plasma membrane [GO:0005886]; potassium ion-transporting ATPase complex [GO:0031004]; potassium:proton antiporter complex [GO:1903103] | P-type potassium transmembrane transporter activity [GO:0008556]; potassium ion binding [GO:0030955] | PF03814; | null | KdpA family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00275, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2849541, ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378, ECO:0000269|PubMed:7896809}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00275, ECO:0000269|PubMed:28636601, ECO:00002... | null | null | null | null | null | FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm (PubMed:23930894, PubMed:2849541, PubMed:8499455). This subunit binds the periplasmic potassium ions and delivers the ions to ... | Escherichia coli (strain K12) |
P03960 | KDPB_ECOLI | MSRKQLALFEPTLVVQALKEAVKKLNPQAQWRNPVMFIVWIGSLLTTCISIAMASGAMPGNALFSAAISGWLWITVLFANFAEALAEGRSKAQANSLKGVKKTAFARKLREPKYGAAADKVPADQLRKGDIVLVEAGDIIPCDGEVIEGGASVDESAITGESAPVIRESGGDFASVTGGTRILSDWLVIECSVNPGETFLDRMIAMVEGAQRRKTPNEIALTILLIALTIVFLLATATLWPFSAWGGNAVSVTVLVALLVCLIPTTIGGLLSAIGVAGMSRMLGANVIATSGRAVEAAGDVDVLLLDKTGTITLGNRQAS... | 7.2.2.6 | null | monoatomic cation transmembrane transport [GO:0098655]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813] | plasma membrane [GO:0005886]; potassium ion-transporting ATPase complex [GO:0031004]; potassium:proton antiporter complex [GO:1903103] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; magnesium ion binding [GO:0000287]; P-type potassium transmembrane transporter activity [GO:0008556] | PF00122;PF00702; | 3.40.1110.10;2.70.150.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IA subfamily | PTM: Phosphorylated at Ser-162, which leads to the inhibition of the ATPase activity. {ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378}. | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00285, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2849541, ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00285, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:28636601, ECO:0000... | CATALYTIC ACTIVITY: Reaction=ATP + H2O + K(+)(out) = ADP + H(+) + K(+)(in) + phosphate; Xref=Rhea:RHEA:16777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00285, ECO:0000269|PubMed:2849541, ECO:0000269|... | null | null | null | null | FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm (PubMed:23930894, PubMed:2849541, PubMed:8499455). This subunit is responsible for energy coupling to the transport system and... | Escherichia coli (strain K12) |
P03961 | KDPC_ECOLI | MSGLRPALSTFIFLLLITGGVYPLLTTVLGQWWFPWQANGSLIREGDTVRGSALIGQNFTGNGYFHGRPSATAEMPYNPQASGGSNLAVSNPELDKLIAARVAALRAANPDASASVPVELVTASASGLDNNITPQAAAWQIPRVAKARNLSVEQLTQLIAKYSQQPLVKYIGQPVVNIVELNLALDKLDE | null | null | monoatomic cation transmembrane transport [GO:0098655]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813] | plasma membrane [GO:0005886]; potassium ion-transporting ATPase complex [GO:0031004]; potassium:proton antiporter complex [GO:1903103] | ATP binding [GO:0005524]; P-type potassium transmembrane transporter activity [GO:0008556] | PF02669; | null | KdpC family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00276, ECO:0000269|PubMed:2849541, ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00276, ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378}. | null | null | null | null | null | FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm (PubMed:23930894, PubMed:2849541, PubMed:8499455). This subunit acts as a catalytic chaperone that increases the ATP-binding a... | Escherichia coli (strain K12) |
P03962 | PYRF_YEAST | MSKATYKERAATHPSPVAAKLFNIMHEKQTNLCASLDVRTTKELLELVEALGPKICLLKTHVDILTDFSMEGTVKPLKALSAKYNFLLFEDRKFADIGNTVKLQYSAGVYRIAEWADITNAHGVVGPGIVSGLKQAAEEVTKEPRGLLMLAELSCKGSLATGEYTKGTVDIAKSDKDFVIGFIAQRDMGGRDEGYDWLIMTPGVGLDDKGDALGQQYRTVDDVVSTGSDIIIVGRGLFAKGRDAKVEGERYRKAGWEAYLRRCGQQN | 4.1.1.23 | null | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; UMP biosynthetic process [GO:0006222] | cytosol [GO:0005829] | orotate phosphoribosyltransferase activity [GO:0004588]; orotidine-5'-phosphate decarboxylase activity [GO:0004590] | PF00215; | 3.20.20.70; | OMP decarboxylase family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU10110}; | null | PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P03965 | CARB_YEAST | MTSIYTSTEPTNSAFTTEDYKPQLVEGVNSVLVIGSGGLSIGQAGEFDYSGSQAIKALKEDNKFTILVNPNIATNQTSHSLADKIYYLPVTPEYITYIIELERPDAILLTFGGQTGLNCGVALDESGVLAKYNVKVLGTPIKTLITSEDRDLFASALKDINIPIAESFACETVDEALEAAERVKYPVIVRSAYALGGLGSGFANNASEMKELAAQSLSLAPQILVEKSLKGWKEVEYEVVRDRVGNCITVCNMENFDPLGVHTGDSMVFAPSQTLSDEEFHMLRSAAIKIIRHLGVIGECNVQYALQPDGLDYRVIEVNA... | 6.3.4.16; 6.3.5.5 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00409}; | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; arginine biosynthetic process [GO:0006526]; citrulline biosynthetic process [GO:0019240]; glutamine metabolic process [GO:0006541]; pyrimidine nucleotide biosynthetic process [GO:0006221]; UTP biosynthetic process [GO:0006228] | carbamoyl-phosphate synthase complex [GO:0005951]; cytoplasm [GO:0005737]; cytosol [GO:0005829] | aspartate carbamoyltransferase activity [GO:0004070]; ATP binding [GO:0005524]; carbamoyl-phosphate synthase (ammonia) activity [GO:0004087]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; dihydroorotase activity [GO:0004151]; metal ion binding [GO:0046872] | PF02786;PF02787;PF02142; | 3.40.50.20;3.30.1490.20;3.30.470.20;1.10.1030.10;3.40.50.1380; | CarB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:200419, ECO:0000269|PubMed:205532}. | CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.3 mM for hydrogencarbonate {ECO:0000269|PubMed:206535}; KM=75 mM for NH4(+) {ECO:0000269|PubMed:206535}; KM=0.2 mM for ATP {ECO:0000269|PubMed:206652}; KM=6.08 mM for ATP (for the ammonia-dependent ATPase reaction) {ECO:0000269|PubMed:12392708}; Vmax=0.64 umol/mi... | PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. {ECO:0000305|PubMed:5856369}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:206652}; | null | FUNCTION: Large subunit of the arginine-specific carbamoyl phosphate synthase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, hydrogencarbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P03966 | MYCN_MOUSE | MPSCTASTMPGMICKNPDLEFDSLQPCFYPDEDDFYFGGPDSTPPGEDIWKKFELLPTPPLSPSRAFPEHSPEPSNWATEMLLPEADLWGNPAEEDAFGLGGLGGLTPNPVILQDCMWSGFSAREKLERAVNEKLQHGHGPPGVSSACSAPGVGASSPGGRALGGSSSASHTGATLPTDLSHPAAECVDPAVVFPFPVNKRESASVPAAPTSAPATSAAVTSVSVPATAPVAAPARAGGRPASSGEAKALSTSGEDTLSDSDDEDDEEEDEEEEIDVVTVEKRRSSSNNKAVTTFTITVRPKTSALGLGRAQPGELILKR... | null | null | astrocyte differentiation [GO:0048708]; autosome genomic imprinting [GO:0141068]; branching morphogenesis of an epithelial tube [GO:0048754]; cartilage condensation [GO:0001502]; cell population proliferation [GO:0008283]; embryonic digit morphogenesis [GO:0042733]; embryonic skeletal system morphogenesis [GO:0048704];... | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00010;PF01056; | 4.10.280.10; | null | PTM: Phosphorylated by GSK3-beta which may promote its degradation. Phosphorylated by AURKA. {ECO:0000250|UniProtKB:P04198}. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Positively regulates the transcription of MYCNOS in neuroblastoma cells. {ECO:0000250|UniProtKB:P04198}. | Mus musculus (Mouse) |
P03967 | RASD_DICDI | MTEYKLVIVGGGGVGKSALTIQLIQNHFIDEYDPTIEDSYRKQVSIDDETCLLDILDTAGQEEYSAMRDQYMRTGQGFLCVYSITSRSSYDEIASFREQILRVKDKDRVPLILVGNKADLDHERQVSVNEGQELAKGFNCPFMESSAKSRINVEEAFYSLVREIRKELKGDQSSGKAQKKKKQCLIL | 3.6.5.2 | null | adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway [GO:0140582]; chemotaxis [GO:0006935]; ERK1 and ERK2 cascade [GO:0070371]; mitotic cytokinesis [GO:0000281]; phototaxis [GO:0042331]; Ras protein signal transduction [GO:0007265]; response to bacterium [GO:0009617]; thermotaxis [GO:0043052] | cytosol [GO:0005829]; lipid droplet [GO:0005811]; plasma membrane [GO:0005886] | filamin binding [GO:0031005]; G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; mitogen-activated protein kinase binding [GO:0051019]; protein kinase B binding [GO:0043422]; protein kinase inhibitor activity [GO:0004860]; protein kinase regulator activity... | PF00071; | 3.40.50.300; | Small GTPase superfamily, Ras family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000305|PubMed:18948008}; | null | null | null | null | FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. {ECO:0000269|PubMed:18948008}. | Dictyostelium discoideum (Social amoeba) |
P03968 | FGF1_BOVIN | MAEGETTTFTALTEKFNLPLGNYKKPKLLYCSNGGYFLRILPDGTVDGTKDRSDQHIQLQLCAESIGEVYIKSTETGQFLAMDTDGLLYGSQTPNEECLFLERLEENHYNTYISKKHAEKHWFVGLKKNGRSKLGPRTHFGQKAILFLPLPVSSD | null | null | activation of protein kinase B activity [GO:0032148]; angiogenesis [GO:0001525]; animal organ morphogenesis [GO:0009887]; branch elongation involved in ureteric bud branching [GO:0060681]; cell differentiation [GO:0030154]; cellular response to heat [GO:0034605]; fibroblast growth factor receptor signaling pathway [GO:... | cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634] | fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; integrin binding [GO:0005178]; S100 protein binding [GO:0044548] | PF00167; | 2.80.10.50; | Heparin-binding growth factors family | PTM: In the nucleus, phosphorylated by PKC/PRKCD. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted. Cytoplasm {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytosol. Nucleus. Note=Lacks a cleavable signal sequence. Within the cytoplasm, it is transported to the cell membrane and then secreted by a non-classical pathway that requires Cu(2+) ions and S100A13. Secreted in... | null | null | null | null | null | FUNCTION: Plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration. Functions as a potent mitogen in vitro. Acts as a ligand for FGFR1 and integrins. Binds to FGFR1 in the presence of heparin leading to FGFR1 dimerization and activation via sequent... | Bos taurus (Bovine) |
P03969 | FGF2_BOVIN | MAAGSITTLPALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYSSWYVALKRTGQYKLGPKTGPGQKAILFLPMSAKS | null | null | angiogenesis [GO:0001525]; animal organ morphogenesis [GO:0009887]; branching involved in ureteric bud morphogenesis [GO:0001658]; cell differentiation [GO:0030154]; fibroblast growth factor receptor signaling pathway [GO:0008543]; lung development [GO:0030324]; positive regulation of angiogenesis [GO:0045766]; positiv... | cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634] | fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; integrin binding [GO:0005178] | PF00167; | 2.80.10.50; | Heparin-binding growth factors family | PTM: Phosphorylation at Tyr-82 regulates FGF2 unconventional secretion. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P09038}. Nucleus {ECO:0000250|UniProtKB:P09038}. Note=Exported from cells by an endoplasmic reticulum (ER)/Golgi-independent mechanism (By similarity). Unconventional secretion of FGF2 occurs by direct translocation across the plasma membrane (By similarity). Bindin... | null | null | null | null | null | FUNCTION: Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Also acts as an integrin ligand which is required for FGF2 signaling (By similarity). Binds to integrin ITGAV:ITGB3 (By similarity). Plays an important role in the regulation of cell survival, cell division, cell differentiation and cell migr... | Bos taurus (Bovine) |
P03970 | INHBA_PIG | MPLLWLRGFLLASCWIIVRSSPTPGSGGHSAAPDCPSCALATLPKDVPNSQPEMVEAVKKHILNMLHLKKRPDVTQPVPKAALLNAIRKLHVGKVGENGYVELEDDIGRRAEMNELMEQTSEIITFAEAGTARKTLRFEISKEGSDLSVVERAEIWLFLKVPKANRTRTKVSIRLFQQQRRPQGSADAGEEAEDVGFPEEKSEVLISEKVVDARKSTWHIFPVSSSIQRLLDQGKSALDIRTACEQCHETGASLVLLGKKKKKEEEAEGRKRDGEGAGVDEEKEQSHRPFLMLQARQSEEHPHRRRRRGLECDGKVNICC... | null | null | activin receptor signaling pathway [GO:0032924]; eyelid development in camera-type eye [GO:0061029]; hair follicle development [GO:0001942]; hematopoietic progenitor cell differentiation [GO:0002244]; hemoglobin biosynthetic process [GO:0042541]; male gonad development [GO:0008584]; negative regulation of cell growth [... | activin A complex [GO:0043509]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; inhibin A complex [GO:0043512] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; hormone activity [GO:0005179] | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, eryth... | Sus scrofa (Pig) |
P03971 | MIS_HUMAN | MRDLPLTSLALVLSALGALLGTEALRAEEPAVGTSGLIFREDLDWPPGSPQEPLCLVALGGDSNGSSSPLRVVGALSAYEQAFLGAVQRARWGPRDLATFGVCNTGDRQAALPSLRRLGAWLRDPGGQRLVVLHLEEVTWEPTPSLRFQEPPPGGAGPPELALLVLYPGPGPEVTVTRAGLPGAQSLCPSRDTRYLVLAVDRPAGAWRGSGLALTLQPRGEDSRLSTARLQALLFGDDHRCFTRMTPALLLLPRSEPAPLPAHGQLDTVPFPPPRPSAELEESPPSADPFLETLTRLVRALRVPPARASAPRLALDPDAL... | null | null | anti-Mullerian hormone signaling pathway [GO:1990262]; cell-cell signaling [GO:0007267]; gonadal mesoderm development [GO:0007506]; Leydig cell differentiation [GO:0033327]; Mullerian duct regression [GO:0001880]; negative regulation of ovarian follicle development [GO:2000355]; ovarian follicle development [GO:0001541... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | growth factor activity [GO:0008083]; hormone activity [GO:0005179]; signaling receptor binding [GO:0005102]; type II transforming growth factor beta receptor binding [GO:0005114] | PF04709;PF00019; | 2.10.90.10; | TGF-beta family | PTM: Preproprotein is proteolytically processed to generate N- and C-terminal cleavage products that homodimerize and associate to form a biologically active non-covalent complex (PubMed:2974034, PubMed:8469238). Binding of the non-covalent complex to AMHR2 induces dissociation of the pro-region from the mature C-termi... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2974034, ECO:0000269|PubMed:3754790}. | null | null | null | null | null | FUNCTION: Plays an important role in several reproductive functions. Induces Muellerian duct regression during male fetal sexual differentiation (PubMed:34155118, PubMed:3754790, PubMed:8469238). Also plays a role in Leydig cell differentiation and function (By similarity). In female acts as a negative regulator of the... | Homo sapiens (Human) |
P03973 | SLPI_HUMAN | MKSSGLFPFLVLLALGTLAPWAVEGSGKSFKAGVCPPKKSAQCLRYKKPECQSDWQCPGKKRCCPDTCGIKCLDPVDTPNPTRRKPGKCPVTYGQCLMLNPPNFCEMDGQCKRDLKCCMGMCGKSCVSPVKA | null | null | antibacterial humoral response [GO:0019731]; immune response [GO:0006955]; innate immune response [GO:0045087]; modulation of process of another organism [GO:0035821]; negative regulation of protein binding [GO:0032091]; negative regulation of viral genome replication [GO:0045071]; response to lipopolysaccharide [GO:00... | collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; specific granule lumen [GO:0035580] | DNA binding [GO:0003677]; endopeptidase inhibitor activity [GO:0004866]; enzyme binding [GO:0019899]; mRNA binding [GO:0003729]; serine-type endopeptidase inhibitor activity [GO:0004867] | PF00095; | 4.10.75.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2039600, ECO:0000269|PubMed:24352879, ECO:0000269|PubMed:3462719, ECO:0000269|PubMed:3485543}. | null | null | null | null | null | FUNCTION: Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G (PubMed:10702419, PubMed:2039600, PubMed:2110563, PubMed:24121345, PubMed:3462719, PubMed:3533531). Modulates the inflammatory and immune responses after bacterial infection, and after infection by the... | Homo sapiens (Human) |
P03974 | TERA_PIG | MASGADSKGDDLSTAILKQKNRPNRLIVDEAINEDNSVVSLSQPKMDELQLFRGDTVLLKGKKRREAVCIVLSDDTCSDEKIRMNRVVRNNLRVHLGDVISIQPCPDVKYGKRIHVLPIDDTVEGITGNLFEVYLKPYFLEAYRPIRKGDIFLVRGGMRAVEFKVVETDPSPYCIVAPDTVIHCEGEPIKREDEEESLNEVGYDDIGGCRKQLAQIKEMVELPLRHPALFKAIGVKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAIIFIDELDAIAPKREKTHGEV... | 3.6.4.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | autophagosome maturation [GO:0097352]; autophagy [GO:0006914]; cellular response to arsenite ion [GO:1903843]; cellular response to heat [GO:0034605]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; endoplasmic reticulum stress-induced pre-emptive quality control [GO:... | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]; VCP-NPL4-UFD1 AAA ATPase complex [GO:0034098] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; lipid binding [GO:0008289]; polyubiquitin modification-dependent protein binding [GO:0031593] | PF00004;PF17862;PF02933;PF02359; | 1.10.8.60;2.40.40.20;3.10.330.10;6.10.20.150;3.40.50.300; | AAA ATPase family | PTM: ISGylated. {ECO:0000250|UniProtKB:P55072}.; PTM: Methylation at Lys-315 catalyzed by VCPKMT is increased in the presence of ASPSCR1. Lys-315 methylation may decrease ATPase activity. {ECO:0000250|UniProtKB:P55072}.; PTM: Phosphorylated by tyrosine kinases in response to T-cell antigen receptor activation. Phosphor... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P55072}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P55072}. Nucleus {ECO:0000250|UniProtKB:P55072}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P55072}. Note=Recruited to the cytoplasmic surface of the endoplasmic reticulum via interaction with AMF... | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6; Evidence={ECO:0000250|UniProtKB:P55072}; | null | null | null | null | FUNCTION: Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive... | Sus scrofa (Pig) |
P03991 | HA1W_MOUSE | MAPCMLLLLLAAALAPTQTRAGPHSLRYFHTAVSRPGLGKPRFISVGYVDDTEFVRFDSDAENPRYEPRARWMEQVEPEYWERNTQIAKDNEQSSRVDLRTLLRYYNQSAGGSHTIQRMYGCDVGSDGRLLRGYEQVAYDGCDYIALNEDLKTWTAADMAALITKHKWEQAGAAERRRAYLEGACVEWLSRHLKNGNATLLRTDSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVYHQGLPKPLTLRWEPPPSAVSNTVIIAVLVVLGAAIVT... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent [GO:0002485]; antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen ... | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670] | beta-2-microglobulin binding [GO:0030881]; peptide antigen binding [GO:0042605]; peptide binding [GO:0042277]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102] | PF07654;PF00129;PF06623; | 2.60.40.10;3.30.500.10; | MHC class I family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Mus musculus (Mouse) |
P03994 | HPLN1_RAT | MRSLLFLVLISVCRADHLSDSYTPDQDRVIHIQAENGPRLLVEAEQAKVFSHRGGNVTLPCKFYRDPTAFGSGIHKIRIKWTKLTSDYLREVDVFVSMGYHKKTYGGYQGRVFLKGGSDNDASLIITDLTLEDYGRYKCEVIEGLEDDTAVVALELQGVVFPYFPRLGRYNLNFHEARQACLDQDAVIASFDQLYDAWRGGLDWCNAGWLSDGSVQYPITKPREPCGGQNTVPGVRNYGFWDKDKSRYDVFCFTSNFNGRFYYLIHPTKLTYDEAVQACLNDGAQIAKVGQIFAAWKLLGYDRCDAGWLADGSVRYPISR... | null | null | cell adhesion [GO:0007155]; central nervous system development [GO:0007417]; glial cell differentiation [GO:0010001]; positive regulation of neuroblast proliferation [GO:0002052]; skeletal system development [GO:0001501] | extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; perineuronal net [GO:0072534]; synapse [GO:0045202] | hyaluronic acid binding [GO:0005540]; structural molecule activity [GO:0005198] | PF07686;PF00193; | 2.60.40.10;3.10.100.10; | HAPLN family | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. | null | null | null | null | null | FUNCTION: Stabilizes the aggregates of proteoglycan monomers with hyaluronic acid in the extracellular cartilage matrix. | Rattus norvegicus (Rat) |
P03995 | GFAP_MOUSE | MERRRITSARRSYASETVVRGLGPSRQLGTMPRFSLSRMTPPLPARVDFSLAGALNAGFKETRASERAEMMELNDRFASYIEKVRFLEQQNKALAAELNQLRAKEPTKLADVYQAELRELRLRLDQLTANSARLEVERDNFAQDLGTLRQKLQDETNLRLEAENNLAAYRQEADEATLARVDLERKVESLEEEIQFLRKIYEEEVRELREQLAQQQVHVEMDVAKPDLTAALREIRTQYEAVATSNMQETEEWYRSKFADLTDAASRNAELLRQAKHEANDYRRQLQALTCDLESLRGTNESLERQMREQEERHARESAS... | null | null | astrocyte development [GO:0014002]; Bergmann glial cell differentiation [GO:0060020]; D-aspartate import across plasma membrane [GO:0070779]; extracellular matrix organization [GO:0030198]; gene expression [GO:0010467]; intermediate filament organization [GO:0045109]; intermediate filament-based process [GO:0045103]; i... | astrocyte end-foot [GO:0097450]; astrocyte projection [GO:0097449]; cell body [GO:0044297]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytoplasmic side of lysosomal membrane [GO:0098574]; cytoskeleton [GO:0005856]; glial cell projection [GO:0097386]; intermediate filament [GO:0005882]; membrane [GO:0016020];... | identical protein binding [GO:0042802]; integrin binding [GO:0005178]; kinase binding [GO:0019900]; structural constituent of cytoskeleton [GO:0005200] | PF00038;PF04732; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: Phosphorylated by PKN1. {ECO:0000250|UniProtKB:P14136}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P14136}. Note=Associated with intermediate filaments. {ECO:0000250|UniProtKB:P14136}. | null | null | null | null | null | FUNCTION: GFAP, a class-III intermediate filament, is a cell-specific marker that, during the development of the central nervous system, distinguishes astrocytes from other glial cells. | Mus musculus (Mouse) |
P03999 | OPSB_HUMAN | MSEEEFYLFKNISSVGPWDGPQYHIAPVWAFYLQAAFMGTVFLIGFPLNAMVLVATLRYKKLRQPLNYILVNVSFGGFLLCIFSVFPVFVASCNGYFVFGRHVCALEGFLGTVAGLVTGWSLAFLAFERYIVICKPFGNFRFSSKHALTVVLATWTIGIGVSIPPFFGWSRFIPEGLQCSCGPDWYTVGTKYRSESYTWFLFIFCFIVPLSLICFSYTQLLRALKAVAAQQQESATTQKAEREVSRMVVVMVGSFCVCYVPYAAFAMYMVNNRNHGLDLRLVTIPSFFSKSACIYNPIIYCFMNKQFQACIMKMVCGKAM... | null | null | cellular response to light stimulus [GO:0071482]; cellular response to UV-A [GO:0071492]; G protein-coupled receptor signaling pathway [GO:0007186]; phototransduction [GO:0007602]; signal transduction [GO:0007165]; visual perception [GO:0007601] | cone photoreceptor outer segment [GO:0120199]; cytosol [GO:0005829]; intercellular bridge [GO:0045171]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; photoreceptor disc membrane [GO:0097381]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750]; plasma membrane [G... | G protein-coupled photoreceptor activity [GO:0008020]; signaling receptor activity [GO:0038023] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Opsin subfamily | PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2937147, ECO:0000269|PubMed:31380578, ECO:0000269|PubMed:31730232}; Multi-pass membrane protein {ECO:0000255}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P51491}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P51491}. Cytoplas... | null | null | null | null | null | FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal (Probable). Required for the maintenance of cone outer segment organization in the ventral retina, but not essential for the maintenance of functioning cone photorecept... | Homo sapiens (Human) |
P04000 | OPSR_HUMAN | MAQQWSLQRLAGRHPQDSYEDSTQSSIFTYTNSNSTRGPFEGPNYHIAPRWVYHLTSVWMIFVVTASVFTNGLVLAATMKFKKLRHPLNWILVNLAVADLAETVIASTISIVNQVSGYFVLGHPMCVLEGYTVSLCGITGLWSLAIISWERWMVVCKPFGNVRFDAKLAIVGIAFSWIWAAVWTAPPIFGWSRYWPHGLKTSCGPDVFSGSSYPGVQSYMIVLMVTCCIIPLAIIMLCYLQVWLAIRAVAKQQKESESTQKAEKEVTRMVVVMIFAYCVCWGPYTFFACFAAANPGYAFHPLMAALPAYFAKSATIYNPV... | null | null | cellular response to light stimulus [GO:0071482]; G protein-coupled receptor signaling pathway [GO:0007186]; phototransduction [GO:0007602]; positive regulation of cytokinesis [GO:0032467]; signal transduction [GO:0007165]; visual perception [GO:0007601] | photoreceptor disc membrane [GO:0097381]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886] | G protein-coupled photoreceptor activity [GO:0008020]; photoreceptor activity [GO:0009881] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Opsin subfamily | PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. | SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. | Homo sapiens (Human) |
P04001 | OPSG_HUMAN | MAQQWSLQRLAGRHPQDSYEDSTQSSIFTYTNSNSTRGPFEGPNYHIAPRWVYHLTSVWMIFVVIASVFTNGLVLAATMKFKKLRHPLNWILVNLAVADLAETVIASTISVVNQVYGYFVLGHPMCVLEGYTVSLCGITGLWSLAIISWERWMVVCKPFGNVRFDAKLAIVGIAFSWIWAAVWTAPPIFGWSRYWPHGLKTSCGPDVFSGSSYPGVQSYMIVLMVTCCITPLSIIVLCYLQVWLAIRAVAKQQKESESTQKAEKEVTRMVVVMVLAFCFCWGPYAFFACFAAANPGYPFHPLMAALPAFFAKSATIYNPV... | null | null | cellular response to light stimulus [GO:0071482]; G protein-coupled receptor signaling pathway [GO:0007186]; phototransduction [GO:0007602]; positive regulation of cytokinesis [GO:0032467]; visual perception [GO:0007601] | photoreceptor disc membrane [GO:0097381]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886] | G protein-coupled photoreceptor activity [GO:0008020]; identical protein binding [GO:0042802]; photoreceptor activity [GO:0009881] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Opsin subfamily | PTM: N-glycosylated (PubMed:30948514). O-glycosylated (PubMed:30948514). {ECO:0000269|PubMed:30948514}.; PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. {ECO:0000305|PubMed:2937147}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20579627}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. {ECO:0000305|PubMed:12051694, ECO:0000305|PubMed:1302020, ECO:0000305|PubMed:2937147}. | Homo sapiens (Human) |
P04002 | ANPA_PSEAM | MALSLFTVGQLIFLFWTMRITEASPDPAAKAAPAAAAAPAAAAPDTASDAAAAAALTAANAKAAAELTAANAAAAAAATARG | null | null | null | extracellular space [GO:0005615] | ice binding [GO:0050825]; identical protein binding [GO:0042802] | null | null | Type-I AFP family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6952188}. | null | null | null | null | null | FUNCTION: Contributes to protect fish blood from freezing at subzero sea water temperatures. Lowers the blood freezing point. Binds to nascent ice crystals and prevents further growth. {ECO:0000269|PubMed:3769927, ECO:0000269|PubMed:6952188}. | Pseudopleuronectes americanus (Winter flounder) (Pleuronectes americanus) |
P04003 | C4BPA_HUMAN | MHPPKTPSGALHRKRKMAAWPFSRLWKVSDPILFQMTLIAALLPAVLGNCGPPPTLSFAAPMDITLTETRFKTGTTLKYTCLPGYVRSHSTQTLTCNSDGEWVYNTFCIYKRCRHPGELRNGQVEIKTDLSFGSQIEFSCSEGFFLIGSTTSRCEVQDRGVGWSHPLPQCEIVKCKPPPDIRNGRHSGEENFYAYGFSVTYSCDPRFSLLGHASISCTVENETIGVWRPSPPTCEKITCRKPDVSHGEMVSGFGPIYNYKDTIVFKCQKGFVLRGSSVIHCDADSKWNPSPPACEPNSCINLPDIPHASWETYPRPTKED... | null | null | complement activation, classical pathway [GO:0006958]; innate immune response [GO:0045087]; negative regulation of complement activation, classical pathway [GO:0045959]; positive regulation of protein catabolic process [GO:0045732]; regulation of opsonization [GO:1903027]; response to symbiotic bacterium [GO:0009609]; ... | blood microparticle [GO:0072562]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | RNA binding [GO:0003723] | PF18453;PF00084; | 1.20.5.3730;2.10.70.10; | null | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Controls the classical pathway of complement activation. It binds as a cofactor to C3b/C4b inactivator (C3bINA), which then hydrolyzes the complement fragment C4b. It also accelerates the degradation of the C4bC2a complex (C3 convertase) by dissociating the complement fragment C2a. Alpha chain binds C4b. It i... | Homo sapiens (Human) |
P04004 | VTNC_HUMAN | MAPLRPLLILALLAWVALADQESCKGRCTEGFNVDKKCQCDELCSYYQSCCTDYTAECKPQVTRGDVFTMPEDEYTVYDDGEEKNNATVHEQVGGPSLTSDLQAQSKGNPEQTPVLKPEEEAPAPEVGASKPEGIDSRPETLHPGRPQPPAEEELCSGKPFDAFTDLKNGSLFAFRGQYCYELDEKAVRPGYPKLIRDVWGIEGPIDAAFTRINCQGKTYLFKGSQYWRFEDGVLDPDYPRNISDGFDGIPDNVDAALALPAHSYSGRERVYFFKGKQYWEYQFQHQPSQEECEGSSLSAVFEHFAMMQRDSWEDIFELL... | null | null | cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell migration [GO:0016477]; cell-matrix adhesion [GO:0007160]; endodermal cell differentiation [GO:0035987]; extracellular matrix organization [GO:0030198]; immune response [GO:0006955]; liver regeneration [GO:0097421]; negative regulation of... | alphav-beta3 integrin-vitronectin complex [GO:0071062]; basement membrane [GO:0005604]; blood microparticle [GO:0072562]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Go... | collagen binding [GO:0005518]; extracellular matrix binding [GO:0050840]; extracellular matrix structural constituent [GO:0005201]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; polysaccharide binding [GO:0030247]; scavenger receptor activity [GO:0005044] | PF00045;PF01033; | 4.10.410.20;2.110.10.10; | null | PTM: Sulfated on tyrosine residues. {ECO:0000269|PubMed:17558413, ECO:0000269|PubMed:2479556, ECO:0000269|PubMed:25136834}.; PTM: N- and O-glycosylated. {ECO:0000250}.; PTM: Phosphorylation on Thr-69 and Thr-76 favors cell adhesion and spreading. {ECO:0000269|PubMed:9733784}.; PTM: It has been suggested that the active... | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:2448300, ECO:0000269|PubMed:29567995}.; SUBCELLULAR LOCATION: Parasitophorous vacuole {ECO:0000269|PubMed:29567995}. Note=(Microbial infection) In P.falciparum-infected red blood cells, VTN internalization is detected at the early trophozoite stage... | null | null | null | null | null | FUNCTION: Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal... | Homo sapiens (Human) |
P04011 | VP2_POVLY | MGGVLSLLFNISEIAAELSLSTGFTVDAILTGEAFAAVSTEAAWLIEIEAVDLAGLSTLEALSLTGLTTEQFSLLSAIPTALNNAIGIGVFFQTVSGASAVVAAGVTTFGYSKEVPVVNMALVPWFPQVDYLFPGFTSFSYYLNAVLDWGESLFHAVGREVWRHLMRQATLQIGQATRAVAVRSTNELSHTLAQIAENARWALTSGPVHIYSSVQDYYRYLPARNPIQLRQEYRNRGEPPPSRADFEYQENREGQRARRELGYDEPRSGQYVEHYTAPGGAHQRVTQDWMLPLILGLYGDITPTWEVELNKLEKEEDGPS... | null | null | symbiont entry into host cell [GO:0046718]; viral penetration into host nucleus [GO:0075732] | host cell [GO:0043657]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; viral capsid [GO:0019028] | DNA binding [GO:0003677]; structural molecule activity [GO:0005198] | PF00761; | null | Polyomaviruses capsid protein VP2 family | null | SUBCELLULAR LOCATION: [Isoform VP2]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform VP3]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}. | null | null | null | null | null | FUNCTION: [Isoform VP2]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic ret... | B-lymphotropic polyomavirus (LPV) |
P04014 | VE1_HPV11 | MADDSGTENEGSGCTGWFMVEAIVEHTTGTQISEDEEEEVEDSGYDMVDFIDDRHITQNSVEAQALFNRQEADAHYATVQDLKRKYLGSPYVSPISNVANAVESEISPRLDAIKLTTQPKKVKRRLFETRELTDSGYGYSEVEAATQVEKHGDPENGGDGQERDTGRDIEGEGVEHREAEAVDDSTREHADTSGILELLKCKDIRSTLHGKFKDCFGLSFVDLIRPFKSDRTTCADWVVAGFGIHHSIADAFQKLIEPLSLYAHIQWLTNAWGMVLLVLIRFKVNKSRCTVARTLGTLLNIPENHMLIEPPKIQSGVRAL... | 3.6.4.12 | null | bidirectional double-stranded viral DNA replication [GO:0039686]; DNA duplex unwinding [GO:0032508]; DNA replication [GO:0006260]; protein hexamerization [GO:0034214]; viral DNA genome replication [GO:0039693] | host cell nucleus [GO:0042025] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; TPR domain binding [GO:0030911] | PF00519;PF20450;PF00524; | 3.40.1310.10;3.40.50.300;1.10.10.510; | Papillomaviridae E1 protein family | PTM: Phosphorylated. {ECO:0000255|HAMAP-Rule:MF_04000}.; PTM: Sumoylated. {ECO:0000255|HAMAP-Rule:MF_04000}. | SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04000, ECO:0000269|PubMed:15564503}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000255|HAMAP-Rule:MF_04000}; | null | null | null | null | FUNCTION: ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of protein E2 leading to a ... | Human papillomavirus 11 |
P04021 | PG057_VACCW | MWPFASVPAGAKCRLVETLPENMDFRSDHLTTFECFNEIITLAKKYIYIASFCCNPLSTTRGALIFDKLKEASEKGIKIIVLLDERGKRNLGELQSHCPDINFITVNIDKKNNVGLLLGCFWVSDDERCYVGNASFTGGSIHTIKTLGVYSDYPPLATDLRRRFDTFKAFNSAKNSWLNLCSAACCLPVSTAYHIKNPIGGVFFTDSPEHLLGYSRDLDTDVVIDKLKSAKTSIDIEHLAIVPTTRVDGNSYYWPDIYNSIIEAAINRGVKIRLLVGNWDKNDVYSMATARSLDALCVQNDLSVKVFTIQNNTKLLIVDD... | 3.1.1.-; 3.1.4.4 | null | viral budding from Golgi membrane [GO:0046760]; viral budding via host ESCRT complex [GO:0039702] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi apparatus [GO:0044177]; membrane [GO:0016020]; viral envelope [GO:0019031]; viral membrane [GO:0036338]; virion membrane [GO:0055036] | phospholipase D activity [GO:0004630] | PF13918; | 3.30.870.10; | Orthopoxvirus OPG057 family | PTM: Palmitoylated. Attachment of the palmitate moiety is essential for correct intracellular targeting and protein function. {ECO:0000269|PubMed:11017799, ECO:0000269|PubMed:8999886}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:12706074}; Lipid-anchor {ECO:0000269|PubMed:12706074}. Host Golgi apparatus, host trans-Golgi network {ECO:0000269|PubMed:27466413, ECO:0000269|PubMed:29540596}. Host endoplasmic reticulum membrane {ECO:0000269|PubMed:12706074}; Lipid-anchor {ECO:0000269|PubMed:... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4; Evidence={ECO:0000269|PubMed:9405398}; PhysiologicalDirecti... | null | null | null | null | FUNCTION: Major envelope protein that plays a role in the biogenesis of the viral double membrane and in egress of virus from the host cell (PubMed:17475658, PubMed:27466413, PubMed:8999886). Produces the wrapped form of virus that is required for cell-to-cell spread (PubMed:27466413, PubMed:29540596). Acts as a lipase... | Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) |
P04022 | GAG_SRV1 | MGQELSQHERYVEQLKQALKTRGVKVKYADLLKFFDFVKDTCPWFPQEGTIDIKRWRRVGDCFQDYYNTFGPEKVPVTAFSYWNLIKELIDKKEVNPQVMAAVAQTEEILKTSSHTELTTKPSQNPDLDLISLDSDDEGAKGSSLKDKNLSCTKKPKRFPVLLTAQTSADPEDPNPSEVDWDGLEDEAAKYHNPDWPPFLTRPPPYNKATPSAPTVMAVVNPKEELKEKIAQLEEQIKLEELHQALISKLQKLKTGNETVTSPETAGGFSRTPHWPGQHIPKGKCCASREKEEQTPKDIFPVTETVDGQGQAWRHHNGFD... | null | null | viral budding via host ESCRT complex [GO:0039702] | viral nucleocapsid [GO:0019013] | nucleic acid binding [GO:0003676]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270] | PF02337;PF00607;PF19317;PF14787; | 1.10.1200.30;1.10.375.10;1.10.150.490;4.10.60.10; | null | PTM: [Gag polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and is required for the assembly of viral particles. {ECO:0000250|UniProtKB:P10258}.; PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield matu... | SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: Virion {ECO:0000305}. | null | null | null | null | null | FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.; FUNCTION: [Nucleocapsid protein p14]: Nucleocapsid protein. {ECO:0000305}.; FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000305}. | Simian retrovirus SRV-1 |
P04024 | PRO_SRV1 | MGQELSQHERYVEQLKQALKTRGVKVKYADLLKFFDFVKDTCPWFPQEGTIDIKRWRRVGDCFQDYYNTFGPEKVPVTAFSYWNLIKELIDKKEVNPQVMAAVAQTEEILKTSSHTELTTKPSQNPDLDLISLDSDDEGAKGSSLKDKNLSCTKKPKRFPVLLTAQTSADPEDPNPSEVDWDGLEDEAAKYHNPDWPPFLTRPPPYNKATPSAPTVMAVVNPKEELKEKIAQLEEQIKLEELHQALISKLQKLKTGNETVTSPETAGGFSRTPHWPGQHIPKGKCCASREKEEQTPKDIFPVTETVDGQGQAWRHHNGFD... | 3.4.23.-; 3.6.1.23 | null | nucleotide metabolic process [GO:0009117]; proteolysis [GO:0006508]; viral process [GO:0016032] | viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; dUTP diphosphatase activity [GO:0004170]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270] | PF00692;PF01585;PF02337;PF00607;PF19317;PF00077;PF14787; | 1.10.1200.30;2.70.40.10;2.40.70.10;1.10.375.10;1.10.150.490;4.10.60.10; | null | PTM: [Protease 17 kDa]: Released by autocatalytic processing. The protease can undergo further autoprocessing to yield 2 shorter but enzymatically active forms of 12 kDa and 13 kDa without the GDP domain. {ECO:0000250|UniProtKB:P07570}.; PTM: [Gag-Pro polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domai... | SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein-dUTPase]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Protease 13 kDa]: Virion {ECO:0000250|UniProtKB:P07570}.; SUBCELLULAR LOCATION: [Prote... | CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23; Evidence={ECO:0000250|UniProtKB:P07570}; | null | null | null | null | FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.; FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein. {ECO:0000305}.; FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000305}.; FUNCTION: [Protease 17 kDa]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins duri... | Simian retrovirus SRV-1 |
P04025 | POL_SRV1 | MGQELSQHERYVEQLKQALKTRGVKVKYADLLKFFDFVKDTCPWFPQEGTIDIKRWRRVGDCFQDYYNTFGPEKVPVTAFSYWNLIKELIDKKEVNPQVMAAVAQTEEILKTSSHTELTTKPSQNPDLDLISLDSDDEGAKGSSLKDKNLSCTKKPKRFPVLLTAQTSADPEDPNPSEVDWDGLEDEAAKYHNPDWPPFLTRPPPYNKATPSAPTVMAVVNPKEELKEKIAQLEEQIKLEELHQALISKLQKLKTGNETVTSPETAGGFSRTPHWPGQHIPKGKCCASREKEEQTPKDIFPVTETVDGQGQAWRHHNGFD... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.-; 3.6.1.23 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; Note=The RT polymerase active site binds 2 magnesium ions. {ECO:0000255|PROSITE-ProRule:PRU00405}; | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; viral genome integration into host DNA [GO:0044826] | viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; dUTP diphosphatase activity [GO:0004170]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural c... | PF00692;PF01585;PF02337;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06817;PF14787; | 1.10.10.200;1.10.1200.30;2.70.40.10;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;2.30.30.10;1.10.150.490;3.30.420.10;4.10.60.10; | Retroviral Pol polyprotein family | PTM: [Protease 17 kDa]: Released by autocatalytic processing. The protease can undergo further autoprocessing to yield 2 shorter but enzymatically active forms of 12 kDa and 13 kDa. {ECO:0000250|UniProtKB:P07572}.; PTM: [Gag-Pro-Pol polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the tran... | SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein-dUTPase]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Protease 13 kDa]: Virion {ECO:0000250|UniProtKB:P07572}.; SUBCELLULAR LOCATION: [Prote... | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=... | null | null | null | null | FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000250|UniProtKB:P07572}.; FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein. {ECO:0000250|UniProtKB:P07572}.; FUNCTION: [Capsid protein p27]: Capsid protein. {ECO:0000250|UniProtKB:P07572}.; FUNCTION: [Protease 17 kDa]: The aspartyl protease mediates proteol... | Simian retrovirus SRV-1 |
P04035 | HMDH_HUMAN | MLSRLFRMHGLFVASHPWEVIVGTVTLTICMMSMNMFTGNNKICGWNYECPKFEEDVLSSDIIILTITRCIAILYIYFQFQNLRQLGSKYILGIAGLFTIFSSFVFSTVVIHFLDKELTGLNEALPFFLLLIDLSRASTLAKFALSSNSQDEVRENIARGMAILGPTFTLDALVECLVIGVGTMSGVRQLEIMCCFGCMSVLANYFVFMTFFPACVSLVLELSRESREGRPIWQLSHFARVLEEEENKPNPVTQRVKMIMSLGLVLVHAHSRWIADPSPQNSTADTSKVSLGLDENVSKRIEPSVSLWQFYLSKMISMDI... | 1.1.1.34 | null | cholesterol biosynthetic process [GO:0006695]; coenzyme A metabolic process [GO:0015936]; ergosterol biosynthetic process [GO:0006696]; isoprenoid biosynthetic process [GO:0008299]; long-term synaptic potentiation [GO:0060291]; negative regulation of amyloid-beta clearance [GO:1900222]; negative regulation of protein c... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; peroxisomal membrane [GO:0005778] | coenzyme A binding [GO:0120225]; GTPase regulator activity [GO:0030695]; hydroxymethylglutaryl-CoA reductase (NADPH) activity [GO:0004420]; NADPH binding [GO:0070402] | PF00368;PF12349; | 1.10.3270.10;3.30.70.420; | HMG-CoA reductase family | PTM: N-glycosylated. Deglycosylated by NGLY1 on release from the endoplasmic reticulum (ER) in a sterol-mediated manner. {ECO:0000269|PubMed:19458199}.; PTM: Undergoes sterol-mediated ubiquitination and ER-associated degradation (ERAD) (PubMed:12535518, PubMed:19458199, PubMed:21778231). Accumulation of sterols in the ... | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17180682, ECO:0000305|PubMed:2991281}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00347}. Peroxisome membrane {ECO:0000269|PubMed:17180682}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00347}. | CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34; Evidence={ECO:0000269|PubMed:21357570, ECO:0000269|Pu... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13.73 uM for (3S)-hydroxy-3-methylglutaryl-CoA {ECO:0000269|PubMed:36745799}; | PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3. | null | null | FUNCTION: Catalyzes the conversion of (3S)-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to mevalonic acid, the rate-limiting step in the synthesis of cholesterol and other isoprenoids, thus plays a critical role in cellular cholesterol homeostasis (PubMed:21357570, PubMed:2991281, PubMed:36745799, PubMed:6995544). HMGCR is t... | Homo sapiens (Human) |
P04036 | DAPB_ECOLI | MHDANIRVAIAGAGGRMGRQLIQAALALEGVQLGAALEREGSSLLGSDAGELAGAGKTGVTVQSSLDAVKDDFDVFIDFTRPEGTLNHLAFCRQHGKGMVIGTTGFDEAGKQAIRDAAADIAIVFAANFSVGVNVMLKLLEKAAKVMGDYTDIEIIEAHHRHKVDAPSGTALAMGEAIAHALDKDLKDCAVYSREGHTGERVPGTIGFATVRAGDIVGEHTAMFADIGERLEITHKASSRMTFANGAVRSALWLSGKESGLFDMRDVLDLNNL | 1.17.1.8 | null | amino acid biosynthetic process [GO:0008652]; diaminopimelate biosynthetic process [GO:0019877]; lysine biosynthetic process via diaminopimelate [GO:0009089] | cytosol [GO:0005829] | 4-hydroxy-tetrahydrodipicolinate reductase [GO:0008839]; identical protein binding [GO:0042802]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor [GO:0016726] | PF05173;PF01113; | 3.40.50.720; | DapB family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=(S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH; Xref=Rhea:RHEA:35323, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16845, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:67139; EC=1.17.1.8; Evidence={ECO:0000255|HAMA... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.6 uM for NADH {ECO:0000269|PubMed:7893644, ECO:0000269|PubMed:9398235}; KM=8 uM for NADPH {ECO:0000269|PubMed:7893644, ECO:0000269|PubMed:9398235}; | PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. {ECO:0000255|HAMAP-Rule:MF_00102}. | null | null | FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. Can use both NADH and NADPH as a reductant, with NADH being twice as effective as NADPH. {ECO:0000255|HAMAP-Rule:MF_00102, ECO:0000269|PubMed:20503968, ECO:0000269|PubMed:7893644}. | Escherichia coli (strain K12) |
P04037 | COX4_YEAST | MLSLRQSIRFFKPATRTLCSSRYLLQQKPVVKTAQNLAEVNGPETLIGPGAKEGTVPTDLDQETGLARLELLGKLEGIDVFDTKPLDSSRKGTMKDPIIIESYDDYRYVGCTGSPAGSHTIMWLKPTVNEVARCWECGSVYKLNPVGVPNDDHHH | null | null | mitochondrial cytochrome c oxidase assembly [GO:0033617]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; proton transmembrane transport [GO:1902600] | mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739] | oxidoreductase activity [GO:0016491]; zinc ion binding [GO:0008270] | PF01215; | 2.60.11.10; | Cytochrome c oxidase subunit 5B family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:30598554}; Peripheral membrane protein {ECO:0000269|PubMed:30598554}; Matrix side {ECO:0000269|PubMed:30598554}. | null | null | PATHWAY: Energy metabolism; oxidative phosphorylation. | null | null | FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P04039 | COX8_YEAST | MLCQQMIRTTAKRSSNIMTRPIIMKRSVHFKDGVYENIPFKVKGRKTPYALSHFGFFAIGFAVPFVACYVQLKKSGAF | null | null | mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; proton transmembrane transport [GO:1902600] | mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739] | oxidoreductase activity [GO:0016491] | PF02935; | 4.10.49.10; | Cytochrome c oxidase VIIc family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:30598554}; Single-pass membrane protein {ECO:0000269|PubMed:30598554}. | null | null | PATHWAY: Energy metabolism; oxidative phosphorylation. | null | null | FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P04040 | CATA_HUMAN | MADSRDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNR... | 1.11.1.6 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:10656833, ECO:0000269|PubMed:10666617}; COFACTOR: Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:10656833}; | aerobic respiration [GO:0009060]; cellular detoxification of hydrogen peroxide [GO:0061692]; cellular response to growth factor stimulus [GO:0071363]; cholesterol metabolic process [GO:0008203]; hemoglobin metabolic process [GO:0020027]; hydrogen peroxide catabolic process [GO:0042744]; negative regulation of apoptotic... | catalase complex [GO:0062151]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; focal adhesion [GO:0005925]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005... | aminoacylase activity [GO:0004046]; antioxidant activity [GO:0016209]; catalase activity [GO:0004096]; enzyme binding [GO:0019899]; heme binding [GO:0020037]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; NADP binding [GO:0050661]; oxidoreductase activity, acting on peroxide as acceptor [GO:00... | PF00199;PF06628; | 2.40.180.10; | Catalase family | null | SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:21976670, ECO:0000269|PubMed:8769411}. | CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10013, ECO:0000269|PubMed:7882369}; | null | null | null | null | FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide (PubMed:7882369). Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells... | Homo sapiens (Human) |
P04041 | GPX1_RAT | MSAARLSAVAQSTVYAFSARPLAGGEPVSLGSLRGKVLLIENVASLUGTTTRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEILNSLKYVRPGGGFEPNFTLFEKCEVNGEKAHPLFTFLRNALPAPSDDPTALMTDPKYIIWSPVCRNDISWNFEKFLVGPDGVPVRRYSRRFRTIDIEPDIEALLSKQPSNP | 1.11.1.12; 1.11.1.9 | null | angiogenesis involved in wound healing [GO:0060055]; apoptotic process [GO:0006915]; arachidonic acid metabolic process [GO:0019369]; biological process involved in interaction with symbiont [GO:0051702]; blood vessel endothelial cell migration [GO:0043534]; cell redox homeostasis [GO:0045454]; cellular response to glu... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; Lewy body [GO:0097413]; mitochondrion [GO:0005739] | glutathione peroxidase activity [GO:0004602]; peroxidase activity [GO:0004601]; phospholipid-hydroperoxide glutathione peroxidase activity [GO:0047066]; SH3 domain binding [GO:0017124] | PF00255; | 3.40.30.10; | Glutathione peroxidase family | PTM: During periods of oxidative stress, Sec-47 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine. {ECO:0000250|UniProtKB:P11352}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11352}. Mitochondrion {ECO:0000250|UniProtKB:P11352}. | CATALYTIC ACTIVITY: Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O; Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9; Evidence={ECO:0000250|UniProtKB:P11352}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16834; Evidence={ECO:0000250|Uni... | null | null | null | null | FUNCTION: Catalyzes the reduction of hydroperoxides in a glutathione-dependent manner thus regulating cellular redox homeostasis. Can reduce small soluble hydroperoxides such as H2O2, cumene hydroperoxide and tert-butyl hydroperoxide, as well as several fatty acid-derived hydroperoxides. In platelets catalyzes the redu... | Rattus norvegicus (Rat) |
P04042 | CHEB_SALTY | MSKIRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLVARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVSSLTGKGSEVTLRALELGAIDFVTKPQLGIREGMLAYSEMIAEKVRTAARARIAAHKPMAAPTTLKAGPLLSSEKLIAIGASTGGTEAIRHVLQPLPLSSPAVIITQHMPPGFTRSFAERLNKLCQISVKEAEDGERVLPGHAYIAPGDKHMELARSGANYQIKIHDGPPVNRHRPSVDVLFHSVAKHAGRNAVGVILTGMGNDGAAGMLAMYQAGAWTIAQNEASCVVFGMPREAIN... | 3.1.1.61; 3.5.1.44 | null | chemotaxis [GO:0006935] | cytoplasm [GO:0005737] | phosphorelay response regulator activity [GO:0000156]; protein-glutamate methylesterase activity [GO:0008984]; protein-glutamine glutaminase activity [GO:0050568] | PF01339;PF00072; | 3.40.50.2300;3.40.50.180; | CheB family | PTM: Phosphorylated by CheA (PubMed:2677005, PubMed:3280143, PubMed:9465023). Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity (PubMed:2677005, PubMed:9760239). {ECO:0000269|PubMed:2677005, ECO:0000269|PubMed:3280143, ECO:0000269|PubMed:9465023, ECO:0000269|PubMed:9760239}.; PTM... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07330, ECO:0000255|HAMAP-Rule:MF_00099}. | CATALYTIC ACTIVITY: Reaction=[protein]-L-glutamate 5-O-methyl ester + H2O = H(+) + L-glutamyl-[protein] + methanol; Xref=Rhea:RHEA:23236, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:29973, ChEBI:CHEBI:82795; EC=3.1.1.61; Evidence={ECO:0000255|HAMAP-Ru... | null | null | null | null | FUNCTION: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR (PubMed:2677005, PubMed:29... | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P04049 | RAF1_HUMAN | MEHIQGAWKTISNGFGFKDAVFDGSSCISPTIVQQFGYQRRASDDGKLTDPSKTSNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDWSNIRQLLLFPNSTIGDSGVPALPSLTMRRMRESVSRMPVSSQHRYSTPHAFTFNTSSPSSEGSLSQRQRSTSTPNVHMVSTTLPVDSRMIEDAIRSHSESASPSALSSSPNNLSPTGWSQPKTPVPAQRERAP... | 2.7.11.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | activation of adenylate cyclase activity [GO:0007190]; apoptotic process [GO:0006915]; death-inducing signaling complex assembly [GO:0071550]; ERBB2-ERBB3 signaling pathway [GO:0038133]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; face development [GO:0060324]; insulin receptor signal... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; pseudopodium [GO:0031143] | ATP binding [GO:0005524]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00130;PF00069;PF02196; | 3.30.60.20;1.10.510.10; | Protein kinase superfamily, TKL Ser/Thr protein kinase family, RAF subfamily | PTM: Phosphorylation at Thr-269, Ser-338, Tyr-341, Thr-491 and Ser-494 results in its activation. Phosphorylation at Ser-29, Ser-43, Ser-289, Ser-296, Ser-301 and Ser-642 by MAPK1/ERK2 results in its inactivation. Phosphorylation at Ser-259 induces the interaction with YWHAZ and inactivates kinase activity. Dephosphory... | SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Mitochondrion. Nucleus. Note=Colocalizes with RGS14 and BRAF in both the cytoplasm and membranes. Phosphorylation at Ser-259 impairs its membrane accumulation. Recruited to the cell membrane by the active Ras protein. Phosphorylation at Ser-338 and Ser-339 by PAK1 is requ... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:17603483}; Physiolog... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformatio... | Homo sapiens (Human) |
P04050 | RPB1_YEAST | MVGQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETMDETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHFGHIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNELMRQALAIKDSKKRFAAIWTLCKTKMVCETDVPSEDDPTQLVSRGGCGNTQPTIRKDGLKLVGSWKKDRATGDADEPELRVLSTEEILNIFKHISVKDFTSLGFNEVFSRPEWMILTCLPVPPPPVRPSISFNESQRGEDDLTFKLADILKANISLETLEHNGAPHHAIEEAESLLQFHVATYMDNDIAGQPQALQKSGR... | 2.7.7.6 | null | RNA-templated transcription [GO:0001172]; transcription by RNA polymerase II [GO:0006366]; transcription elongation by RNA polymerase II [GO:0006368]; transcription initiation at RNA polymerase II promoter [GO:0006367]; translesion synthesis [GO:0019985] | cytoplasmic stress granule [GO:0010494]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; RNA polymerase II, core complex [GO:0005665] | DNA binding [GO:0003677]; metal ion binding [GO:0046872]; RNA polymerase II activity [GO:0001055] | PF04997;PF00623;PF04983;PF05000;PF04998;PF04992;PF04990;PF05001; | 1.10.132.30;1.10.150.390;2.40.40.20;3.30.1360.140;6.10.250.2940;6.20.50.80;3.30.1490.180;4.10.860.120;1.10.274.100; | RNA polymerase beta' chain family | PTM: The tandem 7 residues repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat. The phosphorylated form of Pol II appears to carry, on average, one phosphate per repeat. The ph... | SUBCELLULAR LOCATION: Nucleus. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; | null | null | null | null | FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the s... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P04051 | RPC1_YEAST | MKEVVVSETPKRIKGLEFSALSAADIVAQSEVEVSTRDLFDLEKDRAPKANGALDPKMGVSSSSLECATCHGNLASCHGHFGHLKLALPVFHIGYFKATIQILQGICKNCSAILLSETDKRQFLHELRRPGVDNLRRMGILKKILDQCKKQRRCLHCGALNGVVKKAAAGAGSAALKIIHDTFRWVGKKSAPEKDIWVGEWKEVLAHNPELERYVKRCMDDLNPLKTLNLFKQIKSADCELLGIDATVPSGRPETYIWRYLPAPPVCIRPSVMMQDSPASNEDDLTVKLTEIVWTSSLIKAGLDKGISINNMMEHWDYLQ... | 2.7.7.6 | null | termination of RNA polymerase III transcription [GO:0006386]; transcription by RNA polymerase III [GO:0006383]; transcription initiation at RNA polymerase III promoter [GO:0006384]; tRNA transcription by RNA polymerase III [GO:0042797] | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase III complex [GO:0005666] | DNA binding [GO:0003677]; metal ion binding [GO:0046872]; RNA polymerase III activity [GO:0001056] | PF04997;PF00623;PF04983;PF05000;PF04998; | 1.10.132.30;1.10.150.390;2.40.40.20;6.10.250.2940;6.20.50.80;3.30.1490.180;4.10.860.120;1.10.274.100; | RNA polymerase beta' chain family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; | null | null | null | null | FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase active center together with the second la... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P04052 | RPB1_DROME | MSTPTDSKAPLRQVKRVQFGILSPDEIRRMSVTEGGVQFAETMEGGRPKLGGLMDPRQGVIDRTSRCQTCAGNMTECPGHFGHIDLAKPVFHIGFITKTIKILRCVCFYCSKMLVSPHNPKIKEIVMKSRGQPRKRLAYVYDLCKGKTICEGGEDMDLTKENQQPDPNKKPGHGGCGHYQPSIRRTGLDLTAEWKHQNEDSQEKKIVVSAERVWEILKHITDEECFILGMDPKYARPDWMIVTVLPVPPLAVRPAVVMFGAAKNQDDLTHKLSDIIKANNELRKNEASGAAAHVIQENIKMLQFHVATLVDNDMPGMPRA... | 2.7.7.6 | null | transcription by RNA polymerase II [GO:0006366] | nucleus [GO:0005634]; polytene chromosome [GO:0005700]; polytene chromosome puff [GO:0005703]; RNA polymerase II, core complex [GO:0005665] | DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; metal ion binding [GO:0046872]; RNA polymerase II activity [GO:0001055] | PF04997;PF00623;PF04983;PF05000;PF04998;PF04992;PF04990; | 1.10.132.30;1.10.150.390;2.40.40.20;3.30.1360.140;6.10.250.2940;6.20.50.80;3.30.1490.180;4.10.860.120;1.10.274.100; | RNA polymerase beta' chain family | PTM: The tandem 7 residues repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat. The phosphorylation state is believed to result from the balanced action of site-specific CTD ki... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P04050}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; | null | null | null | null | FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the s... | Drosophila melanogaster (Fruit fly) |
P04053 | TDT_HUMAN | MDPPRASHLSPRKKRPRQTGALMASSPQDIKFQDLVVFILEKKMGTTRRAFLMELARRKGFRVENELSDSVTHIVAENNSGSDVLEWLQAQKVQVSSQPELLDVSWLIECIRAGKPVEMTGKHQLVVRRDYSDSTNPGPPKTPPIAVQKISQYACQRRTTLNNCNQIFTDAFDILAENCEFRENEDSCVTFMRAASVLKSLPFTIISMKDTEGIPCLGSKVKGIIEEIIEDGESSEVKAVLNDERYQSFKLFTSVFGVGLKTSEKWFRMGFRTLSKVRSDKSLKFTRMQKAGFLYYEDLVSCVTRAEAEAVSVLVKEAVW... | 2.7.7.31 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:11473582}; Note=Can also utilize other divalent cations, such as Mn(2+) and Co(2+) (in vitro). {ECO:0000250|UniProtKB:P09838, ECO:0000305}; | DNA metabolic process [GO:0006259]; DNA modification [GO:0006304]; double-strand break repair via nonhomologous end joining [GO:0006303]; response to ATP [GO:0033198] | cytosol [GO:0005829]; euchromatin [GO:0000791]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA nucleotidylexotransferase activity [GO:0003912]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872] | PF00533;PF14791;PF10391;PF14716;PF01909; | 1.10.150.20;3.30.460.10;3.40.50.10190;1.10.150.110;3.30.210.10; | DNA polymerase type-X family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16371131}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.31; Evidence={ECO:0000269|PubMed:11473582, ECO:0000269|PubMed:16371131, ECO:000026... | null | null | null | null | FUNCTION: Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments duri... | Homo sapiens (Human) |
P04054 | PA21B_HUMAN | MKLLVLAVLLTVAAADSGISPRAVWQFRKMIKCVIPGSDPFLEYNNYGCYCGLGGSGTPVDELDKCCQTHDNCYDQAKKLDSCKFLLDNPYTHTYSYSCSGSAITCSSKNKECEAFICNCDRNAAICFSKAPYNKAHKNLDTKKYCQS | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P00593}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P00593}; | actin filament organization [GO:0007015]; activation of phospholipase A2 activity [GO:0032431]; antibacterial humoral response [GO:0019731]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; arachidonic acid secretion [GO:0050482]; cellular response to insulin stimulus [GO:0032869]; ... | cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | bile acid binding [GO:0032052]; calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipase A2 activity [GO:0004623]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102] | PF00068; | 1.20.90.10; | Phospholipase A2 family | PTM: Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically. {ECO:0000269|PubMed:19297324, ECO:0000269|PubMed:6349696}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19297324}. Note=Secreted from pancreatic acinar cells in its inactive form. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract (PubMed:10681567, PubMed:1420353, PubMed:17603006). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for pho... | Homo sapiens (Human) |
P04055 | PA21B_RAT | MKLLLLAALLTAGVTAHSISTRAVWQFRNMIKCTIPGSDPLREYNNYGCYCGLGGSGTPVDDLDRCCQTHDHCYNQAKKLESCKFLIDNPYTNTYSYKCSGNVITCSDKNNDCESFICNCDRQAAICFSKVPYNKEYKDLDTKKHC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P00593}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P00593}; | antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; arachidonic acid secretion [GO:0050482]; cellular response to insulin stimulus [GO:0032869]; fatty acid biosynthetic process [GO:0006633]; innate immune response in mucosa [GO:0002227]; lipid catabolic process [GO:0016042]; phosphatid... | cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; secretory granule [GO:0030141] | bile acid binding [GO:0032052]; calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipase A2 activity [GO:0004623]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102] | PF00068; | 1.20.90.10; | Phospholipase A2 family | PTM: Activated by trypsin cleavage in the duodenum. Can also be activated by thrombin or autocatalytically. {ECO:0000250|UniProtKB:P04054}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04054}. Note=Secreted from pancreatic acinar cells in its inactive form. {ECO:0000250|UniProtKB:P04054}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract (PubMed:1420353, PubMed:17158102). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanola... | Rattus norvegicus (Rat) |
P04058 | ACES_TETCF | MNLLVTSSLGVLLHLVVLCQADDHSELLVNTKSGKVMGTRVPVLSSHISAFLGIPFAEPPVGNMRFRRPEPKKPWSGVWNASTYPNNCQQYVDEQFPGFSGSEMWNPNREMSEDCLYLNIWVPSPRPKSTTVMVWIYGGGFYSGSSTLDVYNGKYLAYTEEVVLVSLSYRVGAFGFLALHGSQEAPGNVGLLDQRMALQWVHDNIQFFGGDPKTVTIFGESAGGASVGMHILSPGSRDLFRRAILQSGSPNCPWASVSVAEGRRRAVELGRNLNCNLNSDEELIHCLREKKPQELIDVEWNVLPFDSIFRFSFVPVIDGE... | 3.1.1.7 | null | acetylcholine catabolic process in synaptic cleft [GO:0001507]; choline metabolic process [GO:0019695] | extracellular space [GO:0005615]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; synapse [GO:0045202]; synaptic cleft [GO:0043083] | acetylcholinesterase activity [GO:0003990] | PF00135; | 3.40.50.1820; | Type-B carboxylesterase/lipase family | PTM: An interchain disulfide bond is present in what becomes position 593 of the T isoform. | SUBCELLULAR LOCATION: [Isoform H]: Cell membrane; Lipid-anchor, GPI-anchor. Synapse.; SUBCELLULAR LOCATION: [Isoform T]: Cell membrane; Peripheral membrane protein. Synapse. Note=Attached to the membrane through disulfide linkage with the collagenic subunit, itself bound to the membrane. | CATALYTIC ACTIVITY: Reaction=acetylcholine + H2O = acetate + choline + H(+); Xref=Rhea:RHEA:17561, ChEBI:CHEBI:15354, ChEBI:CHEBI:15355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089; EC=3.1.1.7; | null | null | null | null | FUNCTION: Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions. | Tetronarce californica (Pacific electric ray) (Torpedo californica) |
P04062 | GBA1_HUMAN | MEFSSPSREECPKPLSRVSIMAGSLTGLLLLQAVSWASGARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLML... | 2.4.1.-; 3.2.1.-; 3.2.1.45; 3.2.1.46 | null | antigen processing and presentation [GO:0019882]; autophagosome organization [GO:1905037]; autophagy [GO:0006914]; beta-glucoside catabolic process [GO:1901805]; brain morphogenesis [GO:0048854]; cell maturation [GO:0048469]; cellular response to starvation [GO:0009267]; cellular response to tumor necrosis factor [GO:0... | endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; trans-Golgi network [GO:0005802] | galactosylceramidase activity [GO:0004336]; glucosylceramidase activity [GO:0004348]; glucosyltransferase activity [GO:0046527]; scavenger receptor binding [GO:0005124]; signaling receptor binding [GO:0005102]; steryl-beta-glucosidase activity [GO:0050295] | PF02055;PF17189; | 3.20.20.80; | Glycosyl hydrolase 30 family | null | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:17187079, ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:18022370}; Peripheral membrane protein {ECO:0000269|PubMed:10781797, ECO:0000269|PubMed:18022370, ECO:0000269|PubMed:1848227}; Lumenal side {ECO:0000269|PubMed:18022370}. Note=Interaction with saposin-C... | CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N-acylsphing-4-enine + D-glucose; Xref=Rhea:RHEA:13269, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:22801, ChEBI:CHEBI:52639; EC=3.2.1.45; Evidence={ECO:0000269|PubMed:15916907, ECO:0000269|PubMed:16293621, ECO:0000269|PubMed:2... | null | PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:26724485}.; PATHWAY: Sphingolipid metabolism. {ECO:0000269|PubMed:16293621, ECO:0000269|PubMed:24211208, ECO:0000269|PubMed:26724485, ECO:0000269|PubMed:9201993}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.3. {ECO:0000269|PubMed:24211208}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 43 degrees Celsius. {ECO:0000269|PubMed:24211208}; | FUNCTION: Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramides/GlcCers (such as beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine) into free ceramides (such as N-acylsphing-4-enine) and glucose (PubMed:15916907, PubMed:24211208, PubMed:32144204, PubMed:9201993). Plays a c... | Homo sapiens (Human) |
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