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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P03265 | DNB2_ADE05 | MASREEEQRETTPERGRGAARRPPTMEDVSSPSPSPPPPRAPPKKRMRRRIESEDEEDSSQDALVPRTPSPRPSTSAADLAIAPKKKKKRPSPKPERPPSPEVIVDSEEEREDVALQMVGFSNPPVLIKHGKGGKRTVRRLNEDDPVARGMRTQEEEEEPSEAESEITVMNPLSVPIVSAWEKGMEAARALMDKYHVDNDLKANFKLLPDQVEALAAVCKTWLNEEHRGLQLTFTSKKTFVTMMGRFLQAYLQSFAEVTYKHHEPTGCALWLHRCAEIEGELKCLHGSIMINKEHVIEMDVTSENGQRALKEQSSKAKIV... | null | null | DNA duplex unwinding [GO:0032508]; DNA unwinding involved in DNA replication [GO:0006268]; DNA-templated transcription [GO:0006351]; positive regulation of DNA replication [GO:0045740]; viral DNA genome replication [GO:0039693]; viral DNA strand displacement replication [GO:0039687] | host cell nucleus [GO:0042025]; viral capsid [GO:0019028] | DNA binding [GO:0003677]; identical protein binding [GO:0042802]; single-stranded DNA binding [GO:0003697]; zinc ion binding [GO:0008270] | PF02236;PF03728; | 3.90.148.10;1.10.269.10; | Adenoviridae E2A DNA-binding protein family | null | SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04054}. Note=Accumulates in infected cells. {ECO:0000255|HAMAP-Rule:MF_04054}. | null | null | null | null | null | FUNCTION: Plays a role in the elongation phase of viral strand displacement replication by unwinding the template in an ATP-independent fashion, employing its capacity to form multimers. Also enhances the rate of initiation. Released from template upon second strand synthesis. Assembles in complex with viral pTP, viral... | Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5) |
P03269 | TERM_ADE02 | MALSVNDCARLTGQSVPTMEHFLPLRNIWNRVRDFPRASTTAAGITWMSRYIYGYHRLMLEDLAPGAPATLRWPLYRQPPPHFLVGYQYLVRTCNDYVFDSRAYSRLRYTELSQPGHQTVNWSVMANCTYTINTGAYHRFVDMDDFQSTLTQVQQAILAERVVADLALLQPMRGFGVTRMGGRGRHLRPNSAAAVAIDARDAGQEEGEEEVPVERLMQDYYKDLRRCQNEAWGMADRLRIQQAGPKDMVLLSTIRRLKTAYFNYIISSTSARNNPDRHPLPPATVLSLPCDCDWLDAFLERFSDPVDADSLRSLGGGVPT... | null | null | DNA replication [GO:0006260]; viral DNA strand displacement replication [GO:0039687] | host cell nuclear matrix [GO:0044204]; host cell nucleus [GO:0042025] | double-stranded DNA binding [GO:0003690]; single-stranded DNA binding [GO:0003697] | PF02459; | null | Adenoviridae terminal protein family | PTM: Preterminal protein is used to replicate viral genome, upon genomic encapsidation it is processed first into iTP and finally into TP by adenovirus protease. {ECO:0000255|HAMAP-Rule:MF_04061, ECO:0000269|PubMed:9261355}. | SUBCELLULAR LOCATION: Host nucleus matrix {ECO:0000255|HAMAP-Rule:MF_04061}. | null | null | null | null | null | FUNCTION: Protein covalently bound to the viral DNA that acts as a primer for viral genomic replication by DNA strand displacement. Assembles on the viral origin of replication in an initiation complex with viral polymerase, DBP, host NFIA and host POU2F1/OCT1. During initiation, the polymerase covalently couples the f... | Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2) |
P03272 | PKG1_ADE02 | METRGRRPAALQHQQDQPQAHPGQRAARSAPLHRDPDYADEDPAPVERHDPGPSGRAPTTAVQRKPPQPAKRGDMLDRDAVEHVTELWDRLELLGQTLKSMPTADGLKPLKNFASLQELLSLGGERLLAHLVRENMQVRDMLNEVAPLLRDDGSCSSLNYQLQPVIGVIYGPTGCGKSQLLRNLLSSQLISPTPETVFFIAPQVDMIPPSELKAWEMQICEGNYAPGPDGTIIPQSGTLRPRFVKMAYDDLILEHNYDVSDPRNIFAQAAARGPIAIIMDECMENLGGHKGVSKFFHAFPSKLHDKFPKCTGYTVLVVLH... | null | null | DNA-templated transcription [GO:0006351]; nuclear capsid assembly [GO:0039708]; regulation of DNA-templated transcription [GO:0006355]; viral DNA genome packaging [GO:0019073]; viral DNA genome packaging via site-specific sequence recognition [GO:0098035]; viral release from host cell [GO:0019076]; viral transcription ... | host cell nucleolus [GO:0044196]; host cell nucleoplasm [GO:0044095]; virion component [GO:0044423] | ATP binding [GO:0005524]; DNA binding [GO:0003677] | PF02456; | null | Adenoviridae packaging protein 1 family | null | SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04057, ECO:0000269|PubMed:18614642}. Host nucleus, host nucleoplasm {ECO:0000255|HAMAP-Rule:MF_04057, ECO:0000269|PubMed:8627656}. Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04057, ECO:0000269|PubMed:8627656}. Note=Located at a unique vertex of the ca... | null | null | null | null | null | FUNCTION: Component of the packaging machinery which encapsidates the viral DNA into preformed capsids and transcriptional activator of the viral major late promoter (MLP). Binds, along with packaging proteins 2 and 3, to the specific packaging sequence on the left end of viral genomic DNA and displays ATPase activity ... | Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2) |
P03274 | CAP6_ADE02 | MEDINFASLAPRHGSRPFMGNWQDIGTSNMSGGAFSWGSLWSGIKNFGSTIKNYGSKAWNSSTGQMLRDKLKEQNFQQKVVDGLASGISGVVDLANQAVQNKINSKLDPRPPVEEPPPAVETVSPEGRGEKRPRPDREETLVTQIDEPPSYEEALKQGLPTTRPIAPMATGVLGQHTPVTLDLPPPADTQQKPVLPGPSAVVVTRPSRASLRRAASGPRSMRPVASGNWQSTLNSIVGLGVQSLKRRRCF | null | null | lysis of host organelle involved in viral entry into host cell [GO:0039664]; microtubule-dependent intracellular transport of viral material towards nucleus [GO:0075521]; nuclear capsid assembly [GO:0039708]; viral release from host cell [GO:0019076] | host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; viral capsid [GO:0019028]; viral procapsid [GO:0046729] | null | PF02993; | null | Adenoviridae protein VI family | PTM: Ubiquitinated by Nedd4 following partial capsid disassembly; which might play a role in intracellular virus movement during entry. {ECO:0000255|HAMAP-Rule:MF_04048}.; PTM: [Protease cofactor]: Contains the major nuclear import and export signals. Proteolytically removed during virion maturation. The processing of ... | SUBCELLULAR LOCATION: [Pre-protein VI]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04048}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04048}. Note=Shuttles between host cytoplasm and nucleus. {ECO:0000255|HAMAP-Rule:MF_04048}.; SUBCELLULAR LOCATION: [Endosome lysis protein]: Virion {ECO:0000255|HAMAP-Rule:MF_04048}. Note=A... | null | null | null | null | null | FUNCTION: [Pre-protein VI]: During virus assembly, promotes hexon trimers nuclear import through nuclear pore complexes via an importin alpha/beta-dependent mechanism. By analogy to herpesviruses capsid assembly, might act as a chaperone to promote the formation of the icosahedral capsid. {ECO:0000255|HAMAP-Rule:MF_040... | Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2) |
P03300 | POLG_POL1M | MGAQVSSQKVGAHENSNRAYGGSTINYTTINYYRDSASNAASKQDFSQDPSKFTEPIKDVLIKTAPMLNSPNIEACGYSDRVLQLTLGNSTITTQEAANSVVAYGRWPEYLRDSEANPVDQPTEPDVAACRFYTLDTVSWTKESRGWWWKLPDALRDMGLFGQNMYYHYLGRSGYTVHVQCNASKFHQGALGVFAVPEMCLAGDSNTTTMHTSYQNANPGEKGGTFTGTFTPDNNQTSPARRFCPVDYLLGNGTLLGNAFVFPHQIINLRTNNCATLVLPYVNSLSIDSMVKHNNWGIAILPLAPLNFASESSPEIPITL... | 2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15 | COFACTOR: [RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:21148772}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (PubMed:21148772). The magnesium ions are not prebound but only present for catalysis (PubMed:21148772). Requires the prese... | DNA-templated transcription [GO:0006351]; endocytosis involved in viral entry into host cell [GO:0075509]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:0039522]; symbiont genome entry ... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [G... | PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;6.10.20.20;4.10.880.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000269|PubMed:8097606}.; PTM: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly (PubMed:1850017, PubMed:1851815). Furth... | SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000269|PubMed:1851815}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000269|PubMed:1... | CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]: 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}; CATALY... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=642 uM for ATP {ECO:0000269|PubMed:30231078}; Note=For protein 2C ATPase activity. {ECO:0000269|PubMed:30231078}; | null | null | null | FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (PubMed:2994218). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (PubMed:2994218). Capsid protein VP1 mainly forms... | Poliovirus type 1 (strain Mahoney) |
P03301 | POLG_POL1S | MGAQVSSQKVGAHENSNRAYGGSTINYTTINYYRDSASNAASKQDFSQDPSKFTEPIKDVLIKTSPMLNSPNIEACGYSDRVLQLTLGNSTITTQEAANSVVAYGRWPEYLRDSEANPVDQPTEPDVAACRFYTLDTVSWTKESRGWWWKLPDALRDMGLFGQNMYYHYLGRSGYTVHVQCNASKFHQGALGVFAVPEMCLAGDSNTTTMHTSYQNANPGEKGGTFTGTFTPDDNQTSPARRFCPVDYLFGNGTLLGNAFVFPHQIINLRTNNCATLVLPYVNSLSIDSMVKHNNWGIAILPLAPLNFASESSPEIPITL... | 2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15 | COFACTOR: [RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence... | DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; receptor-mediated endocytosis of virus by host cell [GO:0019065]; suppression by virus of host mRNA export from nucleus [GO:0... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [G... | PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;6.10.20.20;4.10.880.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000269|PubMed:3011278}.; PTM: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a... | SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniPro... | CATALYTIC ACTIVITY: [Protein 2C]: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACT... | null | null | null | null | FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms t... | Poliovirus type 1 (strain Sabin) |
P03302 | POLG_POL3L | MGAQVSSQKVGAHENSNRAYGGSTINYTTINYYKDSASNAASKQDYSQDPSKFTEPLKDVLIKTAPALNSPNVEACGYSDRVLQLTLGNSTITTQEAANSVVAYGRWPEFIRDDEANPVDQPTEPDVATCRFYTLDTVMWGKESKGWWWKLPDALRDMGLFGQNMYYHYLGRSGYTVHVQCNASKFHQGALGVFAIPEYCLAGDSDKQRYTSYANANPGERGGKFYSQFNKDNAVTSPKREFCPVDYLLGCGVLLGNAFVYPHQIINLRTNNSATIVLPYVNALAIDSMVKHNNWGIAILPLSPLDFAQDSSVEIPITVT... | 2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15 | COFACTOR: [RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence... | caveolin-mediated endocytosis of virus by host cell [GO:0075513]; DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:0... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [G... | PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;6.10.20.20;4.10.880.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and... | SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniPro... | CATALYTIC ACTIVITY: [Protein 2C]: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACT... | null | null | null | null | FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms t... | Poliovirus type 3 (strains P3/Leon/37 and P3/Leon 12A[1]B) |
P03303 | POLG_HRV14 | MGAQVSTQKSGSHENQNILTNGSNQTFTVINYYKDAASTSSAGQSLSMDPSKFTEPVKDLMLKGAPALNSPNVEACGYSDRVQQITLGNSTITTQEAANAVVCYAEWPEYLPDVDASDVNKTSKPDTSVCRFYTLDSKTWTTGSKGWCWKLPDALKDMGVFGQNMFFHSLGRSGYTVHVQCNATKFHSGCLLVVVIPEHQLASHEGGNVSVKYTFTHPGERGIDLSSANEVGGPVKDVIYNMNGTLLGNLLIFPHQFINLRTNNTATIVIPYINSVPIDSMTRHNNVSLMVIPIAPLTVPTGATPSLPITVTIAPMCTEF... | 2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15 | COFACTOR: [RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence... | DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; endocytosis involved in viral entry into host cell [GO:0075509]; induction by virus of host autophagy [GO:0039520]; lysis of host organelle involved in viral entry into host cell [GO:0039664]; protein complex oligomerization [GO:0051259]; proteolys... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural mo... | PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.80.10;6.10.20.20;4.10.880.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and... | SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniPro... | CATALYTIC ACTIVITY: [Protein 2C]: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACT... | null | null | null | null | FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms the vertices of t... | Human rhinovirus 14 (HRV-14) |
P03304 | POLG_EMCV | MATTMEQETCAHSLTFEECPKCSALQYRNGFYLLKYDEEWYPEELLTDGEDDVFDPELDMEVVFELQGNSTSSDKNNSSSEGNEGVIINNFYSNQYQNSIDLSANAAGSDPPRLRSIFESLSGAVNAFSNMLPLLADQNTEEMENLSDRGLKTLPAIRSQTPSQQWAVLSVMVPFMMESIRHHVLTLLQKRFWRWKGTTPSRLMIGHQHKSPLSTSAFPFLTSCPVKMVVSLVALRRHYLVKTGWRVQVQCNASQFHAGGLLVFMAPEYPTLDAFAMDNRWSKDNLPNGTRTQTNKKGPFAMDHQNFWQWTLYPHQFLNL... | 2.7.7.48; 3.4.22.28; 3.6.4.13 | null | DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:0039522]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host cytop... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleolus [GO:0044196]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural mo... | PF00548;PF00680;PF00073;PF00910;PF08935;PF11475; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.90.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Leader protein]: Phosphorylated. {ECO:0000250|UniProtKB:Q66765}.; PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (PubMed:3467351, PubMed:6324136). The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by... | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P12296}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:P12296}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:P12296}. Host cyto... | 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: [Leader protein]: Forms a complex with host RAN and probably binds to exportins carrying activated MAPK in order to mediate the hyperphosphorylation of host Phe/Gly containing nuclear pore proteins (Nups) resulting in cessation of active nucleocytoplasmic transport (By similarity). Proteins with NLS signals f... | Encephalomyocarditis virus |
P03305 | POLG_FMDVO | MNTTDCFIALVQAIREIKALFLSRTTGKMELTLYNGEKKTFYSRPNNHDNCWLNAILQLFRYVEEPFFDWVYSSPENLTLEAIKQLEDLTGLELHEGGPPALVIWNIKHLLHTGIGTASRPSEVCMVDGTDMCLADFHAGIFLKGQEHAVFACVTSNGWYAIDDEDFYPWTPDPSDVLVFVPYDQEPLNGEWKAKVQRKLKGAGQSSPATGSQNQSGNTGSIINNYYMQQYQNSMDTQLGDNAISGGSNEGSTDTTSTHTTNTQNNDWFSKLASSAFSGLFGALLADKKTEETTLLEDRILTTRNGHTTSTTQSSVGVTY... | 2.7.7.48; 3.4.22.28; 3.4.22.46; 3.6.1.15 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; modulation by virus of host chromatin organization [GO:0039525]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; regulation of translati... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; molecular adaptor activity [GO:0060090]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase ac... | PF05408;PF00548;PF00680;PF00073;PF00910;PF08935; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.90.10;3.90.70.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Leader protease]: Removes six residues from its own C-terminus, generating sLb(pro). {ECO:0000269|PubMed:25240326}.; PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. The polyprotein seems to be cotranslationally cleaved at th... | SUBCELLULAR LOCATION: [Leader protease]: Host nucleus {ECO:0000269|PubMed:17881445}. Host cytoplasm {ECO:0000269|PubMed:17881445}.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000269|PubMed:2537470}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000269|PubMed:25374... | CATALYTIC ACTIVITY: Reaction=Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.; EC=3.4.22.46; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate... | null | null | null | null | FUNCTION: [Leader protease]: Autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. Also cleaves the host translation initiation factors EIF4G1 and EIF4G3, in order to shut off the capped cellular mRNA transcription. Plays a role in counteracting host innate antiviral response using diverse mechan... | Foot-and-mouth disease virus (isolate Bovine/Germany/O1Kaufbeuren/1966 serotype O) (FMDV) |
P03306 | POLG_FMDV1 | MNTTNCFIALVYLIREIKTLFRSRTKGKMEFTLHNGEKKTFYSRPNNHDNCWLNTILQLFRYVDEPFFDWVYNSPENLTLDAIKQLENFTGLELHEGGPPALVIWNIKHLLQTGIGTASRPSEVCMVDGTDMCLADFHAGIFMKGQEHAVFACVTSDGWYAIDDEDFYPWTPDPSDVLVFVPYDQEPLNGDWKTQVQKKLKGAGQSSPATGSQNQSGNTGSIINNYYMQQYQNSMSTQLGDNTISGGSNEGSTDTTSTHTTNTQNNDWFSKLASSAFTGLFGALLADKKTEETTLLEDRILTTRNGHTTSTTQSSVGVTY... | 2.7.7.48; 3.4.22.28; 3.4.22.46; 3.6.1.15 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; modulation by virus of host chromatin organization [GO:0039525]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; regulation of translati... | host cell cytoplasmic vesicle membrane [GO:0044162]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule ... | PF05408;PF00548;PF00680;PF00073;PF00910;PF08935; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.90.10;3.90.70.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This matur... | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane {... | CATALYTIC ACTIVITY: Reaction=Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.; EC=3.4.22.46; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate... | null | null | null | null | FUNCTION: [Leader protease]: Autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. Also cleaves the host translation initiation factors EIF4G1 and EIF4G3, in order to shut off the capped cellular mRNA transcription. Plays a role in counteracting host innate antiviral response using diverse mechan... | Foot-and-mouth disease virus (strain A10-61) (Aphthovirus A) (FMDV) |
P03307 | POLG_FMDV5 | MHTTDCFIALVHAIREIRALFLPRTTGKMELTLHNGEKKTFYSRPNNHDNCWLNTILQLFRYVDEPFFDWVYNSPENLTLEAINQLEELTGLELHEGGPPALVIWNIKHLLHTGIGTASRPSEVCMVDGTDMCLADFHAGIFLKGQEHAVFACVTSNGWYAIDDEEFYPWTPDPSDVLVFVPYDQEPLNGDWKAMVQRKLKGAGQSSPATGSQNQSGNTGSIINNYYMQQYQNSMDTQLGDNAISGGSNEGSTDTTSTHTTNTQNNDWFSKLASSAFTGLFGALLADKKTEETTLLEDRILTTRNGHTISTTQSSVGVTY... | 2.7.7.48; 3.4.22.28; 3.4.22.46; 3.6.1.15 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; modulation by virus of host chromatin organization [GO:0039525]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; regulation of translati... | host cell cytoplasmic vesicle membrane [GO:0044162]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule ... | PF05408;PF00548;PF00680;PF00073;PF00910;PF08935; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.90.10;3.90.70.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This matur... | SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane {... | CATALYTIC ACTIVITY: Reaction=Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.; EC=3.4.22.46; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate... | null | null | null | null | FUNCTION: [Leader protease]: Autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. Also cleaves the host translation initiation factors EIF4G1 and EIF4G3, in order to shut off the capped cellular mRNA transcription. Plays a role in counteracting host innate antiviral response using diverse mechan... | Foot-and-mouth disease virus (isolate -/Germany/A5Westerwald/1951 serotype A) (FMDV) |
P03308 | POLG_FMDVA | MNTTNCFIALVHAIREIRAFFLSRATGKMEFTLYNGERKTFYSRPNNHDNCWLNTILQLFRYVDEPFFDWVYNSPENLTLAAIKQLEELTGLELHEGGPPALVIWNIKHLLQTGIGTASRPSEVCMVDGTDMCLADFHAGIFLKGQEHAVFACVTSNGWYAIDDEDFYPWTPDPSDVLVFVPYDQEPLNGGWKANVQRKLKGAGQSSPATGSQNQSGNTGSIINNYYMQQYQNSMDTQLGDNAISGGSNEGSTDTTSTHTTNTQNNDWFSKLASSAFTGLFGALLADKKTEETTLLEDRILTTRNGHTTSTTQSSVGVTY... | 2.7.7.48; 3.4.22.28; 3.4.22.46; 3.6.1.15 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; modulation by virus of host chromatin organization [GO:0039525]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; regulation of translati... | host cell cytoplasmic vesicle membrane [GO:0044162]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule ... | PF05408;PF00548;PF00680;PF00073;PF00910;PF08935; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.90.10;3.90.70.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This matur... | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion. Host cytoplasm {ECO:0000269|PubMed:30404792}.; SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic ve... | CATALYTIC ACTIVITY: Reaction=Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.; EC=3.4.22.46; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate... | null | null | null | null | FUNCTION: [Leader protease]: Autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. Also cleaves the host translation initiation factors EIF4G1 and EIF4G3, in order to shut off the capped cellular mRNA transcription. Plays a role in counteracting host innate antiviral response using diverse mechan... | Foot-and-mouth disease virus (isolate Bovine/United Kingdom/A12Valle119/1932 serotype A) (FMDV) |
P03309 | POLG_FMDVC | MNTTDCFIALVHAIREIRAFFLPRATGRMEFTLHNGERKVFYSRPNNHDNCWLNTILQLFRYVGEPFFDWVYDSPENLTLEAIEQLEELTGLELHEGGPPALVIWNIKHLLHTGIGTASRPSEVCMVDGTNMCLADFHAGIFLKGQEHAVFACVTSNGWYAIDDEDFYPWTPDPSDVLVFVPYDQEPLNGEWKTKVQQKLKGAGQSSPATGSQNQSGNTGSIINNYYMQQYQNSMDTQLGDNAISGGSNEGSTDTTSTHTTNTQNNDWFSKLASSAFTGLFGALLADKKTEETTLLEDRILTTRNGHTTSTTQSSVGVTH... | 2.7.7.48; 3.4.22.28; 3.4.22.46; 3.6.1.15 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; modulation by virus of host chromatin organization [GO:0039525]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; regulation of translati... | host cell cytoplasmic vesicle membrane [GO:0044162]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule ... | PF05408;PF00548;PF00680;PF00073;PF00910;PF08935; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.90.10;3.90.70.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This matur... | SUBCELLULAR LOCATION: [Protein VP2]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane {ECO:000... | CATALYTIC ACTIVITY: Reaction=Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.; EC=3.4.22.46; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate... | null | null | null | null | FUNCTION: [Leader protease]: Autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. Also cleaves the host translation initiation factors EIF4G1 and EIF4G3, in order to shut off the capped cellular mRNA transcription. Plays a role in counteracting host innate antiviral response using diverse mechan... | Foot-and-mouth disease virus (isolate Bovine/Brazil/A24Cruzeiro/1955 serotype A) (FMDV) |
P03310 | POLG_FMDVI | MNTTDCFIALVHAIREIKTHFFSRYTGRMEFTLHNGEKKIFYSRPNNHDNCWLNTILQLFRYVDEPFFDWVYNSPENLTLSAIEQLEKLTGLELREGGPPALVIWNIKHLLHTGIGTASRPSEVCMVDGTDMCLADFHAGIFLKGQEHAVFACVTSDGWYAIDDEDFYPWTPDPSDVLVFVPYDQEPLNGGWKANVQRKLKGAGQSSPATGSQNQSGNTGSIINNYYMQQYQNSMDTQLGDNAISGGSNEGSTDTTSTHTTNTQNNDWFSKLASSAFSGLFGALLADKKTEETTLLEDRILTTRNGHTTSTTQSSVGVTY... | 2.7.7.48; 3.4.22.28; 3.4.22.46; 3.6.1.15 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; modulation by virus of host chromatin organization [GO:0039525]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; regulation of translati... | host cell cytoplasmic vesicle membrane [GO:0044162]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule ... | PF05408;PF00548;PF00680;PF00073;PF00910;PF08935; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.90.10;3.90.70.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This matur... | SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane {... | CATALYTIC ACTIVITY: Reaction=Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.; EC=3.4.22.46; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate... | null | null | null | null | FUNCTION: [Leader protease]: Autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. Also cleaves the host translation initiation factors EIF4G1 and EIF4G3, in order to shut off the capped cellular mRNA transcription. Plays a role in counteracting host innate antiviral response using diverse mechan... | Foot-and-mouth disease virus (isolate -/Brazil/C3Indaial/1971 serotype C) (FMDV) |
P03311 | POLG_FMDVS | MNTTDCFIAVVNAIKEVRALFLPRTAGKMEFTLHDGEKKVFYSRPNNHDNCWLNTILQLFRYVDEPFFDWVYNSPENLTLEAIKQLEELTGLELREGGPPALVIWNIKHLLHTGIGTASRPSEVCMVDGTDMCLADFHAGIFMKGREHAVFACVTSNGWYAIDDEDFYPWTPDPSDVLVFVPYDQEPLNEGWKASVQRKLKGAGQSSPATGSQNQSGNTGSIINNYYMQQYQNSMDTQLGDNAISGGSNEGSTDTTSTHTTNTQNNDWFSKLASSAFSGLFGALLADKKTEETTLLEDRILTTRNGHTTSTTQSSVGVTF... | 2.7.7.48; 3.4.22.28; 3.4.22.46; 3.6.1.15 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; modulation by virus of host chromatin organization [GO:0039525]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; regulation of translati... | host cell cytoplasmic vesicle membrane [GO:0044162]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule ... | PF05408;PF00548;PF00680;PF00073;PF00910;PF08935; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.90.10;3.90.70.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This matur... | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane {... | CATALYTIC ACTIVITY: Reaction=Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.; EC=3.4.22.46; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate... | null | null | null | null | FUNCTION: [Leader protease]: Autocatalytically cleaves itself from the polyprotein at the L/VP0 junction. Also cleaves the host translation initiation factors EIF4G1 and EIF4G3, in order to shut off the capped cellular mRNA transcription. Plays a role in counteracting host innate antiviral response using diverse mechan... | Foot-and-mouth disease virus (isolate -/Spain/S8c1SantaPau/1970 serotype C) (FMDV) |
P03313 | POLG_CXB3N | MGAQVSTQKTGAHETRLNASGNSIIHYTNINYYKDAASNSANRQDFTQDPGKFTEPVKDIMIKSLPALNSPTVEECGYSDRARSITLGNSTITTQECANVVVGYGVWPDYLKDSEATAEDQPTQPDVATCRFYTLDSVQWQKTSPGWWWKLPDALSNLGLFGQNMQYHYLGRTGYTVHVQCNASKFHQGCLLVVCVPEAEMGCATLDNTPSSAELLGGDTAKEFADKPVASGSNKLVQRVVYNAGMGVGVGNLTIFPHQWINLRTNNSATIVMPYTNSVPMDNMFRHNNVTLMVIPFVPLDYCPGSTTYVPITVTIAPMC... | 2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15 | COFACTOR: [RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:18632861, ECO:0000269|PubMed:23667424}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By simila... | DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; endocytosis involved in viral entry into host cell [GO:0075509]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:00... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural mo... | PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.80.10;6.10.20.20;4.10.880.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and... | SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniPro... | CATALYTIC ACTIVITY: [Protein 2C]: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACT... | null | null | null | null | FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms t... | Coxsackievirus B3 (strain Nancy) |
P03314 | POLG_YEFV1 | MSGRKAQGKTLGVNMVRRGVRSLSNKIKQKTKQIGNRPGPSRGVQGFIFFFLFNILTGKKITAHLKRLWKMLDPRQGLAVLRKVKRVVASLMRGLSSRKRRSHDVLTVQFLILGMLLMTGGVTLVRKNRWLLLNVTSEDLGKTFSVGTGNCTTNILEAKYWCPDSMEYNCPNLSPREEPDDIDCWCYGVENVRVAYGKCDSAGRSRRSRRAIDLPTHENHGLKTRQEKWMTGRMGERQLQKIERWFVRNPFFAVTALTIAYLVGSNMTQRVVIALLVLAVGPAYSAHCIGITDRDFIEGVHGGTWVSATLEQDKCVTVMA... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity [GO:0039564]; symbion... | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; protein dimerization act... | PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949; | 1.10.10.930;1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;3.40.50.150;3.30.67.10;3.30.387.10; | Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. The nascent capsid protein C contains a C-terminal hydrophobic domain that act as a signal sequence for translocation of prM into the lumen of the ER. Mature capsid protein C is cleaved at a site upstream of this hydrophobic domain b... | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763... | CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; Evidence={ECO:0000269|PubMed:21419753}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9. {ECO:0000269|PubMed:21419753}; | null | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migr... | Yellow fever virus (strain 17D vaccine) (YFV) |
P03315 | POLS_SFV | MNYIPTQTFYGRRWRPRPAARPWPLQATPVAPVVPDFQAQQMQQLISAVNALTMRQNAIAPARPPKPKKKKTTKPKPKTQPKKINGKTQQQKKKDKQADKKKKKPGKRERMCMKIENDCIFEVKHEGKVTGYACLVGDKVMKPAHVKGVIDNADLAKLAFKKSSKYDLECAQIPVHMRSDASKYTHEKPEGHYNWHHGAVQYSGGRFTIPTGAGKPGDSGRPIFDNKGRVVAIVLGGANEGSRTALSVVTWNKDMVTRVTPEGSEEWSAPLITAMCVLANATFPCFQPPCVPCCYENNAEATLRMLEDNVDRPGYYDLLQ... | 3.4.21.90 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; proteolysis [GO:0006508]; symbiont-mediated suppression of host toll-like receptor signaling pathway [GO:0039722]; virion assembly [GO:0019068]; virion attachment to host cell [GO:001906... | host cell endosome [GO:0044174]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; T=4 icosahedral viral capsid [GO:0039619]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; serine-type endopeptidase activity [GO:0004252]; small molecule binding [GO:0036094]; structural molecule activity [GO:0005198] | PF01589;PF00943;PF01563;PF00944; | 1.10.287.2230;2.60.40.350;2.60.40.3200;2.60.40.4310;2.60.40.2400;2.60.98.10;2.40.10.10; | null | PTM: [Isoform Structural polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Capsid protein is auto-cleaved during polyprotein translation, unmasking a signal peptide at the N-terminus of the precursor of E3/E2 (PubMed:3553612). The remaining polyprotein is then targeted to the host endoplasmic re... | SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000250|UniProtKB:P03316}. Host cytoplasm {ECO:0000250|UniProtKB:Q8JUX5}. Host cell membrane {ECO:0000250|UniProtKB:P03316}. Host nucleus {ECO:0000250|UniProtKB:Q8JUX5}. Note=Shuttles between the cytoplasm and the nucleus. {ECO:0000250|UniProtKB:Q8JUX5}.; SUBCELLULAR ... | CATALYTIC ACTIVITY: Reaction=Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.; EC=3.4.21.90; Evidence={ECO:0000269|PubMed:3553612}; | null | null | null | null | FUNCTION: [Capsid protein]: Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers (By similarity). The capsid protein binds to the viral RNA genome at a site adjacent to a ri... | Semliki forest virus (SFV) |
P03316 | POLS_SINDV | MNRGFFNMLGRRPFPAPTAMWRPRRRRQAAPMPARNGLASQIQQLTTAVSALVIGQATRPQPPRPRPPPRQKKQAPKQPPKPKKPKTQEKKKKQPAKPKPGKRQRMALKLEADRLFDVKNEDGDVIGHALAMEGKVMKPLHVKGTIDHPVLSKLKFTKSSAYDMEFAQLPVNMRSEAFTYTSEHPEGFYNWHHGAVQYSGGRFTIPRGVGGRGDSGRPIMDNSGRVVAIVLGGADEGTRTALSVVTWNSKGKTIKTTPEGTEEWSAAPLVTAMCLLGNVSFPCDRPPTCYTREPSRALDILEENVNHEAYDTLLNAILRC... | 3.4.21.90 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; membrane fusion [GO:0061025]; proteolysis [GO:0006508]; symbiont-mediated suppression of host toll-like receptor signaling pathway [GO:0039722]; virion attachment to host cell [GO:001906... | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; icosahedral viral capsid, spike [GO:0098029]; membrane [GO:0016020]; T=4 icosahedral viral capsid [GO:0039619]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198]; ubiquitin-like protein ligase binding [GO:0044389] | PF01589;PF00943;PF01563;PF00944; | 1.10.287.2230;2.60.40.350;2.60.40.3200;2.60.40.4310;2.60.40.2400;2.60.98.10;2.40.10.10; | Alphavirus structural polyprotein family | PTM: [Isoform Structural polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Capsid protein is auto-cleaved during polyprotein translation, unmasking a signal peptide at the N-terminus of the precursor of E3/E2 (PubMed:2335827). The remaining polyprotein is then targeted to the host endoplasmic re... | SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000269|PubMed:3829124}. Host cytoplasm {ECO:0000269|PubMed:23785213}. Host cell membrane {ECO:0000269|PubMed:23785213}. Host nucleus {ECO:0000250|UniProtKB:Q8JUX5}. Note=Shuttles between the cytoplasm and the nucleus. {ECO:0000250|UniProtKB:Q8JUX5}.; SUBCELLULAR LOCA... | CATALYTIC ACTIVITY: Reaction=Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.; EC=3.4.21.90; Evidence={ECO:0000250|UniProtKB:P03315}; | null | null | null | null | FUNCTION: [Capsid protein]: Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers (PubMed:8415660). The capsid protein binds to the viral RNA genome at a site adjacent to a r... | Sindbis virus (SINV) |
P03317 | POLN_SINDV | MEKPVVNVDVDPQSPFVVQLQKSFPQFEVVAQQVTPNDHANARAFSHLASKLIELEVPTTATILDIGSAPARRMFSEHQYHCVCPMRSPEDPDRMMKYASKLAEKACKITNKNLHEKIKDLRTVLDTPDAETPSLCFHNDVTCNMRAEYSVMQDVYINAPGTIYHQAMKGVRTLYWIGFDTTQFMFSAMAGSYPAYNTNWADEKVLEARNIGLCSTKLSEGRTGKLSIMRKKELKPGSRVYFSVGSTLYPEHRASLQSWHLPSVFHLNGKQSYTCRCDTVVSCEGYVVKKITISPGITGETVGYAVTHNSEGFLLCKVTD... | 2.1.1.-; 2.7.7.-; 2.7.7.19; 2.7.7.48; 3.1.3.84; 3.4.22.-; 3.6.1.15; 3.6.1.74; 3.6.4.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17005674}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17005674}; Note=For nsP4 adenylyltransferase activity; Mn(2+) supports catalysis at 60% of the levels observed with Mg(2+). {ECO:0000269|PubMed:17005674}; COFACTOR: Na... | 7-methylguanosine mRNA capping [GO:0006370]; DNA-templated transcription [GO:0006351]; positive stranded viral RNA replication [GO:0039690]; proteolysis [GO:0006508]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host mRNA transcri... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell filopodium [GO:0044176]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type peptidase activity [GO:0008234]; GTP binding [GO:0005525]; metal ion binding [GO:0046872]; mRNA 5'-phosphatase activity [GO:0140818]; mRNA methyltransferase activity [GO:0008174]; O-acetyl-ADP-ribose deacetylase activity [GO:0061463]; poly(A)... | PF01661;PF20852;PF01707;PF00978;PF20896;PF01443;PF01660; | 3.90.70.110;3.40.220.10;3.40.50.300;3.40.50.150; | null | PTM: [Polyprotein P1234]: Specific enzymatic cleavages in vivo yield mature proteins (PubMed:2142454, PubMed:8107248). The processing of the polyprotein is temporally regulated (PubMed:2142454). In early stages (1.7 hpi), P1234 is first cleaved in trans through its nsP2 protease activity, releasing P123' and nsP4, whic... | SUBCELLULAR LOCATION: [Polyprotein P1234]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex. {E... | CATALYTIC ACTIVITY: Reaction=GTP + S-adenosyl-L-methionine = N(7)-methyl-GTP + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:46948, ChEBI:CHEBI:37565, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:87133; Evidence={ECO:0000250|UniProtKB:P27282}; CATALYTIC ACTIVITY: Reaction=L-histidyl-[protein] + N(7)-methyl-GTP = dipho... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.5 for nsP4 polymerase and adenylyltransferase activities. {ECO:0000269|PubMed:17005674, ECO:0000269|PubMed:19036396}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25 degrees Celsius for nsP4 adenylyltransferase activity. {ECO:0000269|PubMed:17005674}; | FUNCTION: [Polyprotein P1234]: Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2. {ECO:0000250|UniProtKB:Q8JUX6}.; FUNCTION: [Polyprotein P123]: The early replication complex formed by the polyprotein P123 and nsP4 synthesizes minus-strand RNAs (PubMed:751... | Sindbis virus (SINV) |
P03318 | POLN_MIDDV | DADLAAVYRAVASLADETVRTMAIPLLSTGTFAGGKDRVLQSLNHLFTALDTTDVDVTIYCRDKSWEKKIQEAIDMRTATELLDDDTTVMKELTRVHPDSCLVGRSGFSTVDGRLHSYLEGTRFHQTAVDVAERPTLWPRREEANEQITHYVLGESMEAIRTKCPVDDTDSSAPPCTVPCLCRYAMTPERVHRLRAAQVKQFTVCSSFPLPKYKIPGVQRVACSAVMLFNHDVPALVSPRKYREPSISSESSSSGLSVFDLDIGSDSEYEPMEPVQPEPLIDLAVVEETAPVRLERVAPVAAPRRARATPFTLEQRVVAP... | 2.7.7.19; 2.7.7.48; 3.1.3.84 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03317}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P03317}; Note=For nsP4 adenylyltransferase activity; Mn(2+) supports catalysis at 60% of the levels observed with Mg(2+). {ECO:0000250|UniProtKB:P03317}; COFACTOR:... | DNA-templated transcription [GO:0006351]; viral RNA genome replication [GO:0039694] | host cell cytoplasmic vesicle membrane [GO:0044162]; membrane [GO:0016020] | hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; poly(A) RNA polymerase activity [GO:1990817]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968] | PF20852;PF00978; | 3.40.220.10;3.40.50.150; | null | PTM: Polyprotein P1234: Specific enzymatic cleavages in vivo yield mature proteins (By similarity). The processing of the polyprotein is temporally regulated (By similarity). In early stages (1.7 hpi), P1234 is first cleaved in trans through its nsP2 protease activity, releasing P123' and nsP4, which associate to form ... | SUBCELLULAR LOCATION: [Polyprotein nsP1234]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Part of cytoplasmic vesicles, which are probably formed at the plasma membrane and internalized leading to late endosomal/lysosomal spherules containing the replication complex. ... | 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 + RN... | null | null | null | null | FUNCTION: Polyprotein P1234: Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2. {ECO:0000250|UniProtKB:Q8JUX6}.; FUNCTION: [Polyprotein P123]: The early replication complex formed by the polyprotein P123 and nsP4 synthesizes minus-strand RNAs (By similarit... | Middelburg virus |
P03322 | GAG_RSVP | MEAVIKVISSACKTYCGKTSPSKKEIGAMLSLLQKEGLLMSPSDLYSPGSWDPITAALSQRAMILGKSGELKTWGLVLGALKAAREEQVTSEQAKFWLGLGGGRVSPPGPECIEKPATERRIDKGEEVGETTVQRDAKMAPEETATPKTVGTSCYHCGTAIGCNCATASAPPPPYVGSGLYPSLAGVGEQQGQGGDTPPGAEQSRAEPGHAGQAPGPALTDWARVREELASTGPPVVAMPVVIKTEGPAWTPLEPKLITRLADTVRTKGLRSPITMAEVEALMSSPLLPHDVTNLMRVILGPAPYALWMDAWGVQLQTVI... | 3.4.23.- | null | proteolysis [GO:0006508]; viral procapsid maturation [GO:0046797] | host cell nucleolus [GO:0044196]; host cell nucleoplasm [GO:0044095]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral capsid [GO:0019028] | aspartic-type endopeptidase activity [GO:0004190]; nucleic acid binding [GO:0003676]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270] | PF00607;PF02813;PF00077;PF00098; | 1.10.1200.30;2.40.70.10;1.10.375.10;1.10.150.90;4.10.60.10; | null | PTM: [Gag polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins (PubMed:8627817, PubMed:8636100). The cleavage at the C-terminus of the Capsid protein p27 is slowly trimmed by the viral protease, sometimes being cut internally thereby generating the short version of the capsid protein and a capsid pr... | SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 1]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 2]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p12]: Virion {ECO:0000305}.; SUBC... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: The p10 domain folds back and interacts with the capsid protein domain during Gag polyprotein assembly in the immature particle (before the maturation cleavage that splits the 2 domains). {ECO:0000269|PubMed:26223638}.; FUNCTION: [Capsid protein p27, alternate cleaved 1]: Self-associates to... | Rous sarcoma virus subgroup C (strain Prague) (RSV-Pr-C) |
P03330 | GAG_WMSV | MGQNNSTPLSLTLDHWKDVRTRAHNLSVKIRKGKWQTFCSSEWPTFGVGWPPEGTFNLSVIFAVKRIVFQETGGHPDQVPYIVVWQDLAQSPPPWVPPSAKIAVVSSPENTRGPSAGRPSAPPRPPIYPATDDLLLLSEPPPYPAALPPPLAPPAVGPAPGQAPDSSDPEGPAAGTRSRRARSPADDSGPDSTVILPLRAIGPPAEPNGLVPLQYWPFSSADLYNWKSNHPSFSENPAGLTGLLESLMFSHQPTWDDCQQLLQILFTTEERERILLEARKNVLGDNGAPTQLENLINEAFPLNRPQWDYNTAAGRERLLV... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell late endosome membrane [GO:0044185]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | RNA binding [GO:0003723]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270] | PF01140;PF02093;PF00098; | 1.10.150.180;1.10.375.10;4.10.60.10; | null | PTM: [Gag polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. {ECO:0000250|UniProtKB:P03332}.; PTM: RNA-binding phosphoprotein p12 is phosphoryl... | SUBCELLULAR LOCATION: [Gag polyprotein]: Virion {ECO:0000250|UniProtKB:P03332}. Host cell membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host late endosome membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular body... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interacti... | Woolly monkey sarcoma virus (WMSV) (Simian sarcoma-associated virus) |
P03332 | GAG_MLVMS | MGQTVTTPLSLTLGHWKDVERIAHNQSVDVKKRRWVTFCSAEWPTFNVGWPRDGTFNRDLITQVKIKVFSPGPHGHPDQVPYIVTWEALAFDPPPWVKPFVHPKPPPPLPPSAPSLPLEPPRSTPPRSSLYPALTPSLGAKPKPQVLSDSGGPLIDLLTEDPPPYRDPRPPPSDRDGNGGEATPAGEAPDPSPMASRLRGRREPPVADSTTSQAFPLRAGGNGQLQYWPFSSSDLYNWKNNNPSFSEDPGKLTALIESVLITHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGDDGRPTQLPNEVDAAFPLERPDWD... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell late endosome membrane [GO:0044185]; host cell plasma membrane [GO:0020002]; host cell uropod [GO:0120026]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | RNA binding [GO:0003723]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270] | PF01140;PF01141;PF02093;PF00098; | 1.10.150.180;1.10.375.10;4.10.60.10; | null | PTM: [Gag polyprotein]: Ubiquitinated by ITCH. Gag can recruit the ubiquitin ligase Itch in an L domain-independent manner to facilitate virus release via a mechanism that involves Gag ubiquitination. {ECO:0000269|PubMed:19864377}.; PTM: [Gag polyprotein]: Specific enzymatic cleavages by the viral protease yield mature... | SUBCELLULAR LOCATION: [Gag polyprotein]: Virion {ECO:0000305}. Host cell membrane {ECO:0000269|PubMed:8991095}; Lipid-anchor {ECO:0000305}. Host late endosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P26807}. Note=These locations are probably lin... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interacti... | Moloney murine leukemia virus (isolate Shinnick) (MoMLV) |
P03334 | GAG_MSVMO | MGQTVTTPLSLTLDHWKDVERLAHNQSVDVKKRRWVTFCSAEWPTFNVGWPRDGTFNRDLITQVKIKVFSPGPHGHPDQVPYIVTWEALAFDPPPWVKPFVHPKPPPPLLPSAPSLPLEPPLSTPPQSSLYPALTPSLGAKPKPQVLSDSGGPLIDLLTEDPPPYRDPRPPPSDRDGDSGEATPAGEAPDPSPMASRLRGRREPPVADSTTSQAFPLRTGGNGQLQYWPFSSSDLYNWKNNNPSFSEDPGKLTALIESVLITHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGDDGRPTQLPNEVDAAFPLERPDWE... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | nucleic acid binding [GO:0003676]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270] | PF01140;PF01141;PF02093;PF00098; | 1.10.150.180;1.10.375.10;4.10.60.10; | null | PTM: [Gag polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. {ECO:0000250|UniProtKB:P03332}. | SUBCELLULAR LOCATION: [Gag polyprotein]: Virion {ECO:0000250}. Host cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.; SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p30]: Virion {ECO:0000305}. | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interacti... | Moloney murine sarcoma virus (MoMSV) |
P03336 | GAG_MLVAV | MGQTVTTPLSLTLEHWEDVQRIASNQSVDVKKRRWVTFCSAEWPTFGVGWPQDGTFNLDIILQVKSKVFSPGPHGHPDQVPYIVTWEAIAYEPPPWVKPFVSPKLSPSPTAPILPSGPSTQPPPRSALYPALTPSIKPRPSKPQVLSDNGGPLIDLLSEDPPPYGGQGLSSSDGDGDREEATSTSEIPAPSPIVSRLRGKRDPPAADSTTSRAFPLRLGGNGQLQYWPFSSSDLYNWKNNNPSFSEDPGKLTALIESVLTTHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGNDGRPTQLPNEVDAAFPLERPDWDY... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | RNA binding [GO:0003723]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270] | PF01140;PF01141;PF02093;PF00098; | 1.10.150.180;1.10.375.10;4.10.60.10; | null | PTM: [Gag polyprotein]: Ubiquitinated by ITCH. Gag can recruit the ubiquitin ligase Itch in an L domain-independent manner to facilitate virus release via a mechanism that involves Gag ubiquitination. {ECO:0000250|UniProtKB:P03332}.; PTM: [Gag polyprotein]: Specific enzymatic cleavages by the viral protease yield matur... | SUBCELLULAR LOCATION: [Gag polyprotein]: Virion {ECO:0000250|UniProtKB:P03332}. Host cell membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P26807}.; SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000250|UniProt... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interacti... | AKV murine leukemia virus (AKR (endogenous) murine leukemia virus) |
P03341 | GAG_BAEVM | MGQTLTTPLSLTLTHFSDVRARAHNLSVGVRKGRWQTFCSSEWPTLHVGWPRDGTFDLSVILQVKTKVMDPGPHGHPDQVAYIITWEDLVRNPPPWVKPFLHTPSTSKSTLLALEVPKNRTLDPPKPVLPDESQQDLLFQDPLPHPPHNPLLEPPPYNSPSPPVLSPVSPTTPSAPTPSSLVSSSTPPSSPAPPELTPRTPPQTPRLRLRRAEGQDGPSTWQSSLFPLRTVNRTIQYWPFSASDLYNWKTHNPSFSQDPQALTSLIESILLTHQPTWDDCQQLLQVLLTTEERQRVLLEARKNVPGPGGLPTQLPNEIDE... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell late endosome membrane [GO:0044185]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | RNA binding [GO:0003723]; structural constituent of virion [GO:0039660]; zinc ion binding [GO:0008270] | PF01140;PF02093;PF00098; | 1.10.150.180;1.10.375.10;4.10.60.10; | null | PTM: [Gag polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. {ECO:0000250|UniProtKB:P03332}.; PTM: RNA-binding phosphoprotein p12 is phosphoryl... | SUBCELLULAR LOCATION: [Gag polyprotein]: Virion {ECO:0000250|UniProtKB:P03332}. Host cell membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host late endosome membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular body... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interacti... | Baboon endogenous virus (strain M7) |
P03345 | GAG_HTL1A | MGQIFSRSASPIPRPPRGLAAHHWLNFLQAAYRLEPGPSSYDFHQLKKFLKIALETPARICPINYSLLASLLPKGYPGRVNEILHILIQTQAQIPSRPAPPPPSSPTHDPPDSDPQIPPPYVEPTAPQVLPVMHPHGAPPNHRPWQMKDLQAIKQEVSQAAPGSPQFMQTIRLAVQQFDPTAKDLQDLLQYLCSSLVASLHHQQLDSLISEAETRGITGYNPLAGPLRVQANNPQQQGLRREYQQLWLAAFAALPGSAKDPSWASILQGLEEPYHAFVERLNIALDNGLPEGTPKDPILRSLAYSNANKECQKLLQARGH... | null | null | viral process [GO:0016032] | viral nucleocapsid [GO:0019013] | nucleic acid binding [GO:0003676]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF02228;PF00607;PF19317;PF00098; | 1.10.1200.30;1.10.185.10;1.10.375.10;4.10.60.10; | null | PTM: [Gag polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation. {ECO:0000269|PubMed:2843670, ECO:0000269|PubMed:6280175}.; PTM: [Matrix protein p19]: Phosphorylation of the matrix protein p19 by MAP... | SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000269|PubMed:15476809}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p15-gag]: Virion {ECO:0000305}. | null | null | null | null | null | FUNCTION: [Gag polyprotein]: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. {ECO:0000269|PubMed:15476809}.; FUNCTION: [Matrix protein p19]: Matrix protein. {ECO:0000269|PubMed:15476809}.; ... | Human T-cell leukemia virus 1 (strain Japan ATK-1 subtype A) (HTLV-1) |
P03346 | GAG_HTLV2 | MGQIHGLSPTPIPKAPRGLSTHHWLNFLQAAYRLQPRPSDFDFQQLRRFLKLALKTPIWLNPIDYSLLASLIPKGYPGRVVEIINILVKNQVSPSAPAAPVPTPICPTTTPPPPPPPSPEAHVPPPYVEPTTTQCFPILHPPGAPSAHRPWQMKDLQAIKQEVSSSALGSPQFMQTLRLAVQQFDPTAKDLQDLLQYLCSSLVVSLHHQQLNTLITEAETRGMTGYNPMAGPLRMQANNPAQQGLRREYQNLWLAAFSTLPGNTRDPSWAAILQGLEEPYCAFVERLNVALDNGLPEGTPKEPILRSLAYSNANKECQKI... | null | null | viral process [GO:0016032] | viral nucleocapsid [GO:0019013] | nucleic acid binding [GO:0003676]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF02228;PF00607;PF19317;PF00098; | 1.10.1200.30;1.10.185.10;1.10.375.10;4.10.60.10; | null | PTM: [Gag polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation. {ECO:0000250|UniProtKB:P03345}.; PTM: [Matrix protein p19]: Phosphorylation of the matrix protein p19 by MAPK1 seems to play a role in... | SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p15-gag]: Virion {ECO:0000250|UniProtKB:P03345}. | null | null | null | null | null | FUNCTION: [Gag polyprotein]: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. {ECO:0000250|UniProtKB:P03345}.; FUNCTION: [Matrix protein p19]: Matrix protein. {ECO:0000250|UniProtKB:P03345}.... | Human T-cell leukemia virus 2 (HTLV-2) |
P03347 | GAG_HV1B1 | MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSSQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTET... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | identical protein binding [GO:0042802]; RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF08705;PF00098; | 1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype B (isolate BH10) (HIV-1) |
P03348 | GAG_HV1BR | MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSSQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTET... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF08705;PF00098; | 1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1) |
P03349 | GAG_HV1A2 | MGARASVLSGGELDKWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIDVKDTKEALEKIEEEQNKSKKKAQQAAAAAGTGNSSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQDVKNWMT... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF08705;PF00098; | 1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2) (HIV-1) |
P03353 | PRO_HTLV2 | MGQIHGLSPTPIPKAPRGLSTHHWLNFLQAAYRLQPRPSDFDFQQLRRFLKLALKTPIWLNPIDYSLLASLIPKGYPGRVVEIINILVKNQVSPSAPAAPVPTPICPTTTPPPPPPPSPEAHVPPPYVEPTTTQCFPILHPPGAPSAHRPWQMKDLQAIKQEVSSSALGSPQFMQTLRLAVQQFDPTAKDLQDLLQYLCSSLVVSLHHQQLNTLITEAETRGMTGYNPMAGPLRMQANNPAQQGLRREYQNLWLAAFSTLPGNTRDPSWAAILQGLEEPYCAFVERLNVALDNGLPEGTPKEPILRSLAYSNANKECQKI... | 3.4.23.- | null | proteolysis [GO:0006508]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral process [GO:0016032] | viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; nucleic acid binding [GO:0003676]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF02228;PF00607;PF19317;PF00077;PF00098; | 1.10.1200.30;2.40.70.10;1.10.185.10;1.10.375.10;4.10.60.10; | null | PTM: [Gag-Pro polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation. The protease is autoproteolytically processed at its N- and C-termini. {ECO:0000250|UniProtKB:P10274}.; PTM: [Matrix protein p19]:... | SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p15-pro]: Virion {ECO:0000250|UniProtKB:P03345}. | null | null | null | null | null | FUNCTION: [Gag-Pro polyprotein]: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. {ECO:0000250|UniProtKB:P03345}.; FUNCTION: [Matrix protein p19]: Matrix protein. {ECO:0000250|UniProtKB:P033... | Human T-cell leukemia virus 2 (HTLV-2) |
P03354 | POL_RSVP | MEAVIKVISSACKTYCGKTSPSKKEIGAMLSLLQKEGLLMSPSDLYSPGSWDPITAALSQRAMILGKSGELKTWGLVLGALKAAREEQVTSEQAKFWLGLGGGRVSPPGPECIEKPATERRIDKGEEVGETTVQRDAKMAPEETATPKTVGTSCYHCGTAIGCNCATASAPPPPYVGSGLYPSLAGVGEQQGQGGDTPPGAEQSRAEPGHAGQAPGPALTDWARVREELASTGPPVVAMPVVIKTEGPAWTPLEPKLITRLADTVRTKGLRSPITMAEVEALMSSPLLPHDVTNLMRVILGPAPYALWMDAWGVQLQTVI... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.- | COFACTOR: [Reverse transcriptase alpha-subunit]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=The RT polymerase active site binds 2 magnesium ions. {ECO:0000255|PROSITE-ProRule:PRU00405}; COFACTOR: [Reverse transcriptase alpha-subunit]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; N... | 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]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; zinc ion binding [GO:0008270] | PF00607;PF00552;PF02022;PF02813;PF00665;PF00077;PF00078;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;4.10.60.10; | null | PTM: [Isoform Gag-Pol polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000269|PubMed:15102858, ECO:0000269|PubMed:8636100}.; PTM: Capsid protein p27: The cleavage at the C-terminus is slowly trimmed by the viral protease, sometimes being cut internally thereby generating the short version... | SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 1]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p27, alternate cleaved 2]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p12]: Virion {ECO:0000305}. | CATALYTIC ACTIVITY: [Reverse transcriptase alpha-subunit]: 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:P... | null | null | null | null | FUNCTION: Capsid protein p27: Self-associates to form the irregular polyhedron core composed of hexamers and pentamers, that encapsulates the genomic RNA-nucleocapsid complex. Assembles as a tube in vitro. Binds to inositol hexakisphosphate (IP6), which allows the assembly of the polyhedral capsid. {ECO:0000250|UniProt... | Rous sarcoma virus subgroup C (strain Prague) (RSV-Pr-C) |
P03355 | POL_MLVMS | MGQTVTTPLSLTLGHWKDVERIAHNQSVDVKKRRWVTFCSAEWPTFNVGWPRDGTFNRDLITQVKIKVFSPGPHGHPDQVPYIVTWEALAFDPPPWVKPFVHPKPPPPLPPSAPSLPLEPPRSTPPRSSLYPALTPSLGAKPKPQVLSDSGGPLIDLLTEDPPPYRDPRPPPSDRDGNGGEATPAGEAPDPSPMASRLRGRREPPVADSTTSQAFPLRAGGNGQLQYWPFSSSDLYNWKNNNPSFSEDPGKLTALIESVLITHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGDDGRPTQLPNEVDAAFPLERPDWD... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.- | 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}; COFACTOR: [Reverse transcriptase/ribonuclease H]: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q2F7J3... | DNA catabolic process [GO:0006308]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; vi... | host cell late endosome membrane [GO:0044185]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; protein-DNA complex [GO:0032993]; viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; retroviral 3' processing activity [GO:0044824]; RNA binding [GO:0003723]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural const... | PF01140;PF01141;PF02093;PF18697;PF00075;PF17919;PF00665;PF00077;PF00078;PF00098;PF16721; | 1.10.340.70;2.30.30.850;3.10.20.370;3.30.70.270;2.40.70.10;1.10.150.180;3.10.10.10;1.10.375.10;3.30.420.10;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Ubiquitinated by ITCH. Gag can recruit the ubiquitin ligase Itch in an L domain-independent manner to facilitate virus release via a mechanism that involves Gag ubiquitination. {ECO:0000250|UniProtKB:P03332}.; PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yie... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Virion {ECO:0000250|UniProtKB:P03332}. Host cell membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host late endosome membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular ... | 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 | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0 for protease activity. {ECO:0000269|PubMed:16603535}; | null | FUNCTION: [Gag-Pol polyprotein]: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag-Pol, or to Gag-Pol binding host factor... | Moloney murine leukemia virus (isolate Shinnick) (MoMLV) |
P03356 | POL_MLVAV | MGQTVTTPLSLTLEHWEDVQRIASNQSVDVKKRRWVTFCSAEWPTFGVGWPQDGTFNLDIILQVKSKVFSPGPHGHPDQVPYIVTWEAIAYEPPPWVKPFVSPKLSPSPTAPILPSGPSTQPPPRSALYPALTPSIKPRPSKPQVLSDNGGPLIDLLSEDPPPYGGQGLSSSDGDGDREEATSTSEIPAPSPIVSRLRGKRDPPAADSTTSRAFPLRLGGNGQLQYWPFSSSDLYNWKNNNPSFSEDPGKLTALIESVLTTHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGNDGRPTQLPNEVDAAFPLERPDWDY... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.- | 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}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03355}; Note=Binds 1 magnesium ion for ribonu... | 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]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; virion a... | host cell late endosome membrane [GO:0044185]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; RNA binding [GO:0003723]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural constituent of virion [GO:0039660]; zinc ion binding ... | PF01140;PF01141;PF02093;PF18697;PF00075;PF17919;PF00665;PF00077;PF00078;PF00098;PF16721; | 1.10.340.70;2.30.30.850;3.10.20.370;3.30.70.270;2.40.70.10;1.10.150.180;3.10.10.10;1.10.375.10;3.30.420.10;4.10.60.10; | Retroviral Pol polyprotein family | PTM: [Gag-Pol polyprotein]: Ubiquitinated by ITCH. Gag can recruit the ubiquitin ligase Itch in an L domain-independent manner to facilitate virus release via a mechanism that involves Gag ubiquitination. {ECO:0000250|UniProtKB:P03332}.; PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yie... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Virion {ECO:0000250|UniProtKB:P03332}. Host cell membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host late endosome membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular ... | 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: [Gag-Pol polyprotein]: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag-Pol, or to Gag-Pol binding host factor... | AKV murine leukemia virus (AKR (endogenous) murine leukemia virus) |
P03359 | POL_WMSV | MGQNNSTPLSLTLDHWKDVRTRAHNLSVKIRKGKWQTFCSSEWPTFGVGWPPEGTFNLSVIFAVKRIVFQETGGHPDQVPYIVVWQDLAQSPPPWVPPSAKIAVVSSPENTRGPSAGRPSAPPRPPIYPATDDLLLLSEPPPYPAALPPPLAPPAVGPAPGQAPDSSDPEGPAAGTRSRRARSPADDSGPDSTVILPLRAIGPPAEPNGLVPLQYWPFSSADLYNWKSNHPSFSENPAGLTGLLESLMFSHQPTWDDCQQLLQILFTTEERERILLEARKNVLGDNGAPTQLENLINEAFPLNRPQWDYNTAAGRERLLV... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.- | 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}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03355}; Note=Binds 1 magnesium ion for ribonu... | 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]; virion assembly [GO:0019068] | host cell late endosome membrane [GO:0044185]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; RNA binding [GO:0003723]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural constituent of virion [GO:0039660]; zinc ion binding ... | PF01140;PF02093;PF18697;PF00075;PF17919;PF00665;PF00077;PF00078;PF00098;PF09337; | 1.10.340.70;2.30.30.850;3.10.20.370;3.30.70.270;2.40.70.10;1.10.150.180;3.10.10.10;1.10.375.10;3.30.420.10;4.10.60.10; | Retroviral Pol polyprotein family | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. {ECO:0000250|UniProtKB:P03355}.; PTM: [RNA-binding phosphoprotein p12]: Phosph... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Virion {ECO:0000250|UniProtKB:P03332}. Host cell membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host late endosome membrane {ECO:0000250|UniProtKB:P03332}; Lipid-anchor {ECO:0000250|UniProtKB:P03332}. Host endosome, host multivesicular ... | 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: [Gag-Pol polyprotein]: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag-Pol, or to Gag-Pol binding host factor... | Woolly monkey sarcoma virus (WMSV) (Simian sarcoma-associated virus) |
P03360 | POL_AVIRE | MSKESVAIIGATGNIRNYPKSEGRLVDLGRGLVTHSFLVIPECPDPLLGRDLLQKLRATISFTGEGPPEIRTEGKLLVTAPLEEEYRLFLEAPIQNVTLLEQWKREIPKVWAEINPPGLASTQAPIHVQLLSTALPVRVRQYPITLEAKRSLRETIRKFRAAGILRPVHSPWNTPLLPVRKSGTSEYRMVQDLREVNKRVETIHPTVPNPYTLLSLLPPDRIWYSVLDLKDAFFCIPLAPESQLIFAFEWADAEEGESGQLTWTRLPQGFKNSPTLFDEALNRDLQGFRLDHPSVSLLQYVDDLLIAADTQAACLSATRD... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.- | 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}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:24124581}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; E... | 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] | null | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523] | PF18697;PF00075;PF17919;PF00665;PF00077;PF00078;PF09337; | 1.10.340.70;2.30.30.850;3.10.20.370;3.30.70.270;2.40.70.10;3.10.10.10;3.30.420.10; | Retroviral Pol polyprotein family | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000305}. | 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=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405}; CATALYTIC ACTIVITY: Reaction=... | null | null | null | null | FUNCTION: [Protease]: The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activ... | Avian reticuloendotheliosis virus |
P03361 | POL_BLVJ | MGNSPSYNPPAGISPSDWLNLLQSAQRLNPRPSPSDFTDLKNYIHWFHKTQKKPWTFTSGGPTSCPPGRFGRVPLVLATLNEVLSNEGGAPGASAPEEQPPPYDPPAILPIISEGNRNRHRAWALRELQDIKKEIENKAPGSQVWIQTLRLAILQADPTPADLEQLCQYIASPVDQTAHMTSLTAAIAAAEAANTLQGFNPKTGTLTQQSAQPNAGDLRSQYQNLWLQAGKNLPTRPSAPWSTIVQGPAESSVEFVNRLQISLADNLPDGVPKEPIIDSLSYANANRECQQILQGRGPVAAVGQKLQACAQWAPKNKQPA... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.- | 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 budding via host ESCRT complex [GO:0039702]; 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]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural constituent of virion [GO:0039660]; zinc io... | PF02228;PF00607;PF19317;PF00552;PF00075;PF00665;PF00077;PF00078;PF00098; | 1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;3.30.420.10;4.10.60.10; | Retroviral Pol polyprotein family | PTM: [Matrix protein p15]: Phosphorylation of the matrix protein p15 by MAPK1 seems to play a role in budding. {ECO:0000250|UniProtKB:P03345}.; PTM: [Gag-Pro-Pol polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and i... | SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p12-pro]: Virion {ECO:0000250|UniProtKB:P03345}. | 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: Gag-Pro polyprotein: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. {ECO:0000250|UniProtKB:P03345}.; FUNCTION: [Matrix protein p15]: Matrix protein. {ECO:0000250|UniProtKB:P03345... | Bovine leukemia virus (isolate Japanese BLV-1) (BLV) |
P03362 | POL_HTL1A | MGQIFSRSASPIPRPPRGLAAHHWLNFLQAAYRLEPGPSSYDFHQLKKFLKIALETPARICPINYSLLASLLPKGYPGRVNEILHILIQTQAQIPSRPAPPPPSSPTHDPPDSDPQIPPPYVEPTAPQVLPVMHPHGAPPNHRPWQMKDLQAIKQEVSQAAPGSPQFMQTIRLAVQQFDPTAKDLQDLLQYLCSSLVASLHHQQLDSLISEAETRGITGYNPLAGPLRVQANNPQQQGLRREYQQLWLAAFAALPGSAKDPSWASILQGLEEPYHAFVERLNIALDNGLPEGTPKDPILRSLAYSNANKECQKLLQARGH... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.- | 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]; symbiont-mediated suppression of host gene expression [GO:0039657]; 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]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural molecule activity [GO:0005198]; zinc ion bi... | PF02228;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF00098; | 1.10.1200.30;3.30.70.270;2.40.70.10;1.10.185.10;3.10.10.10;1.10.375.10;3.30.420.10;4.10.60.10; | null | PTM: [Matrix protein p19]: Phosphorylation of the matrix protein p19 by MAPK1 seems to play a role in budding. {ECO:0000250|UniProtKB:P03345}.; PTM: [Gag-Pro-Pol polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and i... | SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p15-pro]: Virion {ECO:0000250|UniProtKB:P03345}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU00408}; 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:CH... | null | null | null | null | FUNCTION: [Gag-Pro-Pol polyprotein]: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. {ECO:0000250|UniProtKB:P03345}.; FUNCTION: [Matrix protein p19]: Matrix protein. {ECO:0000250|UniProtKB:... | Human T-cell leukemia virus 1 (strain Japan ATK-1 subtype A) (HTLV-1) |
P03363 | POL_HTLV2 | MGQIHGLSPTPIPKAPRGLSTHHWLNFLQAAYRLQPRPSDFDFQQLRRFLKLALKTPIWLNPIDYSLLASLIPKGYPGRVVEIINILVKNQVSPSAPAAPVPTPICPTTTPPPPPPPSPEAHVPPPYVEPTTTQCFPILHPPGAPSAHRPWQMKDLQAIKQEVSSSALGSPQFMQTLRLAVQQFDPTAKDLQDLLQYLCSSLVVSLHHQQLNTLITEAETRGMTGYNPMAGPLRMQANNPAQQGLRREYQNLWLAAFSTLPGNTRDPSWAAILQGLEEPYCAFVERLNVALDNGLPEGTPKEPILRSLAYSNANKECQKI... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.26.4; 3.4.23.- | 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}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase ... | 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]; symbiont-mediated suppression of host gene expression [GO:0039657]; 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]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural molecule activity [GO:0005198]; zinc ion bi... | PF02228;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF00098; | 1.10.1200.30;3.30.70.270;2.40.70.10;1.10.185.10;3.10.10.10;1.10.375.10;3.30.420.10;4.10.60.10; | null | PTM: [Matrix protein p19]: Phosphorylation of the matrix protein p19 by MAPK1 seems to play a role in budding. {ECO:0000250|UniProtKB:P03345}.; PTM: [Gag-Pro-Pol polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and i... | SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P03345}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p15-pro]: Virion {ECO:0000250|UniProtKB:P03345}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU00408}; 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:CH... | null | null | null | null | FUNCTION: [Gag-Pro-Pol polyprotein]: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. {ECO:0000250|UniProtKB:P03345}.; FUNCTION: [Matrix protein p19]: Matrix protein. {ECO:0000250|UniProtKB:... | Human T-cell leukemia virus 2 (HTLV-2) |
P03364 | POL_SMRVH | MGQASSHSENDLFISHLKESLKVRRIRVRKKDLVSFFSFIFKTCPWFPQEGSIDSRVWGRVGDCLNDYYRVFGPETIPITTFNYYNLIRDVLTNQSDSPDIQRLCKEGHKILISHSRPPSRQAPVTITTSEKASSRPPSRAPSTCPSVAIDIGSHDTGQSSLYPNLATLTDPPIQSPHSRAHTPPQHLPLLANSKTLHNSGSQDDQLNPADQADLEEAAAQYNNPDWPQLTNTPALPPFRPPSYVSTAVPPVAVAAPVLHAPTSGVPGSPTAPNLPGVALAKPSGPIDETVSLLDGVKTLVTKLSDLALLPPAGVMAFPV... | 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; | null | PTM: [Gag-Pro-Pol 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-Pro-Pol polyprotein]: Specific enzymatic cleavages in... | SUBCELLULAR LOCATION: [Capsid protein p35]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Matrix protein p19]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Probable nucleocapsid protein-dUTPase]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Protease 13 kDa]: Virion {ECO:0000250|UniProtKB:P07572}.; SUBCELLULAR LOCATIO... | 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 p19]: Matrix protein. {ECO:0000250|UniProtKB:P07567}.; FUNCTION: [Capsid protein p35]: Capsid protein. {ECO:0000250|UniProtKB:P07567}.; FUNCTION: Matrix protein p10: Matrix protein. {ECO:0000250|UniProtKB:P07572}.; FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein. {ECO:0000250|UniProtK... | Squirrel monkey retrovirus (SMRV-H) (SMRV-HLB) |
P03365 | POL_MMTVB | MGVSGSKGQKLFVSVLQRLLSERGLHVKESSAIEFYQFLIKVSPWFPEEGGLNLQDWKRVGREMKRYAAEHGTDSIPKQAYPIWLQLREILTEQSDLVLLSAEAKSVTEEELEEGLTGLLSTSSQEKTYGTRGTAYAEIDTEVDKLSEHIYDEPYEEKEKADKNEEKDHVRKIKKVVQRKENSEGKRKEKDSKAFLATDWNDDDLSPEDWDDLEEQAAHYHDDDELILPVKRKVVKKKPQALRRKPLPPVGFAGAMAEAREKGDLTFTFPVVFMGESDEDDTPVWEPLPLKTLKELQSAVRTMGPSAPYTLQVVDMVASQ... | 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}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Magnesium ions are required for NC-dUTPase activity. {ECO:0000250|UniProt... | 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;PF02337;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06817;PF00098;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: [Gag-Pro-Pol polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. {ECO:0000269|PubMed:1331110}.; PTM: [Protease]: Released by autocatalytic processing. {ECO:0000269|PubMed:1331110}.; PTM: [Gag-Pro-Pol polyprotein]: Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport ... | SUBCELLULAR LOCATION: [Matrix protein p10]: Virion {ECO:0000269|PubMed:6197754}.; SUBCELLULAR LOCATION: [Capsid protein p27]: Virion {ECO:0000269|PubMed:6197754}.; SUBCELLULAR LOCATION: [Nucleocapsid protein-dUTPase]: Virion {ECO:0000250|UniProtKB:P10258}. | 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 | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-6. {ECO:0000269|PubMed:1331110}; | null | FUNCTION: [Matrix protein p10]: Matrix protein. {ECO:0000305}.; FUNCTION: Nucleocapsid protein p14: Binds strongly to viral nucleic acids and promote their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs. {ECO:0000305}.; FUNCTION: [Capsid protein p27]: Capsid protein.... | Mouse mammary tumor virus (strain BR6) (MMTV) |
P03366 | POL_HV1B1 | MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSSQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTET... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | 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]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.; EC=3.1.13.2; Evidence={ECO:0000250}; CATALYTIC ACTIV... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype B (isolate BH10) (HIV-1) |
P03367 | POL_HV1BR | MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIEIKDTKEALDKIEEEQNKSKKKAQQAAADTGHSSQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTET... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | 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]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endoso... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RN... | null | null | null | null | FUNCTION: Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shut off translation (By similarity). {ECO:000... | Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1) |
P03369 | POL_HV1A2 | MGARASVLSGGELDKWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTVATLYCVHQRIDVKDTKEALEKIEEEQNKSKKKAQQAAAAAGTGNSSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRVHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQDVKNWMT... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | 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]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RN... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2) (HIV-1) |
P03370 | POL_VILV | MAKQGSKEKKGYPELKEVIKATCKIRVGPGKETLTEGNCLWALKTIDFIFEDLKTEPWTITKMYTVWDRLKGLTPEETSKREFASLQATLACIMCSQMGMKPETVQAAKGIISMKEGLHENKEAKGEKVEQLYPNLEKHREVYPIVNLQAGGRSWKAVESVVFQQLQTVAMQHGLVSEDFERQLAYYATTWTSKDILEVLAMMPGNRAQKELIQGKLNEEAERWVRQNPPGPNVLTVDQIMGVGQTNQQASQANMDQARQICLQWVITALRSVRHMSHRPGNPMLVKQKNTESYEDFIARLLEAIDAEPVTDPIKTYLKV... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 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]; nucleotide metabolic process [GO:0009117]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; viral genome integration into host DNA [GO:0044826] | viral capsid [GO:0019028] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; dUTP diphosphatase activity [GO:0004170]; exoribonuclease H activity [GO:0004533]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; zinc io... | PF00692;PF00607;PF19317;PF02022;PF00075;PF00665;PF00077;PF00078;PF00098; | 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;3.30.420.10;4.10.60.10; | Retroviral Pol polyprotein family | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000305}. | SUBCELLULAR LOCATION: [Matrix protein p16]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p25]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p14]: Virion {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU00408}; CATALYTIC ACTIVITY: Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid.; EC=3.1.13.2; CATALYTIC ACTIVITY: Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xr... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Maedi visna virus (strain 1514) (MVV) (Visna lentivirus) |
P03371 | POL_EIAVY | TAWTFLKAMQKCSKKREARGSREAPETNFPDTTEESAQQICCTRDSSDSKSVPRSERNKKGIQCQGEGSSRGSQPGQFVGVTYNLEKRPTTIVLINDTPLNVLLDTGADTSVLTTAHYNRLKYRGRKYQGTGIIGVGGNVETFSTPVTIKKKGRHIKTRMLVADIPVTILGRDILQDLGAKLVLAQLSKEIKFRKIELKEGTMGPKIPQWPLTKEKLEGAKETVQRLLSEGKISEASDNNPYNSPIFVIKKRSGKWRLLQDLRELNKTVQVGTEISRGLPHPGGLIKCKHMTVLDIGDAYFTIPLDPEFRPYTAFTIPSI... | 2.7.7.-; 2.7.7.49; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.- | null | 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] | null | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; exoribonuclease H activity [GO:0004533]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; zinc ion binding [GO:0008270] | PF00692;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817; | 1.10.10.200;2.70.40.10;3.30.70.270;2.40.70.10;3.10.10.10;2.30.30.10;3.30.420.10; | Retroviral Pol polyprotein family | PTM: Specific enzymatic cleavages in vivo yield mature proteins. | null | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end... | null | null | null | null | FUNCTION: During replicative cycle of retroviruses, the reverse-transcribed viral DNA is integrated into the host chromosome by the viral integrase enzyme. RNase H activity is associated with the reverse transcriptase. | Equine infectious anemia virus (strain Wyoming) (EIAV) |
P03372 | ESR1_HUMAN | MTMTLHTKASGMALLHQIQGNELEPLNRPQLKIPLERPLGEVYLDSSKPAVYNYPEGAAYEFNAAAAANAQVYGQTGLPYGPGSEAAAFGSNGLGGFPPLNSVSPSPLMLLHPPPQLSPFLQPHGQQVPYYLENEPSGYTVREAGPPAFYRPNSDNRRQGGRERLASTNDKGSMAMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDGEGRGEVGSAGDMRAANLWPSPLMIKRSKKNSLALSLTADQMVSALL... | null | null | androgen metabolic process [GO:0008209]; antral ovarian follicle growth [GO:0001547]; cellular response to estradiol stimulus [GO:0071392]; cellular response to estrogen stimulus [GO:0071391]; chromatin remodeling [GO:0006338]; epithelial cell development [GO:0002064]; epithelial cell proliferation involved in mammary ... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; euchromatin [GO:0000791]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; transcription regulator complex [GO:0005667] | 14-3-3 protein binding [GO:0071889]; ATPase binding [GO:0051117]; beta-catenin binding [GO:0008013]; calmodulin binding [GO:0005516]; chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding... | PF12743;PF00104;PF02159;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | PTM: Phosphorylated by cyclin A/CDK2 and CK1. Phosphorylation probably enhances transcriptional activity. Self-association induces phosphorylation. Dephosphorylation at Ser-118 by PPP5C inhibits its transactivation activity. Phosphorylated by LMTK3 in vitro. {ECO:0000269|PubMed:10428798, ECO:0000269|PubMed:14764652, EC... | SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:12682286, ECO:0000269|PubMed:20074560}. Cytoplasm {ECO:0000269|PubMed:12682286, ECO:0000269|PubMed:24498420}. Cell membrane {ECO:0000269|PubMed:12682286}; Peripheral membrane protein {ECO:0000269|PubMed:12682286}; Cytop... | null | null | null | null | null | FUNCTION: Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen r... | Homo sapiens (Human) |
P03375 | ENV_HV1B1 | MRVKEKYQHLWRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYTLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSANFTDNAKTIIVQLNQSVEINCTRPNNNTRKSIRIQRGPGRAFVTI... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell perinuclear region of cytoplasm [GO:0044220]; host cell periphery [GO:0044538]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | CD4 receptor binding [GO:0042609]; protein-containing complex binding [GO:0044877]; structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group M subtype B (isolate BH10) (HIV-1) |
P03377 | ENV_HV1BR | MRVKEKYQHLWRWGWKWGTMLLGILMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLGNATNTNSSNTNSSSGEMMMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYTLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSANFTDNAKTIIVQLNQSVEINCTRPNNNTRKSIRIQRGPGR... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1) |
P03378 | ENV_HV1A2 | MKVKGTRRNYQHLWRWGTLLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDARAYDTEVHNVWATHACVPTDPNPQEVVLGNVTENFNMWKNNMVEQMQEDIISLWDQSLKPCVKLTPLCVTLNCTDLGKATNTNSSNWKEEIKGEIKNCSFNITTSIRDKIQKENALFRNLDVVPIDNASTTTNYTNYRLIHCNRSVITQACPKVSFEPIPIHYCTPAGFAILKCNNKTFNGKGPCTNVSTVQCTHGIRPIVSTQLLLNGSLAEEEVVIRSDNFTNNAKTIIVQLNESVAINCTRPNNNTRKSIYIGPGRAFHT... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2) (HIV-1) |
P03383 | ENV_HTLV2 | MGNVFFLLLFSLTHFPLAQQSRCTLTIGISSYHSSPCSPTQPVCTWNLDLNSLTTDQRLHPPCPNLITYSGFHKTYSLYLFPHWIKKPNRQGLGYYSPSYNDPCSLQCPYLGCQAWTSAYTGPVSSPSWKFHSDVNFTQEVSQVSLRLHFSKCGSSMTLLVDAPGYDPLWFITSEPTQPPPTSPPLVHDSDLEHVLTPSTSWTTKILKFIQLTLQSTNYSCMVCVDRSSLSSWHVLYTPNISIPQQTSSRTILFPSLALPAPPSQPFPWTHCYQPRLQAITTDNCNNSIILPPFSLAPVPPPATRRRRAVPIAVWLVSAL... | null | null | fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718]; syncytium formation by plasma membrane fusion [GO:0000768]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00429; | 1.10.287.210; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires th... | SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by cont... | null | null | null | null | null | FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).... | Human T-cell leukemia virus 2 (HTLV-2) |
P03385 | ENV_MLVMS | MARSTLSKPLKNKVNPRGPLIPLILLMLRGVSTASPGSSPHQVYNITWEVTNGDRETVWATSGNHPLWTWWPDLTPDLCMLAHHGPSYWGLEYQSPFSSPPGPPCCSGGSSPGCSRDCEEPLTSLTPRCNTAWNRLKLDQTTHKSNEGFYVCPGPHRPRESKSCGGPDSFYCAYWGCETTGRAYWKPSSSWDFITVNNNLTSDQAVQVCKDNKWCNPLVIRFTDAGRRVTSWTTGHYWGLRLYVSGQDPGLTFGIRLRYQNLGPRVPIGPNPVLADQQPLSKPKPVKSPSVTKPPSGTPLSPTQLPPAGTENRLLNLVDG... | null | null | fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF00429; | 1.10.287.210;3.90.310.10; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires th... | SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral membrane protein. Host cell membrane... | null | null | null | null | null | FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. Interaction with HECT ubiquitin ligases activates a thiol in a CXXC motif of the C-terminal domain, where the other Cys residue participates in the formation of the intersubunit disulfide. The activated thiol will attack ... | Moloney murine leukemia virus (isolate Shinnick) (MoMLV) |
P03386 | ENV_MLVAV | MESTTLSKPFKNQVNPWGPLIVLLILGGVNPVTLGNSPHQVFNLTWEVTNGDRETVWAITGNHPLWTWWPDLTPDLCMLALHGPSYWGLEYRAPFSPPPGPPCCSGSSDSTPGCSRDCEEPLTSYTPRCNTAWNRLKLSKVTHAHNGGFYVCPGPHRPRWARSCGGPESFYCASWGCETTGRASWKPSSSWDYITVSNNLTSDQATPVCKGNEWCNSLTIRFTSFGKQATSWVTGHWWGLRLYVSGHDPGLIFGIRLKITDSGPRVPIGPNPVLSDRRPPSRPRPTRSPPPSNSTPTETPLTLPEPPPAGVENRLLNLVK... | null | null | fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | metal ion binding [GO:0046872] | PF00429; | 1.10.287.210;3.90.310.10; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires th... | SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral membrane protein. Host cell membrane... | null | null | null | null | null | FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).... | AKV murine leukemia virus (AKR (endogenous) murine leukemia virus) |
P03390 | ENV_MLVF5 | MACSTLPKSPKDKIDPRDLLIPLILFLSLKGARSAAPGSSPHQVYNITWEVTNGDRETVWAISGNHPLWTWWPVLTPDLCMLALSGPPHWGLEYQAPYSSPPGPPCCSGSSGSSAGCSRDCDEPLTSLTPRCNTAWNRLKLDQVTHKSSEGFYVCPGSHRPREAKSCGGPDSFYCASWGCETTGRVYWKPSSSWDYITVDNNLTTSQAVQVCKDNKWCNPLAIQFTNAGKQVTSWTTGHYWGLRLYVSGRDPGLTFGIRLRYQNLGPRVPIGPNPVLADQLSLPRPNPLPKPAKSPPASNSTPTLISPSPTPTQPPPAGT... | null | null | fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host antigen processing and presentation [GO:0039588]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | metal ion binding [GO:0046872] | PF00429; | 1.10.287.210;3.90.310.10; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires th... | SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral membrane protein. Host cell membrane... | null | null | null | null | null | FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).... | Friend murine leukemia virus (isolate 57) (FrMLV) |
P03391 | ENV_FSVGA | MESPTHPKPSKDKTLSWNLVFLVGILFTIDIGMANPSPHQVYNVTWTITNLVTGTKANATSMLGTLTDAFPTMYFDLCDIIGNTWNPSDQEPFPGYGCDQPMRRWQQRNTPFYVCPGHANRKQCGGPQDGFCAVWGCETTGETYWRPTSSWDYITVKKGVTQGIYQCSGGGWCGPCYDKAVHSSTTGASEGGRCNPLILQFTQKGRQTSWDGPKSWGLRLYRSGYDPIALFSVSRQVMTITPPQAMGPNLVLPDQKPPSRQSQIESRVTPHHSQGNGGTPGITLVNASIAPLSTPVTPASPKRIGTGDRLINLVQGTYLA... | null | null | fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00429; | 1.10.287.210;3.90.310.10; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires th... | SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Surface protein]: Virion membrane; Peripheral membrane protein. Host cell membrane... | null | null | null | null | null | FUNCTION: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).... | Feline sarcoma virus (strain Gardner-Arnstein) (Ga-FeSV) (Gardner-Arnstein feline leukemia oncovirus B) |
P03396 | ENV_RSVP | MEAVIKAFLTGYPGKTSKKDSKEKPLATSKKDPEKTPLLPTRVNYILIIGVLVLCEVTGVRADVHLLEQPGNLWITWANRTGQTDFCLSTQSATSPFQTCLIGIPSPISEGDFKGYVSDTNCSTVGTDRLVLSASITGGPDNSTTLTYRKVSCLLLKLNVSMWDEPPELQLLGSQSLPNVTNITQVSGVAGGCVYFAPRATGLFLGWSKQGLSRFLLRHPFTSTSNSTEPFTVVTADRHNLFMGSEYCGAYGYRFWEIYNCSQTRNTYRCGDVGGTGLPETWCRGKGGIWVNQSKEINETEPFSFTANCTGSNLGNVSGC... | null | null | fusion of virus membrane with host plasma membrane [GO:0019064]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF03708;PF00429; | 1.10.287.210; | Alpharetroviruses envelope glycoprotein family | PTM: [Envelope glycoprotein gp95]: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is N-glycosylated and processed likely by host cell furin or by a furin-like protease in the Golgi to yield the mature SU and TM proteins. The cleavage site... | SUBCELLULAR LOCATION: [Transmembrane protein]: Virion membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000303|PubMed:31151254}. Host cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000303|PubMed:31151254}.; SUBCELLULAR LOCATION: [Surface protein]: Virion membrane {ECO:0000305}; P... | null | null | null | null | null | FUNCTION: [Surface protein]: The surface protein (SU) attaches the virus to the host cell entry receptor TVC (PubMed:16051833). This interaction triggers the refolding of the transmembrane protein (TM) thereby unmasking its fusion peptide and the formation of a reactive thiolate on Cys-100 to activate its fusogenic pot... | Rous sarcoma virus subgroup C (strain Prague) (RSV-Pr-C) |
P03404 | NEF_HV1B1 | MGGKWSKSSVIGWPAVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAANNAACAWLEAQEEEKVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGIRYPLTFGWCYKLVPVEPDKVEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC | null | null | negative regulation of CD4 production [GO:0045225]; perturbation by virus of host immune response [GO:0075528]; regulation of calcium-mediated signaling [GO:0050848]; suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC... | extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | ATPase binding [GO:0051117]; CD4 receptor binding [GO:0042609]; GTP binding [GO:0005525]; MHC class I protein binding [GO:0042288]; protein kinase binding [GO:0019901]; SH3 domain binding [GO:0017124]; signaling receptor binding [GO:0005102]; thioesterase binding [GO:0031996] | PF00469; | 4.10.890.10;3.30.62.10; | Lentivirus primate group Nef protein family | PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM... | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_0... | null | null | null | null | null | FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells... | Human immunodeficiency virus type 1 group M subtype B (isolate BH10) (HIV-1) |
P03406 | NEF_HV1BR | MGGKWSKSSVVGWPTVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAATNAACAWLEAQEEEEVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGVRYPLTFGWCYKLVPVEPDKVEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC | null | null | negative regulation of CD4 production [GO:0045225]; perturbation by virus of host immune response [GO:0075528]; regulation of calcium-mediated signaling [GO:0050848]; regulation of T cell activation [GO:0050863]; suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processi... | extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | ATPase binding [GO:0051117]; calmodulin binding [GO:0005516]; CD4 receptor binding [GO:0042609]; GTP binding [GO:0005525]; MHC class I protein binding [GO:0042288]; peptidase activator activity [GO:0016504]; protein kinase binding [GO:0019901]; SH3 domain binding [GO:0017124]; signaling receptor binding [GO:0005102]; t... | PF00469; | 4.10.890.10;3.30.62.10; | Lentivirus primate group Nef protein family | PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078, ECO:0000269|PubMed:7835426, ECO:0000269|PubMed:8623533}.; PTM... | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078, ECO:0000269|PubMed:19781555}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078, ECO:0000269|PubMed:19781555}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078, ECO:0000269|PubMed:19781555}. Virion {ECO:0000255|HAMAP-Rule:MF_04078, ECO:0000269|PubM... | null | null | null | null | null | FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication (PubMed:8151761). Alters numerous pathways of T-lymphocytes function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity (PubMed:25585010). Alters the functionality of other ... | Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1) |
P03407 | NEF_HV1A2 | MGGKWSKRSMGGWSAIRERMRRAEPRAEPAADGVGAVSRDLEKHGAITSSNTAATNADCAWLEAQEEEEVGFPVRPQVPLRPMTYKAALDISHFLKEKGGLEGLIWSQRRQEILDLWIYHTQGYFPDWQNYTPGPGIRYPLTFGWCFKLVPVEPEKVEEANEGENNSLLHPMSLHGMEDAEKEVLVWRFDSKLAFHHMARELHPEYYKDC | null | null | activation of transmembrane receptor protein tyrosine kinase activity [GO:0007171]; endocytosis involved in viral entry into host cell [GO:0075509]; suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:00467... | extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | GTP binding [GO:0005525]; SH3 domain binding [GO:0017124] | PF00469; | 4.10.890.10;3.30.62.10; | Lentivirus primate group Nef protein family | PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM... | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_0... | null | null | null | null | null | FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells... | Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2) (HIV-1) |
P03409 | TAX_HTL1A | MAHFPGFGQSLLFGYPVYVFGDCVQGDWCPISGGLCSARLHRHALLATCPEHQITWDPIDGRVIGSALQFLIPRLPSFPTQRTSKTLKVLTPPITHTTPNIPPSFLQAMRKYSPFRNGYMEPTLGQHLPTLSFPDPGLRPQNLYTLWGGSVVCMYLYQLSPPITWPLLPHVIFCHPGQLGAFLTNVPYKRIEELLYKISLTTGALIILPEDCLPTTLFQPARAPVTLTAWQNGLLPFHSTLTTPGLIWTFTDGTPMISGPCPKDGQPSLVLQSSSFIFHKFQTKAYHPSFLLSHGLIQYSSFHSLHLLFEEYTNIPISLL... | null | null | positive regulation of DNA-templated transcription [GO:0045893]; symbiont-mediated perturbation of host cell cycle G0/G1 transition checkpoint [GO:0039646]; symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint [GO:0039645]; symbiont-mediated perturbation of host exit from mitosis [GO:0039593] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | DNA binding [GO:0003677]; metal ion binding [GO:0046872]; SH3 domain binding [GO:0017124] | PF02959; | null | Deltaretrovirus Tax protein family | PTM: Phosphorylation at Thr-48 results in the loss of NF-kappa-B activation function. Phosphorylation at Thr-215 results in loss of CREB and NF-B responsive promoters activation. Phosphorylation at Thr-184 and Ser-336 have no effect on these Tax functions. Phosphorylation of either Ser-300 or Ser-301 is necessary for l... | SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:15269214, ECO:0000269|PubMed:22789739}. Host cytoplasm {ECO:0000269|PubMed:15269214, ECO:0000269|PubMed:22789739, ECO:0000269|PubMed:29665857}. Note=Shuttles from the host nucleus to the cytoplasm. Found predominantly in the nucleus, where it is equally distributed... | null | null | null | null | null | FUNCTION: Transcriptional activator that governs the viral transcription from the 5'LTR via the recruitment of dimers of host phosphorylated CREB1. Together they bind cAMP response elements within the viral promoter and mediate high-level viral transcription (PubMed:22789739, PubMed:8970957). Increases host CREB1 O-Glc... | Human T-cell leukemia virus 1 (strain Japan ATK-1 subtype A) (HTLV-1) |
P03410 | TAX_HTLV2 | MAHFPGFGQSLLYGYPVYVFGDCVQADWCPVSGGLCSTRLHRHALLATCPEHQLTWDPIDGRVVSSPLQYLIPRLPSFPTQRTSRTLKVLTPPTTPVSPKVPPAFFQSMRKHTPYRNGCLEPTLGDQLPSLAFPEPGLRPQNIYTTWGKTVVCLYLYQLSPPMTWPLIPHVIFCHPRQLGAFLTKVPLKRLEELLYKMFLHTGTVIVLPEDDLPTTMFQPVRAPCIQTAWCTGLLPYHSILTTPGLIWTFNDGSPMISGPYPKAGQPSLVVQSSLLIFEKFETKAFHPSYLLSHQLIQYSSFHNLHLLFDEYTNIPVSIL... | null | null | positive regulation of DNA-templated transcription [GO:0045893]; symbiont-mediated perturbation of host cell cycle G0/G1 transition checkpoint [GO:0039646] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | 2 iron, 2 sulfur cluster binding [GO:0051537]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]; SH3 domain binding [GO:0017124] | PF02959; | null | Deltaretrovirus Tax protein family | PTM: Phosphorylation at Thr-48 results in the loss of NF-kappa-B activation function. Phosphorylation at Thr-215 results in loss of CREB and NF-B responsive promoters activation. Phosphorylation at Thr-184 has no effect on these Tax functions. Phosphorylation of either Ser-300 or Ser-301 is necessary for localization t... | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:15269214}. Host nucleus {ECO:0000269|PubMed:15269214}. Note=Tax-2 is mainly found in the cytoplasm. | null | null | null | null | null | FUNCTION: Transcriptional activator that activates both the viral long terminal repeat (LTR) and cellular promoters via activation of CREB, NF-kappa-B, SRF and AP-1 pathways. Binds to three 21 bp repeat elements located within the LTRs, referred to as Tax-responsive elements (TRE). Binding to TRE requires the interacti... | Human T-cell leukemia virus 2 (HTLV-2) |
P03416 | NCAP_CVMA5 | MSFVPGQENAGGRSSSVNRAGNGILKKTTWADQTERGPNNQNRGRRNQPKQTATTQPNSGSVVPHYSWFSGITQFQKGKEFQFAEGQGVPIANGIPASEQKGYWYRHNRRSFKTPDGQQKQLLPRWYFYYLGTGPHAGASYGDSIEGVFWVANSQADTNTRSDIVERDPSSHEAIPTRFAPGTVLPQGFYVEGSGRSAPASRSGSRSQSRGPNNRARSSSNQRQPASTVKPDMAEEIAALVLAKLGKDAGQPKQVTKQSAKEVRQKILNKPRQKRTPNKQCPVQQCFGKRGPNQNFGGSEMLKLGTSDPQFPILAELAPT... | null | null | null | host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell Golgi apparatus [GO:0044177]; ribonucleoprotein complex [GO:1990904]; viral nucleocapsid [GO:0019013] | RNA binding [GO:0003723] | PF00937; | null | Betacoronavirus nucleocapsid protein family | PTM: ADP-ribosylated. The ADP-ribosylation is retained in the virion during infection. {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:29199039}.; PTM: Phosphorylated on serine and threonine residues. {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:17367888}. | SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:29199039}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:17210170}. Host Golgi apparatus {ECO:0000255|HAMAP-Rule:MF_04096}. Note=Located inside the virion, complexed with th... | null | null | null | null | null | FUNCTION: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as vi... | Murine coronavirus (strain A59) (MHV-A59) (Murine hepatitis virus) |
P03418 | NCAP_HRSVA | MALSKVKLNDTLNKDQLLSSSKYTIQRSTGDSIDTPNYDVQKHINKLCGMLLITEDANHKFTGLIGMLYAMSRLGREDTIKILRDAGYHVKANGVDVTTHRQDINGKEMKFEVLTLASLTTEIQINIEIESRKSYKKMLKEMGEVAPEYRHDSPDCGMIILCIAALVITKLAAGDRSGLTAVIRRANNVLKNEMKRYKGLLPKDIANSFYEVFEKHPHFIDVFVHFGIAQSSTRGGSRVEGIFAGLFMNAYGAGQVMLRWGVLAKSVKNIMLGHASVQAEMEQVVEVYEYAQKLGGEAGFYHILNNPKASLLSLTQFPHF... | null | null | symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity [GO:0039545]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity [GO:0039554]; symbiont-mediated suppression of ... | helical viral capsid [GO:0019029]; host cell cytoplasm [GO:0030430]; ribonucleoprotein complex [GO:1990904]; viral capsid [GO:0019028]; viral nucleocapsid [GO:0019013] | protein serine/threonine kinase inhibitor activity [GO:0030291]; RNA binding [GO:0003723] | PF03246; | null | Paramyxoviruses nucleocapsid family | PTM: Tyrosine phosphorylation modulates viral transcription and replication. {ECO:0000269|PubMed:22019509}. | SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm {ECO:0000269|PubMed:17703289, ECO:0000269|PubMed:32878896}. Note=Localizes in cytoplasmic inclusion bodies. {ECO:0000269|PubMed:17703289, ECO:0000269|PubMed:32878896}. | null | null | null | null | null | FUNCTION: Encapsidates the viral RNA genome by forming a left-handed helical nucleocapsid that protects the RNA from nucleases (PubMed:19965480, PubMed:23677789, PubMed:31229488). RNA replication depends on the availability of soluble nucleoprotein (PubMed:22623798, PubMed:9299631). The encapsidated genomic RNA is term... | Human respiratory syncytial virus A (strain A2) |
P03420 | FUS_HRSVA | MELLILKANAITTILTAVTFCFASGQNITEEFYQSTCSAVSKGYLSALRTGWYTSVITIELSNIKENKCNGTDAKVKLIKQELDKYKNAVTELQLLMQSTPPTNNRARRELPRFMNYTLNNAKKTNVTLSKKRKRRFLGFLLGVGSAIASGVAVSKVLHLEGEVNKIKSALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDKQLLPIVNKQSCSISNIETVIEFQQKNNRLLEITREFSVNAGVTTPVSTYMLTNSELLSLINDMPITNDQKKLMSNNVQIVRQQSYSIMSIIKEEVLAYVVQLPLYGVIDTPCWKLHTSP... | null | null | entry receptor-mediated virion attachment to host cell [GO:0098670]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of syncytium formation by virus [GO:0060141]; symbiont entry into host cell [GO:0046718] | host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; plasma membrane [GO:0005886]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | identical protein binding [GO:0042802] | PF00523; | 1.10.287.2480;6.10.250.1160;6.20.370.50; | Paramyxoviruses fusion glycoprotein family | PTM: [Fusion glycoprotein F0]: The F glycoprotein is synthesized as a F0 inactive precursor that is heavily N-glycosylated and processed at two sites by a host furin-like protease probably in the Golgi (PubMed:11369882, PubMed:11418598, PubMed:11493675, PubMed:23593008). The cleavage site between p27 and F1 may occur a... | SUBCELLULAR LOCATION: [Fusion glycoprotein F0]: Host Golgi apparatus membrane {ECO:0000305|PubMed:16160180}; Single-pass membrane protein {ECO:0000269|PubMed:16160180}.; SUBCELLULAR LOCATION: [Fusion glycoprotein F1]: Virion membrane {ECO:0000269|PubMed:23776214}; Single-pass type I membrane protein {ECO:0000269|PubMed... | null | null | null | null | null | FUNCTION: [Fusion glycoprotein F0]: Inactive precursor that is cleaved at two sites by a furin-like protease to give rise to the mature F1 and F2 fusion glycoproteins. {ECO:0000269|PubMed:23593008}.; FUNCTION: [Fusion glycoprotein F1]: Class I viral fusion protein (PubMed:23618766). Under the current model, the protein... | Human respiratory syncytial virus A (strain A2) |
P03421 | PHOSP_HRSVA | MEKFAPEFHGEDANNRATKFLESIKGKFTSPKDPKKKDSIISVNSIDIEVTKESPITSNSTIINPTNETDDTAGNKPNYQRKPLVSFKEDPTPSDNPFSKLYKETIETFDNNEEESSYSYEEINDQTNDNITARLDRIDEKLSEILGMLHTLVVASAGPTSARDGIRDAMIGLREEMIEKIRTEALMTNDRLEAMARLRNEESEKMAKDTSDEVSLNPTSEKLNNLLEGNDSDNDLSLEDF | null | null | viral life cycle [GO:0019058] | host cell cytoplasm [GO:0030430]; virion component [GO:0044423] | RNA-dependent RNA polymerase activity [GO:0003968] | PF02478; | null | Pneumoviridae phosphoprotein P family | PTM: Constitutively phosphorylated by host (PubMed:17098979). Phosphorylation at S-116, S-117, S-119, S-232 and S-237 is required for transcription inhibition by M2-2 and viral particle egress (PubMed:26474524). Phosphorylation at S-232 and S-237 increases the affinity of the binding to the nucleoprotein (PubMed:254078... | SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:27654298}. Host cytoplasm {ECO:0000269|PubMed:27654298}. Note=Localizes in cytoplasmic inclusion bodies. {ECO:0000269|PubMed:27654298}. | null | null | null | null | null | FUNCTION: Plays critical roles in regulating RNA replication and transcription through its interactions with multiple proteins (PubMed:25568210, PubMed:26474524). Tethers the RNA-directed RNA polymerase L to the nucleoprotein-RNA complex (PubMed:26474524). Recruits the M2-1 protein, a processivity factor that is requir... | Human respiratory syncytial virus A (strain A2) |
P03423 | GLYC_HRSVA | MSKNKDQRTAKTLERTWDTLNHLLFISSCLYKLNLKSVAQITLSILAMIISTSLIIAAIIFIASANHKVTPTTAIIQDATSQIKNTTPTYLTQNPQLGISPSNPSEITSQITTILASTTPGVKSTLQSTTVKTKNTTTTQTQPSKPTTKQRQNKPPSKPNNDFHFEVFNFVPCSICSNNPTCWAICKRIPNKKPGKKTTTKPTKKPTLKTTKKDPKPQTTKSKEVPTTKPTEEPTINTTKTNIITTLLTSNTTGNPELTSQMETFHSTSSEGNPSPSQVSTTSEYPSQPSSPPNTPRQ | null | null | adhesion receptor-mediated virion attachment to host cell [GO:0098671]; symbiont entry into host cell [GO:0046718]; virus-mediated perturbation of host defense response [GO:0019049] | extracellular region [GO:0005576]; host cell plasma membrane [GO:0020002]; plasma membrane [GO:0005886]; virion membrane [GO:0055036] | null | PF00802; | null | Pneumoviruses glycoprotein G family | PTM: [Isoform Secreted glycoprotein G]: Cleaved to give rise to the mature sG protein which lacks the transmembrane domain. {ECO:0000250|UniProtKB:P20895}.; PTM: [Isoform Membrane-bound glycoprotein G]: N- and O-glycosylated (PubMed:4069997). May carry 30-40 separate O-linked carbohydrate chains distributed among the 9... | SUBCELLULAR LOCATION: [Isoform Membrane-bound glycoprotein G]: Virion membrane {ECO:0000269|PubMed:15958665}; Single-pass type II membrane protein {ECO:0000303|PubMed:2164608}. Host cell membrane {ECO:0000269|PubMed:15958665, ECO:0000269|PubMed:28939853}; Single-pass type II membrane protein {ECO:0000303|PubMed:2164608... | null | null | null | null | null | FUNCTION: [Isoform Membrane-bound glycoprotein G]: Attaches the virion to the host cell membrane by interacting with heparan sulfate, initiating the infection (PubMed:10400758, PubMed:10864656, PubMed:3655746). Interacts with host CX3CR1, the receptor for the CX3C chemokine fractalkine, to modulate the immune response ... | Human respiratory syncytial virus A (strain A2) |
P03427 | PB2_I33A0 | MERIKELRNLMSQSRTREILTKTTVDHMAIIKKYTSGRQEKNPALRMKWMMAMKYPITADKRITEMIPERNEQGQTLWSKMNDAGSDRVMVSPLAVTWWNRNGPVTSTVHYPKIYKTYFEKVERLKHGTFGPVHFRNQVKIRRRVDINPGHADLSAKEAQDVIMEVVFPNEVGARILTSESQLTTTKEKKEELQGCKISPLMVAYMLERELVRKTRFLPVAGGTSSVYIEVLHLTQGTCWEQMYTPGGEARNDDVDQSLIIAARNIVRRATVSADPLASLLEMCHSTQIGGIRMVNILRQNPTEEQAVDICKAAMGLRIS... | null | null | 7-methylguanosine mRNA capping [GO:0006370]; cap snatching [GO:0075526]; DNA-templated transcription [GO:0006351]; negative stranded viral RNA replication [GO:0039689]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity [GO:0039545]; symbiont... | host cell mitochondrion [GO:0033650]; host cell nucleus [GO:0042025]; virion component [GO:0044423] | RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968] | PF20947;PF20948;PF20949;PF20950;PF00604;PF20951;PF20952; | 3.30.30.90; | Influenza viruses PB2 family | null | SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04062}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04062}. Host mitochondrion {ECO:0000255|HAMAP-Rule:MF_04062, ECO:0000269|PubMed:16242167, ECO:0000269|PubMed:1985200}. | null | null | null | null | null | FUNCTION: Plays an essential role in transcription initiation and cap-stealing mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. Recognizes and binds the 7-methylguanosine-containing cap of the target pre-RNA which is subsequently cleaved after 10-13 nucleotides by the ... | Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1)) |
P03428 | PB2_I34A1 | MERIKELRNLMSQSRTREILTKTTVDHMAIIKKYTSGRQEKNPALRMKWMMAMKYPITADKRITEMIPERNEQGQTLWSKMNDAGSDRVMVSPLAVTWWNRNGPITNTVHYPKIYKTYFERVERLKHGTFGPVHFRNQVKIRRRVDINPGHADLSAKEAQDVIMEVVFPNEVGARILTSESQLTITKEKKEELQDCKISPLMVAYMLERELVRKTRFLPVAGGTSSVYIEVLHLTQGTCWEQMYTPGGEVRNDDVDQSLIIAARNIVRRAAVSADPLASLLEMCHSTQIGGIRMVDILRQNPTEEQAVDICKAAMGLRIS... | null | null | 7-methylguanosine mRNA capping [GO:0006370]; cap snatching [GO:0075526]; DNA-templated transcription [GO:0006351]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity [GO:0039545]; symbiont-mediated suppression of host mRNA transcription via i... | extracellular region [GO:0005576]; host cell mitochondrion [GO:0033650]; host cell nucleus [GO:0042025]; virion component [GO:0044423] | RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968] | PF20947;PF20948;PF20949;PF20950;PF00604;PF20951;PF20952; | 3.30.30.90; | Influenza viruses PB2 family | null | SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04062}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04062, ECO:0000269|PubMed:15308710, ECO:0000269|PubMed:20538852}. Host mitochondrion {ECO:0000255|HAMAP-Rule:MF_04062, ECO:0000269|PubMed:15308710, ECO:0000269|PubMed:16242167, ECO:0000269|PubMed:20538852}. | null | null | null | null | null | FUNCTION: Plays an essential role in transcription initiation and cap-stealing mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. Recognizes and binds the 7-methylguanosine-containing cap of the target pre-RNA which is subsequently cleaved after 10-13 nucleotides by the ... | Influenza A virus (strain A/Puerto Rico/8/1934 H1N1) |
P03430 | RDRP_I33A0 | MDVNPTLLFLKVPAQNAISTTFPYTGDPPYSHGTGTGYTMDTVNRTHQYSERGRWTTNTETGAPQLNPIDGPLPEDNEPSGYAQTDCVLEAMAFLEESHPGIFETSCLETMEVVQQTRVDKLTQGRQTYDWTLNRNQPAATALANTIEVFRSNGLTANESGRLIDFLKDVMESMNKEEMEITTHFQRKRRVRDNMTKKMVTQRTIGKRKQRLNKRSYLIRALTLNTMTKDAERGKLKRRAIATPGMQIRGFVYFVETLARSICEKLEQSGLPVGGNEKKAKLANVVRKMMTNSQDTEISFTITGDNTKWNENQNPRMFLA... | 2.7.7.48 | null | DNA-templated transcription [GO:0006351]; negative stranded viral RNA replication [GO:0039689]; symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity [GO:0039523]; viral transcription [GO:0019083] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | nucleotide binding [GO:0000166]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968] | PF00602; | 6.10.140.720; | Influenza viruses polymerase PB1 family | PTM: Phosphorylated by host PRKCA. {ECO:0000255|HAMAP-Rule:MF_04065}. | SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04065}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04065}. | 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|HAMAP-Rule:MF_04065}; | null | null | null | null | FUNCTION: RNA-dependent RNA polymerase which is responsible for replication and transcription of virus RNA segments. The transcription of viral mRNAs occurs by a unique mechanism called cap-snatching. 5' methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides by PA. In turn, these short capped RNAs are us... | Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1)) |
P03431 | RDRP_I34A1 | MDVNPTLLFLKVPAQNAISTTFPYTGDPPYSHGTGTGYTMDTVNRTHQYSEKGRWTTNTETGAPQLNPIDGPLPEDNEPSGYAQTDCVLEAMAFLEESHPGIFENSCIETMEVVQQTRVDKLTQGRQTYDWTLNRNQPAATALANTIEVFRSNGLTANESGRLIDFLKDVMESMKKEEMGITTHFQRKRRVRDNMTKKMITQRTIGKKKQRLNKRSYLIRALTLNTMTKDAERGKLKRRAIATPGMQIRGFVYFVETLARSICEKLEQSGLPVGGNEKKAKLANVVRKMMTNSQDTELSFTITGDNTKWNENQNPRMFLA... | 2.7.7.48 | null | DNA-templated transcription [GO:0006351]; symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity [GO:0039523]; viral RNA genome replication [GO:0039694]; viral transcription [GO:0019083] | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | nucleotide binding [GO:0000166]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968] | PF00602; | 6.10.140.720; | Influenza viruses polymerase PB1 family | PTM: Phosphorylated by host PRKCA. {ECO:0000255|HAMAP-Rule:MF_04065, ECO:0000269|PubMed:19264651}. | SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04065, ECO:0000269|PubMed:19906916}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04065, ECO:0000269|PubMed:19906916}. | 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|HAMAP-Rule:MF_04065}; | null | null | null | null | FUNCTION: RNA-dependent RNA polymerase which is responsible for replication and transcription of virus RNA segments. The transcription of viral mRNAs occurs by a unique mechanism called cap-snatching. 5' methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides by PA. In turn, these short capped RNAs are us... | Influenza A virus (strain A/Puerto Rico/8/1934 H1N1) |
P03433 | PA_I34A1 | MEDFVRQCFNPMIVELAEKTMKEYGEDLKIETNKFAAICTHLEVCFMYSDFHFINEQGESIIVELGDPNALLKHRFEIIEGRDRTMAWTVVNSICNTTGAEKPKFLPDLYDYKENRFIEIGVTRREVHIYYLEKANKIKSEKTHIHIFSFTGEEMATKADYTLDEESRARIKTRLFTIRQEMASRGLWDSFRQSERGEETIEERFEITGTMRKLADQSLPPNFSSLENFRAYVDGFEPNGYIEGKLSQMSKEVNARIEPFLKTTPRPLRLPNGPPCSQRSKFLLMDALKLSIEDPSHEGEGIPLYDAIKCMRTFFGWKEP... | 3.1.-.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_04063, ECO:0000269|PubMed:26252962, ECO:0000269|PubMed:27088785}; Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-Rule:MF_04063, ECO:0000269|PubMed:26252962, ECO:0000269|PubMed:27088785}; | cap snatching [GO:0075526]; DNA-templated transcription [GO:0006351]; symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity [GO:0039523]; viral RNA genome replication [GO:0039694] | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; RNA binding [GO:0003723] | PF00603; | 3.40.91.90; | Influenza viruses PA family | PTM: Phosphorylated on serines and threonines by host kinases, including human casein kinase II. {ECO:0000255|HAMAP-Rule:MF_04063, ECO:0000269|PubMed:9519825}. | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04063}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04063}. Note=PB1 and PA are transported in the host nucleus as a complex. {ECO:0000255|HAMAP-Rule:MF_04063, ECO:0000269|PubMed:15308710, ECO:0000269|PubMed:22001919, ECO:0000269|PubMed:8113737}. | null | null | null | null | null | FUNCTION: Plays an essential role in viral RNA transcription and replication by forming the heterotrimeric polymerase complex together with PB1 and PB2 subunits. The complex transcribes viral mRNAs by using a unique mechanism called cap-snatching. It consists in the hijacking and cleavage of host capped pre-mRNAs. Thes... | Influenza A virus (strain A/Puerto Rico/8/1934 H1N1) |
P03435 | HEMA_I75A3 | MKTIIALSYIFCLVFAQDLPGNDNNSTATLCLGHHAVPNGTLVKTITNDQIEVTNATELVQSSSTGKICNNPHRILDGINCTLIDALLGDPHCDGFQNEKWDLFVERSKAFSNCYPYDVPDYASLRSLVASSGTLEFINEGFNWTGVTQNGGSSACKRGPDSGFFSRLNWLYKSGSTYPVQNVTMPNNDNSDKLYIWGVHHPSTDKEQTNLYVQASGKVTVSTKRSQQTIIPNVGSRPWVRGLSSRISIYWTIVKPGDILVINSNGNLIAPRGYFKMRTGKSSIMRSDAPIGTCSSECITPNGSIPNDKPFQNVNKITYG... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; viral budding from plasma membrane [GO:0046761]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | host cell surface receptor binding [GO:0046789]; identical protein binding [GO:0042802] | PF00509; | 3.90.20.10;3.90.209.20; | Influenza viruses hemagglutinin family | PTM: Palmitoylated. {ECO:0000255|HAMAP-Rule:MF_04072}.; PTM: In natural infection, inactive HA is matured into HA1 and HA2 outside the cell by one or more trypsin-like, arginine-specific endoprotease secreted by the bronchial epithelial cells. One identified protease that may be involved in this process is secreted in ... | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04072}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04072}. Note=Targeted to the apical plasma membrane ... | null | null | null | null | null | FUNCTION: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-i... | Influenza A virus (strain A/Victoria/3/1975 H3N2) |
P03436 | HEMA_I68A6 | MKTIIALSYIFCLALGQDLPGNDNNTATLCLGHHAVPNGTLVKTITDDQIEVTNATELVQSSSTGKICNNPHRILDGIDCTLIDALLGDPHCDVFQNETWDLFVERSKAFSNCYPYDVPDYASLRSLVASSGTLEFITEGFTWTGVTQNGGSNACKRGPDSGFFSRLNWLTKSGSTYPVLNVTMPNNDNFDKLYIWGVHHPSTNQEQTSLYVQASGRVTVSTRRSQQTIIPNIGSRPWVRGQSSRISIYWTIVKPGDVLVINSNGNLIAPRGYFKMRTGKSSIMRSDAPIDTCISECITPNGSIPNDKPFQNVNKITYGA... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; viral budding from plasma membrane [GO:0046761]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | host cell surface receptor binding [GO:0046789] | PF00509; | 3.90.20.10;3.90.209.20; | Influenza viruses hemagglutinin family | PTM: Palmitoylated. {ECO:0000255|HAMAP-Rule:MF_04072}.; PTM: In natural infection, inactive HA is matured into HA1 and HA2 outside the cell by one or more trypsin-like, arginine-specific endoprotease secreted by the bronchial epithelial cells. One identified protease that may be involved in this process is secreted in ... | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04072}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04072}. Note=Targeted to the apical plasma membrane ... | null | null | null | null | null | FUNCTION: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-i... | Influenza A virus (strain A/Northern Territory/60/1968 H3N2) (Influenza A virus (strain NT60)) (Influenza A virus (strain A/NT/60/1968 H3N2)) |
P03437 | HEMA_I68A0 | MKTIIALSYIFCLALGQDLPGNDNSTATLCLGHHAVPNGTLVKTITDDQIEVTNATELVQSSSTGKICNNPHRILDGIDCTLIDALLGDPHCDVFQNETWDLFVERSKAFSNCYPYDVPDYASLRSLVASSGTLEFITEGFTWTGVTQNGGSNACKRGPGSGFFSRLNWLTKSGSTYPVLNVTMPNNDNFDKLYIWGIHHPSTNQEQTSLYVQASGRVTVSTRRSQQTIIPNIGSRPWVRGLSSRISIYWTIVKPGDVLVINSNGNLIAPRGYFKMRTGKSSIMRSDAPIDTCISECITPNGSIPNDKPFQNVNKITYGA... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; viral budding from plasma membrane [GO:0046761]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | host cell surface receptor binding [GO:0046789] | PF00509; | 3.90.20.10;3.90.209.20; | Influenza viruses hemagglutinin family | PTM: Palmitoylated. {ECO:0000255|HAMAP-Rule:MF_04072}.; PTM: In natural infection, inactive HA is matured into HA1 and HA2 outside the cell by one or more trypsin-like, arginine-specific endoprotease secreted by the bronchial epithelial cells. One identified protease that may be involved in this process is secreted in ... | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04072}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04072}. Note=Targeted to the apical plasma membrane ... | null | null | null | null | null | FUNCTION: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-i... | Influenza A virus (strain A/Aichi/2/1968 H3N2) |
P03451 | HEMA_I57A0 | MAIIYLILLFTAVRGDQICIGYHANNSTEKVDTNLERNVTVTHAKDILEKTHNGKLCKLNGIPPLELGDCSIAGWLLGNPECDRLLSVPEWSYIMEKENPRDGLCYPGSFNDYEELKHLLSSVKHFEKVKILPKDRWTQHTTTGGSRACAVSGNPSFFRNMVWLTKEGSDYPVAKGSYNNTSGEQMLIIWGVHHPIDETEQRTLYQNVGTYVSVGTSTLNKRSTPEIATRPKVNGQGGRMEFSWTLLDMWDTINFESTGNLIAPEYGFKISKRGSSGIMKTEGTLENCETKCQTPLGAINTTLPFHNVHPLTIGECPKYV... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; viral budding from plasma membrane [GO:0046761]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | host cell surface receptor binding [GO:0046789] | PF00509; | 3.90.20.10;3.90.209.20;2.10.77.10; | Influenza viruses hemagglutinin family | PTM: Palmitoylated. {ECO:0000255|HAMAP-Rule:MF_04072, ECO:0000269|PubMed:2249653}.; PTM: In natural infection, inactive HA is matured into HA1 and HA2 outside the cell by one or more trypsin-like, arginine-specific endoprotease secreted by the bronchial epithelial cells. One identified protease that may be involved in ... | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04072}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04072}. Note=Targeted to the apical plasma membrane ... | null | null | null | null | null | FUNCTION: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-i... | Influenza A virus (strain A/Japan/305/1957 H2N2) |
P03452 | HEMA_I34A1 | MKANLLVLLCALAAADADTICIGYHANNSTDTVDTVLEKNVTVTHSVNLLEDSHNGKLCRLKGIAPLQLGKCNIAGWLLGNPECDPLLPVRSWSYIVETPNSENGICYPGDFIDYEELREQLSSVSSFERFEIFPKESSWPNHNTNGVTAACSHEGKSSFYRNLLWLTEKEGSYPKLKNSYVNKKGKEVLVLWGIHHPPNSKEQQNLYQNENAYVSVVTSNYNRRFTPEIAERPKVRDQAGRMNYYWTLLKPGDTIIFEANGNLIAPMYAFALSRGFGSGIITSNASMHECNTKCQTPLGAINSSLPYQNIHPVTIGECP... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; viral budding from plasma membrane [GO:0046761]; virion attachment to host cell [GO:0019062] | extracellular region [GO:0005576]; host cell plasma membrane [GO:0020002]; plasma membrane [GO:0005886]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | host cell surface receptor binding [GO:0046789] | PF00509; | 3.90.20.10;3.90.209.20;2.10.77.10; | Influenza viruses hemagglutinin family | PTM: Palmitoylated. {ECO:0000255|HAMAP-Rule:MF_04072}.; PTM: In natural infection, inactive HA is matured into HA1 and HA2 outside the cell by one or more trypsin-like, arginine-specific endoprotease secreted by the bronchial epithelial cells. One identified protease that may be involved in this process is secreted in ... | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04072, ECO:0000305}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04072, ECO:0000305}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04072, ECO:0000305}. Note=... | null | null | null | null | null | FUNCTION: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin-independent pathway. Plays a major role in the determin... | Influenza A virus (strain A/Puerto Rico/8/1934 H1N1) |
P03454 | HEMA_I33A0 | MKAKLLVLLYAFVATDADTICIGYHANNSTDTVDTIFEKNVAVTHSVNLLEDRHNGKLCKLKGIAPLQLGKCNITGWLLGNPECDSLLPARSWSYIVETPNSENGACYPGDFIDYEELREQLSSVSSLERFEIFPKESSWPNHTFNGVTVSCSHRGKSSFYRNLLWLTKKGDSYPKLTNSYVNNKGKEVLVLWGVHHPSSSDEQQSLYSNGNAYVSVASSNYNRRFTPEIAARPKVKDQHGRMNYYWTLLEPGDTIIFEATGNLIAPWYAFALSRGFESGIITSNASMHECNTKCQTPQGSINSNLPFQNIHPVTIGECP... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; viral budding from plasma membrane [GO:0046761]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | host cell surface receptor binding [GO:0046789] | PF00509; | 3.90.20.10;3.90.209.20;2.10.77.10; | Influenza viruses hemagglutinin family | PTM: Palmitoylated. {ECO:0000255|HAMAP-Rule:MF_04072}.; PTM: In natural infection, inactive HA is matured into HA1 and HA2 outside the cell by one or more trypsin-like, arginine-specific endoprotease secreted by the bronchial epithelial cells. One identified protease that may be involved in this process is secreted in ... | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04072}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04072, ECO:0000269|PubMed:10864667}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04072, ECO:0000269|PubM... | null | null | null | null | null | FUNCTION: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-i... | Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1)) |
P03459 | HEMA_I34A0 | MNTQILVFALVAVIPTNADKICLGHHAVSNGTKVNTLTERGVEVVNATETVERTNIPKICSKGKRTTDLGQCGLLGTITGPPQCDQFLEFSADLIIERREGNDVCYPGKFVNEEALRQILRGSGGIDKETMGFTYSGIRTNGTTSACRRSGSSFYAEMEWLLSNTDNASFPQMTKSYKNTRRESALIVWGIHHSGSTTEQTKLYGSGNKLITVGSSKYHQSFVPSPGTRPQINGQSGRIDFHWLILDPNDTVTFSFNGAFIAPNRASFLRGKSMGIQSDVQVDANCEGECYHSGGTITSRLPFQNINSRAVGKCPRYVKQ... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; viral budding from plasma membrane [GO:0046761]; virion attachment to host cell [GO:0019062] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | host cell surface receptor binding [GO:0046789] | PF00509; | 3.90.20.10;3.90.209.20; | Influenza viruses hemagglutinin family | PTM: Palmitoylated. {ECO:0000255|HAMAP-Rule:MF_04072}.; PTM: In natural infection, inactive HA is matured into HA1 and HA2 outside the cell by one or more trypsin-like, arginine-specific endoprotease secreted by the bronchial epithelial cells. One identified protease that may be involved in this process is secreted in ... | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04072}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04072}. Note=Targeted to the apical plasma membrane ... | null | null | null | null | null | FUNCTION: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-i... | Influenza A virus (strain A/Fowl plague virus/Rostock/8/1934 H7N1) |
P03466 | NCAP_I34A1 | MASQGTKRSYEQMETDGERQNATEIRASVGKMIGGIGRFYIQMCTELKLSDYEGRLIQNSLTIERMVLSAFDERRNKYLEEHPSAGKDPKKTGGPIYRRVNGKWMRELILYDKEEIRRIWRQANNGDDATAGLTHMMIWHSNLNDATYQRTRALVRTGMDPRMCSLMQGSTLPRRSGAAGAAVKGVGTMVMELVRMIKRGINDRNFWRGENGRKTRIAYERMCNILKGKFQTAAQKAMMDQVRESRNPGNAEFEDLTFLARSALILRGSVAHKSCLPACVYGPAVASGYDFEREGYSLVGIDPFRLLQNSQVYSLIRPNE... | null | null | symbiont entry into host cell [GO:0046718]; viral penetration into host nucleus [GO:0075732] | extracellular region [GO:0005576]; helical viral capsid [GO:0019029]; host cell [GO:0043657]; host cell nucleus [GO:0042025]; plasma membrane [GO:0005886]; ribonucleoprotein complex [GO:1990904]; viral nucleocapsid [GO:0019013] | identical protein binding [GO:0042802]; RNA binding [GO:0003723]; structural molecule activity [GO:0005198] | PF00506; | null | Influenza viruses nucleoprotein family | PTM: Late in virus-infected cells, may be cleaved from a 56-kDa protein to a 53-kDa protein by a cellular caspase. This cleavage might be a marker for the onset of apoptosis in infected cells or have a specific function in virus host interaction. {ECO:0000255|HAMAP-Rule:MF_04070}. | SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04070}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04070, ECO:0000269|PubMed:9770415, ECO:0000269|PubMed:9971805}. | null | null | null | null | null | FUNCTION: Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse thr... | Influenza A virus (strain A/Puerto Rico/8/1934 H1N1) |
P03468 | NRAM_I34A1 | MNPNQKIITIGSICLVVGLISLILQIGNIISIWISHSIQTGSQNHTGICNQNIITYKNSTWVKDTTSVILTGNSSLCPIRGWAIYSKDNSIRIGSKGDVFVIREPFISCSHLECRTFFLTQGALLNDKHSNGTVKDRSPYRALMSCPVGEAPSPYNSRFESVAWSASACHDGMGWLTIGISGPDNGAVAVLKYNGIITETIKSWRKKILRTQESECACVNGSCFTIMTDGPSDGLASYKIFKIEKGKVTKSIELNAPNSHYEECSCYPDTGKVMCVCRDNWHGSNRPWVSFDQNLDYQIGYICSGVFGDNPRPEDGTGSC... | 3.2.1.18 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|HAMAP-Rule:MF_04071}; | carbohydrate metabolic process [GO:0005975]; immune response [GO:0006955]; viral budding from plasma membrane [GO:0046761]; viral release from host cell [GO:0019076] | extracellular region [GO:0005576]; host cell plasma membrane [GO:0020002]; plasma membrane [GO:0005886]; virion membrane [GO:0055036] | exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; exo-alpha-sialidase activity [GO:0004308]; metal ion binding [GO:0046872]; peptidase activator activity [GO:0016504] | PF00064; | 2.120.10.10; | Glycosyl hydrolase 34 family | PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04071}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04071}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04071}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04071}. Note=Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the... | CATALYTIC ACTIVITY: Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18; Evidence={ECO:0000255|HAMAP-Rule:MF_04071}; | null | null | null | null | FUNCTION: Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell ... | Influenza A virus (strain A/Puerto Rico/8/1934 H1N1) |
P03470 | NRAM_I33A0 | MNPNQKIITIGSICMVVGIISLILQIGNIISIWISHSIQTGNQNHTGICNQGIITYNVVAGQDSTSVILTGNSSLCPIRGWAIHSKDNGIRIGSKGDVFVIREPFISCSHLECRTFFLTQGALLNDKHSNGTVKDRSPYRALMSCPVGEAPSPYNSRFESVAWSASACHDGMGWLTIGISGPDNGAVAVLKYNGIITETIKSWRKKILRTQESECTCVNGSCFTIMTDGPSNGLASYKIFKIEKGKVTKSIELNAPNSHYEECSCYPDTGKVMCVCRDNWHGSNRPWVSFDQNLDYQIGYICSGVFGDNPRPKDGPGSCG... | 3.2.1.18 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|HAMAP-Rule:MF_04071}; | carbohydrate metabolic process [GO:0005975]; viral budding from plasma membrane [GO:0046761] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; metal ion binding [GO:0046872] | PF00064; | 2.120.10.10; | Glycosyl hydrolase 34 family | PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04071}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:10864667}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:10864667}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:10864667}. Note=Preferentially accumul... | CATALYTIC ACTIVITY: Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18; Evidence={ECO:0000255|HAMAP-Rule:MF_04071}; | null | null | null | null | FUNCTION: Unlike other strains, A/WSN/33 neuraminidase binds and activates plasminogen into plasmin in the vicinity of HA so that activated plasmin cleaves HA rendering the virus infectious. {ECO:0000269|PubMed:16140748}.; FUNCTION: Catalyzes the removal of terminal sialic acid residues from viral and cellular glycocon... | Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1)) |
P03472 | NRAM_I75A5 | MNPNQKILCTSATALVIGTIAVLIGITNLGLNIGLHLKPSCNCSHSQPEATNASQTIINNYYNDTNITQISNTNIQVEERAIRDFNNLTKGLCTINSWHIYGKDNAVRIGEDSDVLVTREPYVSCDPDECRFYALSQGTTIRGKHSNGTIHDRSQYRALISWPLSSPPTVYNSRVECIGWSSTSCHDGKTRMSICISGPNNNASAVIWYNRRPVTEINTWARNILRTQESECVCHNGVCPVVFTDGSATGPAETRIYYFKEGKILKWEPLAGTAKHIEECSCYGERAEITCTCRDNWQGSNRPVIRIDPVAMTHTSQYIC... | 3.2.1.18 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872, ECO:0000269|PubMed:8371267, ECO:0000269|PubMed:9342319}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872, ECO:0000269|PubMed:83... | carbohydrate metabolic process [GO:0005975]; viral budding from plasma membrane [GO:0046761] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; metal ion binding [GO:0046872] | PF00064; | 2.120.10.10; | Glycosyl hydrolase 34 family | PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872, ECO:0000269|PubMed:9342319}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04071}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04071}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04071}. Note=Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the... | CATALYTIC ACTIVITY: Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18; Evidence={ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:23429702}; | null | null | null | null | FUNCTION: Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell ... | Influenza A virus (strain A/Tern/Australia/G70C/1975 H11N9) |
P03474 | NRAM_INBLE | MLPSTVQTLTLLLTSGGVLLSLYVSASLSYLLYSDVLLKFSSTKTTAPTMSLECTNASNAQTVNHSATKEMTFPPPEPEWTYPRLSCQGSTFQKALLISPHRFGEIKGNSAPLIIREPFVACGPKECRHFALTHYAAQPGGYYNGTRKDRNKLRHLVSVKLGKIPTVENSIFHMAAWSGSACHDGREWTYIGVDGPDNDALVKIKYGEAYTDTYHSYAHNILRTQESACNCIGGDCYLMITDGSASGISKCRFLKIREGRIIKEILPTGRVEHTEECTCGFASNKTIECACRDNSYTAKRPFVKLNVETDTAEIRLMCTK... | 3.2.1.18 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:10547289, ECO:0000269|PubMed:15159560, ECO:0000269|PubMed:7880809}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:10547289, ECO:0000269|PubMed:15159560, ECO:0000269|PubMed:7880809}; | carbohydrate metabolic process [GO:0005975]; viral budding from plasma membrane [GO:0046761] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; metal ion binding [GO:0046872] | PF00064; | 2.120.10.10; | Glycosyl hydrolase 34 family | PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:7880809}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04071}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04071}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04071}. Note=Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the... | CATALYTIC ACTIVITY: Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18; Evidence={ECO:0000255|HAMAP-Rule:MF_04071}; | null | null | null | null | FUNCTION: Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell ... | Influenza B virus (strain B/Lee/1940) |
P03485 | M1_I34A1 | MSLLTEVETYVLSIIPSGPLKAEIAQRLEDVFAGKNTDLEVLMEWLKTRPILSPLTKGILGFVFTLTVPSERGLQRRRFVQNALNGNGDPNNMDKAVKLYRKLKREITFHGAKEISLSYSAGALASCMGLIYNRMGAVTTEVAFGLVCATCEQIADSQHRSHRQMVTTTNPLIRHENRMVLASTTAKAMEQMAGSSEQAAEAMEVASQARQMVQAMRTIGTHPSSSAGLKNDLLENLQAYQKRMGVQMQRFK | null | null | viral budding from plasma membrane [GO:0046761] | extracellular region [GO:0005576]; host cell nucleus [GO:0042025]; plasma membrane [GO:0005886]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural constituent of virion [GO:0039660] | PF00598;PF08289; | 1.10.10.180;1.20.91.10; | Influenza viruses Matrix protein M1 family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04068}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04068}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04068}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04068}. | null | null | null | null | null | FUNCTION: Plays critical roles in virus replication, from virus entry and uncoating to assembly and budding of the virus particle. M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral transcription. Interaction of viral NEP with M1-RNP is thought to promote nuclear export of the complex, which is ta... | Influenza A virus (strain A/Puerto Rico/8/1934 H1N1) |
P03492 | M2_I34A0 | MSLLTEVETPTRNGWECRCNDSSDPLIIAASIIGILHLILWILNRLFFKCIYRRLKYGLKRGPSTEGVPESMREEYRQEQQSAVDVDDGHFVNIELE | null | null | protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078] | PF00599; | 6.10.250.1640; | Influenza viruses matrix protein M2 family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximit... | null | null | null | null | null | FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is... | Influenza A virus (strain A/Fowl plague virus/Rostock/8/1934 H7N1) |
P03495 | NS1_I72A2 | MDSNTVSSFQVDCFLWHVRKQVVDQELGDAPFLDRLRRDQKSLRGRGSTLGLNIEAATHVGKQIVEKILKEESDEALKMTMASTPASRYITDMTIEELSRDWFMLMPKQKVEGPLCIRIDQAIMDKNIMLKANFSVIFDRLETLILLRAFTEEGAIVGEISPLPSFPGHTIEDVKNAIGVLIGGLEWNDNTVRVSKTLQRFAWGSSNENGRPPLTPKQKRKMARTARSKVRRDKMAD | null | null | symbiont-mediated suppression of host cytokine production [GO:0140133]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity [GO:0039540]; symbiont-mediated suppression of host innate immune response [GO:0052170]; symbiont-mediated suppression... | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | double-stranded RNA binding [GO:0003725]; identical protein binding [GO:0042802]; protein serine/threonine kinase inhibitor activity [GO:0030291] | PF00600; | 3.30.420.330;1.10.287.10; | Influenza A viruses NS1 family | PTM: Upon interferon induction, ISGylated via host HERC5; this results in the impairment of NS1 interaction with RNA targets due to its inability to form homodimers and to interact with host EIF2AK2/PKR. {ECO:0000255|HAMAP-Rule:MF_04066}. | SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04066}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04066}. Note=In uninfected, transfected cells, NS1 is localized in the nucleus. Only in virus infected cells, the nuclear export signal is unveiled, presumably by a viral protein, and a fraction of NS1 is exp... | null | null | null | null | null | FUNCTION: Inhibits post-transcriptional processing of cellular pre-mRNA, by binding and inhibiting two cellular proteins that are required for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage and polyadenylation specificity factor/CPSF4 and the poly(A)-binding protein 2/PABPN1. In turn, unprocessed 3' e... | Influenza A virus (strain A/Udorn/307/1972 H3N2) |
P03496 | NS1_I34A1 | MDPNTVSSFQVDCFLWHVRKRVADQELGDAPFLDRLRRDQKSLRGRGSTLGLDIETATRAGKQIVERILKEESDEALKMTMASVPASRYLTDMTLEEMSRDWSMLIPKQKVAGPLCIRMDQAIMDKNIILKANFSVIFDRLETLILLRAFTEEGAIVGEISPLPSLPGHTAEDVKNAVGVLIGGLEWNDNTVRVSETLQRFAWRSSNENGRPPLTPKQKREMAGTIRSEV | null | null | symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity [GO:0039540]; symbiont-mediated suppression of host mRNA processing [GO:0039524]; symbiont-mediated suppression of host PKR/eIFalpha signaling [GO:0039580]; symbiont-mediated suppression of ... | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | identical protein binding [GO:0042802]; protein serine/threonine kinase inhibitor activity [GO:0030291]; RNA binding [GO:0003723] | PF00600; | 3.30.420.330;1.10.287.10; | Influenza A viruses NS1 family | PTM: Upon interferon induction, ISGylated via host HERC5; this results in the impairment of NS1 interaction with RNA targets due to its inability to form homodimers and to interact with host EIF2AK2/PKR. There are two ISGylated forms: one form is ISGylated at Lys-20, Lys-41, Lys-217, and Lys-219, and another one at Lys... | SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04066}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04066}. Note=In uninfected, transfected cells, NS1 is localized in the nucleus. Only in virus infected cells, the nuclear export signal is unveiled, presumably by a viral protein, and a fraction of NS1 is exp... | null | null | null | null | null | FUNCTION: Inhibits post-transcriptional processing of cellular pre-mRNA, by binding and inhibiting two cellular proteins that are required for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage and polyadenylation specificity factor/CPSF4 and the poly(A)-binding protein 2/PABPN1. In turn, unprocessed 3' e... | Influenza A virus (strain A/Puerto Rico/8/1934 H1N1) |
P03502 | NS1_INBLE | MADNMTTTQIEVGPGATNATINFEAGILECYERFSWQRALDYPGQDRLHRLKRKLESRIKTHNKSEPENKRMSLEERKAIGVKMMKVLLFMDPSAGIEGFEPYCVKNPSTSKCPNYDWTDYPPTPGKYLDDIEEEPENVDHPIEVVLRDMNNKDARQKIKDEVNTQKEGKFRLTIKRDIRNVLSLRVLVNGTFLKHPNGDKSLSTLHRLNAYDQNGGLVAKLVATDDRTVEDEKDGHRILNSLFERFDEGHSKPIRAAETAVGVLSQFGQEHRLSPEEGDN | null | null | symbiont-mediated suppression of host ISG15-protein conjugation [GO:0039579]; symbiont-mediated suppression of host PKR/eIFalpha signaling [GO:0039580]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | protein serine/threonine kinase inhibitor activity [GO:0030291]; RNA binding [GO:0003723] | PF02942; | 1.10.287.10; | Influenza B viruses NS1 family | null | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04066}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04066}. | null | null | null | null | null | FUNCTION: Binds and inhibits the conjugation of the ubiquitin-like G1P2/ISG15 protein to its target proteins. Since G1P2/ISG15 is an early antiviral protein, NS1 may inhibit the host antiviral response. Prevents EIF2AK2/PKR activation, either by binding double strand RNA or by interacting directly with EIF2AK2/PKR. Als... | Influenza B virus (strain B/Lee/1940) |
P03517 | GP_PTPV | MIFTILNVLTRAMLVMSMYSLTTWDSTSRNDMCFSNDSPLEGLVYYWETHSKRHDYKKQESQRCRVGDSDKKMITNVTIISLISEIQKSISELSLSCVNDDNSTGQVLTFNGLEDTIRGDYIVDCVTGLYQSDIGVGVGLGRTHHGHQQMKNKAVVIDEKERMISLLETQQSENDIKMQVLMSEIEQLKNQLSKKRNERGQEKRDAEKVMSDLMARNSDLRKHNDILTAEISQMKNKNTIQRNKNTVSTTVVPAILSVALLSSSVAPIIAAPPDSPMINPWPHAKNRVGTGMYKYDENDDSGCRPIRYGVSCIGFDFMLK... | null | null | entry receptor-mediated virion attachment to host cell [GO:0098670]; fusion of virus membrane with host endosome membrane [GO:0039654]; symbiont entry into host cell [GO:0046718] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; membrane [GO:0016020]; virion membrane [GO:0055036] | null | PF19019;PF07243;PF07245;PF07246; | 2.60.40.3770;2.60.98.50; | Phlebovirus envelope glycoprotein family | PTM: [Envelopment polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins including NSm protein, Glycoprotein C, and Glycoprotein N. {ECO:0000250|UniProtKB:P21401}.; PTM: [Glycoprotein N]: Glycosylated. The glycans can attach to host CD209/DC-SIGN, and may play a role in virus entry into dendritic cell... | SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host endoplasmic reticulum membran... | null | null | null | null | null | FUNCTION: [Glycoprotein N]: Structural component of the virion that interacts with glycoprotein C (By similarity). It shields the hydrophobic fusion loops of the glycoprotein C, preventing premature fusion (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (By ... | Punta toro phlebovirus |
P03518 | GP_RVFV | MYVLLTILISVLVCEAVIRVSLSSTREETCFGDSTNPEMIEGAWDSLREEEMPEELSCSISGIREVKTSSQELYRALKAIIAADGLNNITCHGKDPEDKISLIKGPPHKKRVGIVRCERRRDAKQIGRETMAGIAMTVLPALAVFALAPVVFAEDPHLRNRPGKGHNYIDGMTQEDATCKPVTYAGACSSFDVLLEKGKFPLFQSYAHHRTLLEAVHDTIIAKADPPSCDLQSAHGNPCMKEKLVMKTHCPNDYQSAHYLNNDGKMASVKCPPKYGLTEDCNFCRQMTGASLKKGSYPLQDLFCQSSEDDGSKLKTKMKG... | null | null | entry receptor-mediated virion attachment to host cell [GO:0098670]; fusion of virus membrane with host endosome membrane [GO:0039654]; symbiont entry into host cell [GO:0046718] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; host cell mitochondrial outer membrane [GO:0044193]; membrane [GO:0016020]; virion membrane [GO:0055036] | null | PF19019;PF07243;PF07245;PF07246; | 2.60.40.3770;2.60.98.50; | Phlebovirus envelope glycoprotein family | PTM: [Envelopment polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins including NSm protein, Glycoprotein C, and Glycoprotein N. {ECO:0000250|UniProtKB:P21401}.; PTM: [Glycoprotein N]: Glycosylated (By similarity). The glycans can attach to host CD209/DC-SIGN, and may play a role in virus entry int... | SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:P09613}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P09613}. Host endoplasmic reticulum membran... | null | null | null | null | null | FUNCTION: [Glycoprotein N]: Structural component of the virion that interacts with glycoprotein C (By similarity). It shields the hydrophobic fusion loops of the glycoprotein C, preventing premature fusion (By similarity). The glycoprotein protrusions are arranged on an icosahedral lattice, with T=12 triangulation (Pub... | Rift valley fever virus (RVFV) |
P03519 | MATRX_VSIVA | MSSLKKILGLKGKGKKSKKLGIAPPPYEEDTSMEYAPSAPIDKSYFGVDEMDTYDPNQLRYEKFFFTVKMTVRSNRPFRTYSDVAAAVSHWDHMYIGMAGKRPFYKILAFLGSSNLKATPAVLADQGQPEYHTHCEGRAYLPHRMGKTPPMLNVPEHFRRPFNIGLYKGTIELTMTIYDDESLEAAPMIWDHFNSSKFSDFREKALMFGLIVEKKASGAWVLDSISHFK | null | null | phosphorylation [GO:0016310]; suppression by virus of host mRNA export from nucleus [GO:0039522]; symbiont-mediated suppression of host transcription initiation from RNA polymerase II promoter [GO:0039602]; viral budding via host ESCRT complex [GO:0039702] | host cell cytoplasm [GO:0030430]; host cell nuclear membrane [GO:0044200]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural constituent of virion [GO:0039660] | PF06326; | 3.10.460.10; | Vesiculoviruses matrix protein family | PTM: Phosphorylated by host. {ECO:0000269|PubMed:1323702}. | SUBCELLULAR LOCATION: Virion membrane; Peripheral membrane protein {ECO:0000269|PubMed:1850035}. Host endomembrane system; Peripheral membrane protein. Host nucleus membrane; Peripheral membrane protein. Host nucleus {ECO:0000269|PubMed:28888655}. Host cytoplasm {ECO:0000269|PubMed:28888655}. | null | null | null | null | null | FUNCTION: Plays a major role in assembly and budding of virion, by recruiting cellular partners of the ESCRT complexes that play a key role in releasing the budding particle from the host membrane. Condensates the ribonucleocapsid core during virus assembly. {ECO:0000269|PubMed:16298982, ECO:0000269|PubMed:20943988}.; ... | Vesicular stomatitis Indiana virus (strain San Juan) (VSIV) |
P03520 | PHOSP_VSIVA | MDNLTKVREYLKSYSRLDQAVGEIDEIEAQRAEKSNYELFQEDGVEEHTKPSYFQAADDSDTESEPEIEDNQGLYAQDPEAEQVEGFIQGPLDDYADEEVDVVFTSDWKPPELESDEHGKTLRLTSPEGLSGEQKSQWLSTIKAVVQSAKYWNLAECTFEASGEGVIMKERQITPDVYKVTPVMNTHPSQSEAVSDVWSLSKTSMTFQPKKASLQPLTISLDELFSSRGEFISVGGDGRMSHKEAILLGLRYKKLYNQARVKYSL | null | null | phosphorylation [GO:0016310]; viral genome replication [GO:0019079]; viral transcription [GO:0019083] | host cell cytoplasm [GO:0030430]; virion component [GO:0044423] | RNA folding chaperone [GO:0140691]; RNA-dependent RNA polymerase activity [GO:0003968] | PF00922; | 6.10.140.830;1.10.8.440; | Vesiculovirus protein P family | PTM: Domain I is phosphorylated by host CK2. Domain II is phosphorylated by other unknown kinases. Phosphorylation play an important role in facilitating trimerization and possibly P-L complex formation (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Virion. Host cytoplasm. | null | null | null | null | null | FUNCTION: Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template. May act as a chaperone for newly synthesized free N protein, so-called N(0). Plays a role in virion assembly. {ECO:0000269|PubMed:15163735, ECO:0000... | Vesicular stomatitis Indiana virus (strain San Juan) (VSIV) |
P03522 | GLYCO_VSIVA | MKCLLYLAFLFIGVNCKFTIVFPHNQKGNWKNVPSNYHYCPSSSDLNWHNDLIGTAIQVKMPKSHKAIQADGWMCHASKWVTTCDFRWYGPKYITQSIRSFTPSVEQCKESIEQTKQGTWLNPGFPPQSCGYATVTDAEAVIVQVTPHHVLVDEYTGEWVDSQFINGKCSNYICPTVHNSTTWHSDYKVKGLCDSNLISMDITFFSEDGELSSLGKEGTGFRSNYFAYETGGKACKMQYCKHWGVRLPSGVWFEMADKDLFAAARFPECPEGSSISAPSQTSVDVSLIQDVERILDYSLCQETWSKIRAGLPISPVDLSY... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062] | host cell membrane [GO:0033644]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00974; | 2.30.29.130;2.30.30.640; | Vesiculovirus glycoprotein family | PTM: Glycosylated by host. {ECO:0000269|PubMed:6326102}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:1850035, ECO:0000269|PubMed:8144707}; Single-pass type I membrane protein {ECO:0000269|PubMed:8144707}. Host membrane {ECO:0000269|PubMed:8144707}; Single-pass type I membrane protein {ECO:0000269|PubMed:8144707}. Note=The cytoplasmic domain sorts the protein to... | null | null | null | null | null | FUNCTION: Attaches the virus to host LDL receptors, inducing clathrin-dependent endocytosis of the virion. {ECO:0000269|PubMed:20941355, ECO:0000269|PubMed:23589850}.; FUNCTION: In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and endosomal mem... | Vesicular stomatitis Indiana virus (strain San Juan) (VSIV) |
P03523 | L_VSIVA | MEVHDFETDEFNDFNEDDYATREFLNPDERMTYLNHADYNLNSPLISDDIDNLIRKFNSLPIPSMWDSKNWDGVLEMLTSCQANPISTSQMHKWMGSWLMSDNHDASQGYSFLHEVDKEAEITFDVVETFIRGWGNKPIEYIKKERWTDSFKILAYLCQKFLDLHKLTLILNAVSEVELLNLARTFKGKVRRSSHGTNICRIRVPSLGPTFISEGWAYFKKLDILMDPNFLLMVKDVIIGRMQTVLSMVCRIDNLFSEQDIFSLLNIYRIGDKIVERQGNFSYDLIKMVEPICNLKLMKLARESRPLVPQFPHFENHIKT... | 2.1.1.375; 2.7.7.48; 2.7.7.88; 3.6.1.- | null | negative stranded viral RNA replication [GO:0039689]; viral transcription [GO:0019083] | host cell cytoplasm [GO:0030430]; virion component [GO:0044423] | ATP binding [GO:0005524]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; RNA-dependent RNA polymerase activity [GO:0003968] | PF21080;PF14314;PF21081;PF14318;PF00946; | 3.40.50.150; | Rhabdoviridae protein L family | null | SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:24055706}. Host cytoplasm {ECO:0000269|PubMed:2999788}. Note=L and P are packaged asymmetrically towards the blunt end of the virus. {ECO:0000269|PubMed:24055706}. | 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=GTP + H2... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.5 uM for mRNA (nucleoside-2'-O-)-methyltransferase {ECO:0000269|PubMed:201777}; KM=10 uM for mRNA (guanine-N(7)-)-methyltransferase {ECO:0000269|PubMed:201777}; | null | null | null | FUNCTION: Responsible for RNA synthesis (replicase and transcriptase), cap addition, and cap methylation (PubMed:24526687). Performs also the polyadenylation of subgenomic mRNAs by a stuttering mechanism at a slipery stop site present at the end of viral genes (By similarity). The template is composed of the viral RNA ... | Vesicular stomatitis Indiana virus (strain San Juan) (VSIV) |
P03533 | VP7_ROTS1 | MYGIEYTTVLTFLISIILLNYILKSLTRIMDCIIYRLLFIIVILSPFLRAQNYGINLPITGSMDTAYANSTQEETFLTSTLCLYYPTEAATEINDNSWKDTLSQLFLTKGWPTGSVYFKEYTNIASFSVDPQLYCDYNVVLMKYDATLQLDMSELADLILNEWLCNPMDITLYYYQQTDEANKWISMGSSCTIKVCPLNTQTLGIGCLTTDATTFEEVATAEKLVITDVVDGVNHKLDVTTATCTIRNCKKLGPRENVAVIQVGGSDILDITADPTTAPQTERMMRINWKKWWQVFYTVVDYVDQIIQVMSKRSRSLNSA... | null | null | receptor-mediated virion attachment to host cell [GO:0046813] | host cell endoplasmic reticulum lumen [GO:0044166]; T=13 icosahedral viral capsid [GO:0039621]; viral outer capsid [GO:0039624] | metal ion binding [GO:0046872] | PF00434; | 3.40.50.11130;2.60.120.800; | Rotavirus VP7 family | PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04131, ECO:0000269|PubMed:2995404}.; PTM: The N-terminus is blocked possibly by pyroglutamic acid. {ECO:0000255|HAMAP-Rule:MF_04131, ECO:0000269|PubMed:2826493}. | SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04131}. Host endoplasmic reticulum lumen {ECO:0000255|HAMAP-Rule:MF_04131}. Note=The outer layer contains 780 copies of VP7, grouped as 260 trimers. Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, ... | null | null | null | null | null | FUNCTION: Calcium-binding protein that interacts with rotavirus cell receptors once the initial attachment by VP4 has been achieved (By similarity). Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors (Pub... | Rotavirus A (strain RVA/SA11-Both/G3P5B[2]) (RV-A) (Simian Agent 11 (strain Both)) |
P03540 | GLYC_PIARV | MGQIVTLIQSIPEVLQEVFNVALIIVSVLCIVKGFVNLMRCGLFQLVTFLILSGRSCDSMMIDRRHNLTHVEFNLTRMFDNLPQSCSKNNTHHYYKGPSNTTWGIELTLTNTSIANETSGNFSNIGSLGYGNISNCDRTREAGHTLKWLLNELHFNVLHVTRHIGARCKTVEGAGVLIQYNLTVGDRGGEVGRHLIASLAQIIGDPKIAWVGKCFNNCSGDTCRLTNCEGGTHYNFLIIQNTTWENHCTYTPMATIRMALQRTAYSSVSRKLLGFFTWDLSDSSGQHVPGGYCLEQWAIIWAGIKCFDNTVMAKCNKDHN... | null | null | fusion of virus membrane with host endosome membrane [GO:0039654]; receptor-mediated endocytosis of virus by host cell [GO:0019065]; virion attachment to host cell [GO:0019062] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | metal ion binding [GO:0046872] | PF00798; | 6.10.140.1590;2.20.28.180; | Arenaviridae GPC protein family | PTM: [Pre-glycoprotein polyprotein GP complex]: Specific enzymatic cleavages in vivo yield mature proteins. GP-C polyprotein is cleaved in the endoplasmic reticulum by the host protease MBTPS1. Only cleaved glycoprotein is incorporated into virions. The SSP remains stably associated with the GP complex following cleava... | SUBCELLULAR LOCATION: [Stable signal peptide]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Go... | null | null | null | null | null | FUNCTION: [Stable signal peptide]: Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glyc... | Pichinde mammarenavirus (PICV) (Pichind mammarenavirus) |
P03562 | TRAP_TGMVY | MRNSSSSTPPSIKAQHRAAKRRAIRRRRIDLNCGCSIYIHIDCRNNGFTHRGTYHCASSREWRLYLGDNKSPLFQDNQRRGSPLHQHQDIPLTNQVQPQPEESIGSPQGISQLPSMDDIDDSFWENLFK | null | null | virus-mediated perturbation of host defense response [GO:0019049] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; viral capsid [GO:0019028] | DNA binding [GO:0003677]; metal ion binding [GO:0046872]; structural molecule activity [GO:0005198] | PF01440; | null | Geminiviridae transcriptional activator protein family | PTM: Phosphorylated. {ECO:0000305|PubMed:10544077, ECO:0000305|PubMed:14615595}. | SUBCELLULAR LOCATION: Host nucleus. Host cytoplasm. Note=The phosphorylated form appears to accumulate almost exclusively in the nucleus, whereas the non-phosphorylated form is found in both nucleus and cytoplasm. | null | null | null | null | null | FUNCTION: Strong activator of the late viral genes promoters. Enhances the expression of the capsid protein and nuclear shuttle protein. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral... | Tomato golden mosaic virus (strain Yellow vein) (TGMV) |
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