Q9YLS4 · POLG_AEVCA
- ProteinGenome polyprotein
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids2134 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes (By similarity).
Capsid protein VP0
VP0 precursor is a component of immature procapsids. The N-terminal domain of VP0, protein VP4, is needed for the assembly of 12 pentamers into the icosahedral structure. Unlike other picornaviruses, AEV VP4 may not be myristoylated (By similarity).
Protein 2B and 2BC precursor affect membrane integrity and cause an increase in membrane permeability.
Protein 2C
Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).
Protein 3A, via its hydrophobic domain, serves as membrane anchor.
Protein 3B is covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. It acts as a genome-linked replication primer (By similarity).
Protease 3C
Cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease (By similarity).
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals.
Catalytic activity
- a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Features
Showing features for site, active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 19-20 | Cleavage | ||||
Sequence: LN | ||||||
Site | 242-243 | Cleavage; by protease 3C | ||||
Sequence: QM | ||||||
Site | 487-488 | Cleavage; by protease 3C | ||||
Sequence: QG | ||||||
Site | 757-758 | Cleavage; by host | ||||
Sequence: ES | ||||||
Active site | 791 | |||||
Sequence: H | ||||||
Active site | 802 | |||||
Sequence: H | ||||||
Site | 806-807 | Cleavage; by protease 3C | ||||
Sequence: EG | ||||||
Active site | 863 | Acyl-thioester intermediate | ||||
Sequence: C | ||||||
Site | 1021-1022 | Cleavage; by protease 3C | ||||
Sequence: QG | ||||||
Binding site | 1153-1160 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GNRGGGKS | ||||||
Site | 1347-1348 | Cleavage; by protease 3C | ||||
Sequence: QS | ||||||
Site | 1412-1413 | Cleavage; by protease 3C | ||||
Sequence: QS | ||||||
Site | 1433-1434 | Cleavage; by protease 3C | ||||
Sequence: QS | ||||||
Active site | 1477 | For protease 3C activity | ||||
Sequence: H | ||||||
Active site | 1515 | For protease 3C activity | ||||
Sequence: D | ||||||
Active site | 1603 | For protease 3C activity | ||||
Sequence: C | ||||||
Site | 1648-1649 | Cleavage; by protease 3C | ||||
Sequence: QC |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell cytoplasmic vesicle membrane | |
Cellular Component | membrane | |
Cellular Component | viral capsid | |
Molecular Function | ATP binding | |
Molecular Function | channel activity | |
Molecular Function | cysteine-type endopeptidase activity | |
Molecular Function | ribonucleoside triphosphate phosphatase activity | |
Molecular Function | RNA binding | |
Molecular Function | RNA helicase activity | |
Molecular Function | RNA-dependent RNA polymerase activity | |
Molecular Function | structural molecule activity | |
Biological Process | DNA-templated transcription | |
Biological Process | monoatomic ion transmembrane transport | |
Biological Process | proteolysis | |
Biological Process | symbiont entry into host cell | |
Biological Process | viral RNA genome replication | |
Biological Process | virion attachment to host cell |
Keywords
- Molecular function
- Biological process
- Ligand
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGenome polyprotein
- Cleaved into 12 chains
Organism names
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Picornavirales > Picornaviridae > Heptrevirinae > Tremovirus > Tremovirus A
- Virus hosts
Accessions
- Primary accessionQ9YLS4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Capsid protein VP2
Capsid protein VP3
Capsid protein VP1
Protein 2B
Host cytoplasmic vesicle membrane ; Peripheral membrane protein
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
Protein 2C
Host cytoplasmic vesicle membrane ; Peripheral membrane protein
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum. May associate with membranes through a N-terminal amphipathic helix (By similarity).
Protein 3A
Host cytoplasmic vesicle membrane ; Peripheral membrane protein
Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
Protein 3B
Protease 3C
RNA-directed RNA polymerase 3D-POL
Host cytoplasmic vesicle membrane ; Peripheral membrane protein
Note: Interacts with membranes in a complex with viral protein 3AB. Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity).
Features
Showing features for topological domain, intramembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-1377 | Cytoplasmic | ||||
Sequence: MSKLFSTVGKTVDEVLSVLNDENTESYAGPDRTAVVGGGFLTTVDQSSVSTATMGSLQDVQYRTAVDIPGSRVTQGERFFLIDQREWNSTQSEWQLLGKIDIVKELLDQSYAVDGLLKYHSYARFGLDVIVQINPTSFQAGGLIAALVPYDQVDIESIAAMTTYCHGKLNCNINNVVRMKVPYIYSRGCYNLRNSAYSIWMLVIRVWSQLQLGSGTSTQITVTTLARFVDLELHGLSPLVAQMMRNEFRLSSSSNIVNLANYEDARAKVSLALGQEEFSRDSSSTGGELLHHFSQWTSIPCLAFTFTFPGTVGPGTQIWSTTVDPFSCNLRASSTVHPTNLSSIAGMFCFWRGDIVFEFQVFCTKYHSGRLMFVYVPGDENTKISTLTAKQASSGLTAVFDINGVNSTLVFRCPFISDTPYRVNPTTHKSLWPYATGKLVCYVYNRLNAPASVSPSVSINVYKSAVDLELYAPVYGVSPTNTSVFAQGKEDEGGFSSVPEVEQHVVEDKEPQGPLHVTPFGAVKAMEDPQLARKTPGTFPELAPGKPRHTVDHMDLYKFMGRAHYLWGHKFTKTDMQYTFQIPLSPIKEGFVTGTLRWFLSLFQLYRGSLDITMTFAGKTNVDGIVYFVPEGVAIETEREEQTPLLTLNYKTSVGAIRFNTGQTTNVQFRIPFYTPLEHIATHSKNAMDSVLGAITTQITNYSAQDEYLQVTYYISFNEDSQFSVPRAVPVVSSFTDTSSKTVMNTYWLDDDELVEESSHSSFDEIEEAQCSKCKMDLGDIVSCSGEKAKHFGVYVGDGVVHVDPEGNATNWFMKRKATVKKSKNLDKWCFALSPRIDRTLICETANLMVGREVEYDIFVKNCETYARGIASGDYGTKEGEKWKTLLSAVGVAAMTTTMMAMRHELLDTSLTKLPQKVGEVTNEVRKILEDTSAGVREFKEKVSSILRKTWPGKTSIKIMKWTCRIVKMCVGVGLCYAHGWDSKTVTAVVTMFSMDFLDLVIDGIEIGRMIIDELTTPKAQGLSEINQVLSIAKNAKDVIKMLIEIFCKVIERITGEHGKKIQWAQDKKEEIMNVLERAEKWITTSDDHSEGIECLKLVRSIQSVIRGEESLKELAGELRAVGTHVLNKLGRLDKPNAPILVRAEPTVLYLYGNRGGGKSLASMAIAVKLCKELGISHVEGIYTKPIMSDFWDGYAGQPVVIMDDLGQSTSDEDWTNFCQLVSSCPLRLNMANLEKKGTQFNSPFIIASSNLSHPCPKTVYCTDAIARRLHIKVKVSPKEEFSTHAMLDVAKAKKAGAYCNLDCLDFQKISDLASTPVSVQDIVLEMLHTNVDKQTLMGDIIQYWAQSNPREVFDTMAEGKNSGKYLWLFEKIKTSK | ||||||
Intramembrane | 1378-1392 | |||||
Sequence: WYILGCVGAVLSVSV | ||||||
Topological domain | 1393-2134 | Cytoplasmic | ||||
Sequence: LGVFAYHMIKNHFRDQQHDQSAYSAAIKPLRVVRLEQSDAQSVVDISNVVHGNLVRVGVGPNEARIHWLYNGLGVYDTYILMPYHGIKDADVDDDLYIERAGTIYSTNMKMVQVLFLESREGDLVLINVPRLPKFRDIRNHFSTEENIRRAEGMPGTLCTLDHERFTLVTESDLKMVEAATYVCEDDKGVRTDISVGRSWKAKACTVAGMCGGALVTSNNKMQNAIVGIHVAGGAHAISRVITKEMIEEMLKTRAQCSRIWKTEFVEEKISVGSKTKYHKSPLYDFCPQEVIKCPTKLFYQGEIDVMQVMLAKYSSPIVSEPLGYATVVEAYTNRMVSFFSEPRQLTYDECINGIEGLDAIDLKTSAGFPYNTLGLRKSDLIINGKMAQRLQQDVEKMEEDLHMNRSIQVVFTTCAKDELRPLSKVMLGKTRAIEACPVSFTILFRRYLGYALAQIQSHPGFHTGIAVGVDPDQDWHCMWYSIVTQCDLVVGLDFSNYDASLSPFMIYHAGRVLGQICGLDPRLVDRIMEPIVNSVHQLGSMRYYVHGSMPSGTPATSVLNSIINVVNICHVLCALEKISVFEVFKLFKILTYGDDVLLCIKKEYLDQKSFPLSSFVQGLEELGLSPTGADKMEVKVTPVHKMSFLKRTFYVDEWSICHPRISEETVYSMLAWKSDNASMKDLIETSIWFMFHHGPRKYVRFCTWLRGVLCRVGIGLYIPTYKELEVRYDRLVKYRFIDDSF |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000310497 | 1-19 | Capsid protein VP4 | |||
Sequence: MSKLFSTVGKTVDEVLSVL | ||||||
Chain | PRO_0000310496 | 1-242 | Capsid protein VP0 | |||
Sequence: MSKLFSTVGKTVDEVLSVLNDENTESYAGPDRTAVVGGGFLTTVDQSSVSTATMGSLQDVQYRTAVDIPGSRVTQGERFFLIDQREWNSTQSEWQLLGKIDIVKELLDQSYAVDGLLKYHSYARFGLDVIVQINPTSFQAGGLIAALVPYDQVDIESIAAMTTYCHGKLNCNINNVVRMKVPYIYSRGCYNLRNSAYSIWMLVIRVWSQLQLGSGTSTQITVTTLARFVDLELHGLSPLVAQ | ||||||
Chain | PRO_0000310495 | 1-2134 | Genome polyprotein | |||
Sequence: MSKLFSTVGKTVDEVLSVLNDENTESYAGPDRTAVVGGGFLTTVDQSSVSTATMGSLQDVQYRTAVDIPGSRVTQGERFFLIDQREWNSTQSEWQLLGKIDIVKELLDQSYAVDGLLKYHSYARFGLDVIVQINPTSFQAGGLIAALVPYDQVDIESIAAMTTYCHGKLNCNINNVVRMKVPYIYSRGCYNLRNSAYSIWMLVIRVWSQLQLGSGTSTQITVTTLARFVDLELHGLSPLVAQMMRNEFRLSSSSNIVNLANYEDARAKVSLALGQEEFSRDSSSTGGELLHHFSQWTSIPCLAFTFTFPGTVGPGTQIWSTTVDPFSCNLRASSTVHPTNLSSIAGMFCFWRGDIVFEFQVFCTKYHSGRLMFVYVPGDENTKISTLTAKQASSGLTAVFDINGVNSTLVFRCPFISDTPYRVNPTTHKSLWPYATGKLVCYVYNRLNAPASVSPSVSINVYKSAVDLELYAPVYGVSPTNTSVFAQGKEDEGGFSSVPEVEQHVVEDKEPQGPLHVTPFGAVKAMEDPQLARKTPGTFPELAPGKPRHTVDHMDLYKFMGRAHYLWGHKFTKTDMQYTFQIPLSPIKEGFVTGTLRWFLSLFQLYRGSLDITMTFAGKTNVDGIVYFVPEGVAIETEREEQTPLLTLNYKTSVGAIRFNTGQTTNVQFRIPFYTPLEHIATHSKNAMDSVLGAITTQITNYSAQDEYLQVTYYISFNEDSQFSVPRAVPVVSSFTDTSSKTVMNTYWLDDDELVEESSHSSFDEIEEAQCSKCKMDLGDIVSCSGEKAKHFGVYVGDGVVHVDPEGNATNWFMKRKATVKKSKNLDKWCFALSPRIDRTLICETANLMVGREVEYDIFVKNCETYARGIASGDYGTKEGEKWKTLLSAVGVAAMTTTMMAMRHELLDTSLTKLPQKVGEVTNEVRKILEDTSAGVREFKEKVSSILRKTWPGKTSIKIMKWTCRIVKMCVGVGLCYAHGWDSKTVTAVVTMFSMDFLDLVIDGIEIGRMIIDELTTPKAQGLSEINQVLSIAKNAKDVIKMLIEIFCKVIERITGEHGKKIQWAQDKKEEIMNVLERAEKWITTSDDHSEGIECLKLVRSIQSVIRGEESLKELAGELRAVGTHVLNKLGRLDKPNAPILVRAEPTVLYLYGNRGGGKSLASMAIAVKLCKELGISHVEGIYTKPIMSDFWDGYAGQPVVIMDDLGQSTSDEDWTNFCQLVSSCPLRLNMANLEKKGTQFNSPFIIASSNLSHPCPKTVYCTDAIARRLHIKVKVSPKEEFSTHAMLDVAKAKKAGAYCNLDCLDFQKISDLASTPVSVQDIVLEMLHTNVDKQTLMGDIIQYWAQSNPREVFDTMAEGKNSGKYLWLFEKIKTSKWYILGCVGAVLSVSVLGVFAYHMIKNHFRDQQHDQSAYSAAIKPLRVVRLEQSDAQSVVDISNVVHGNLVRVGVGPNEARIHWLYNGLGVYDTYILMPYHGIKDADVDDDLYIERAGTIYSTNMKMVQVLFLESREGDLVLINVPRLPKFRDIRNHFSTEENIRRAEGMPGTLCTLDHERFTLVTESDLKMVEAATYVCEDDKGVRTDISVGRSWKAKACTVAGMCGGALVTSNNKMQNAIVGIHVAGGAHAISRVITKEMIEEMLKTRAQCSRIWKTEFVEEKISVGSKTKYHKSPLYDFCPQEVIKCPTKLFYQGEIDVMQVMLAKYSSPIVSEPLGYATVVEAYTNRMVSFFSEPRQLTYDECINGIEGLDAIDLKTSAGFPYNTLGLRKSDLIINGKMAQRLQQDVEKMEEDLHMNRSIQVVFTTCAKDELRPLSKVMLGKTRAIEACPVSFTILFRRYLGYALAQIQSHPGFHTGIAVGVDPDQDWHCMWYSIVTQCDLVVGLDFSNYDASLSPFMIYHAGRVLGQICGLDPRLVDRIMEPIVNSVHQLGSMRYYVHGSMPSGTPATSVLNSIINVVNICHVLCALEKISVFEVFKLFKILTYGDDVLLCIKKEYLDQKSFPLSSFVQGLEELGLSPTGADKMEVKVTPVHKMSFLKRTFYVDEWSICHPRISEETVYSMLAWKSDNASMKDLIETSIWFMFHHGPRKYVRFCTWLRGVLCRVGIGLYIPTYKELEVRYDRLVKYRFIDDSF | ||||||
Chain | PRO_0000310498 | 20-242 | Capsid protein VP2 | |||
Sequence: NDENTESYAGPDRTAVVGGGFLTTVDQSSVSTATMGSLQDVQYRTAVDIPGSRVTQGERFFLIDQREWNSTQSEWQLLGKIDIVKELLDQSYAVDGLLKYHSYARFGLDVIVQINPTSFQAGGLIAALVPYDQVDIESIAAMTTYCHGKLNCNINNVVRMKVPYIYSRGCYNLRNSAYSIWMLVIRVWSQLQLGSGTSTQITVTTLARFVDLELHGLSPLVAQ | ||||||
Chain | PRO_0000310499 | 243-487 | Capsid protein VP3 | |||
Sequence: MMRNEFRLSSSSNIVNLANYEDARAKVSLALGQEEFSRDSSSTGGELLHHFSQWTSIPCLAFTFTFPGTVGPGTQIWSTTVDPFSCNLRASSTVHPTNLSSIAGMFCFWRGDIVFEFQVFCTKYHSGRLMFVYVPGDENTKISTLTAKQASSGLTAVFDINGVNSTLVFRCPFISDTPYRVNPTTHKSLWPYATGKLVCYVYNRLNAPASVSPSVSINVYKSAVDLELYAPVYGVSPTNTSVFAQ | ||||||
Chain | PRO_0000310500 | 488-757 | Capsid protein VP1 | |||
Sequence: GKEDEGGFSSVPEVEQHVVEDKEPQGPLHVTPFGAVKAMEDPQLARKTPGTFPELAPGKPRHTVDHMDLYKFMGRAHYLWGHKFTKTDMQYTFQIPLSPIKEGFVTGTLRWFLSLFQLYRGSLDITMTFAGKTNVDGIVYFVPEGVAIETEREEQTPLLTLNYKTSVGAIRFNTGQTTNVQFRIPFYTPLEHIATHSKNAMDSVLGAITTQITNYSAQDEYLQVTYYISFNEDSQFSVPRAVPVVSSFTDTSSKTVMNTYWLDDDELVEE | ||||||
Chain | PRO_0000310501 | 758-806 | Protein 2A | |||
Sequence: SSHSSFDEIEEAQCSKCKMDLGDIVSCSGEKAKHFGVYVGDGVVHVDPE | ||||||
Chain | PRO_0000310502 | 807-1021 | Protein 2B | |||
Sequence: GNATNWFMKRKATVKKSKNLDKWCFALSPRIDRTLICETANLMVGREVEYDIFVKNCETYARGIASGDYGTKEGEKWKTLLSAVGVAAMTTTMMAMRHELLDTSLTKLPQKVGEVTNEVRKILEDTSAGVREFKEKVSSILRKTWPGKTSIKIMKWTCRIVKMCVGVGLCYAHGWDSKTVTAVVTMFSMDFLDLVIDGIEIGRMIIDELTTPKAQ | ||||||
Chain | PRO_0000310503 | 1022-1347 | Protein 2C | |||
Sequence: GLSEINQVLSIAKNAKDVIKMLIEIFCKVIERITGEHGKKIQWAQDKKEEIMNVLERAEKWITTSDDHSEGIECLKLVRSIQSVIRGEESLKELAGELRAVGTHVLNKLGRLDKPNAPILVRAEPTVLYLYGNRGGGKSLASMAIAVKLCKELGISHVEGIYTKPIMSDFWDGYAGQPVVIMDDLGQSTSDEDWTNFCQLVSSCPLRLNMANLEKKGTQFNSPFIIASSNLSHPCPKTVYCTDAIARRLHIKVKVSPKEEFSTHAMLDVAKAKKAGAYCNLDCLDFQKISDLASTPVSVQDIVLEMLHTNVDKQTLMGDIIQYWAQ | ||||||
Chain | PRO_0000310504 | 1348-1412 | Protein 3A | |||
Sequence: SNPREVFDTMAEGKNSGKYLWLFEKIKTSKWYILGCVGAVLSVSVLGVFAYHMIKNHFRDQQHDQ | ||||||
Chain | PRO_0000310505 | 1413-1433 | Protein 3B | |||
Sequence: SAYSAAIKPLRVVRLEQSDAQ | ||||||
Modified residue | 1415 | O-(5'-phospho-RNA)-tyrosine | ||||
Sequence: Y | ||||||
Chain | PRO_0000310506 | 1434-1648 | Protease 3C | |||
Sequence: SVVDISNVVHGNLVRVGVGPNEARIHWLYNGLGVYDTYILMPYHGIKDADVDDDLYIERAGTIYSTNMKMVQVLFLESREGDLVLINVPRLPKFRDIRNHFSTEENIRRAEGMPGTLCTLDHERFTLVTESDLKMVEAATYVCEDDKGVRTDISVGRSWKAKACTVAGMCGGALVTSNNKMQNAIVGIHVAGGAHAISRVITKEMIEEMLKTRAQ | ||||||
Chain | PRO_0000310507 | 1649-2134 | RNA-directed RNA polymerase 3D-POL | |||
Sequence: CSRIWKTEFVEEKISVGSKTKYHKSPLYDFCPQEVIKCPTKLFYQGEIDVMQVMLAKYSSPIVSEPLGYATVVEAYTNRMVSFFSEPRQLTYDECINGIEGLDAIDLKTSAGFPYNTLGLRKSDLIINGKMAQRLQQDVEKMEEDLHMNRSIQVVFTTCAKDELRPLSKVMLGKTRAIEACPVSFTILFRRYLGYALAQIQSHPGFHTGIAVGVDPDQDWHCMWYSIVTQCDLVVGLDFSNYDASLSPFMIYHAGRVLGQICGLDPRLVDRIMEPIVNSVHQLGSMRYYVHGSMPSGTPATSVLNSIINVVNICHVLCALEKISVFEVFKLFKILTYGDDVLLCIKKEYLDQKSFPLSSFVQGLEELGLSPTGADKMEVKVTPVHKMSFLKRTFYVDEWSICHPRISEETVYSMLAWKSDNASMKDLIETSIWFMFHHGPRKYVRFCTWLRGVLCRVGIGLYIPTYKELEVRYDRLVKYRFIDDSF |
Post-translational modification
Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle (By similarity).
VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity).
Keywords
- PTM
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 781-882 | LRAT | ||||
Sequence: IVSCSGEKAKHFGVYVGDGVVHVDPEGNATNWFMKRKATVKKSKNLDKWCFALSPRIDRTLICETANLMVGREVEYDIFVKNCETYARGIASGDYGTKEGEK | ||||||
Domain | 1127-1289 | SF3 helicase | ||||
Sequence: LNKLGRLDKPNAPILVRAEPTVLYLYGNRGGGKSLASMAIAVKLCKELGISHVEGIYTKPIMSDFWDGYAGQPVVIMDDLGQSTSDEDWTNFCQLVSSCPLRLNMANLEKKGTQFNSPFIIASSNLSHPCPKTVYCTDAIARRLHIKVKVSPKEEFSTHAMLD | ||||||
Domain | 1431-1643 | Peptidase C3 | ||||
Sequence: DAQSVVDISNVVHGNLVRVGVGPNEARIHWLYNGLGVYDTYILMPYHGIKDADVDDDLYIERAGTIYSTNMKMVQVLFLESREGDLVLINVPRLPKFRDIRNHFSTEENIRRAEGMPGTLCTLDHERFTLVTESDLKMVEAATYVCEDDKGVRTDISVGRSWKAKACTVAGMCGGALVTSNNKMQNAIVGIHVAGGAHAISRVITKEMIEEML | ||||||
Domain | 1880-2001 | RdRp catalytic | ||||
Sequence: DLVVGLDFSNYDASLSPFMIYHAGRVLGQICGLDPRLVDRIMEPIVNSVHQLGSMRYYVHGSMPSGTPATSVLNSIINVVNICHVLCALEKISVFEVFKLFKILTYGDDVLLCIKKEYLDQK |
Sequence similarities
Belongs to the picornaviridae polyprotein family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,134
- Mass (Da)238,980
- Last updated1999-05-01 v1
- Checksum5BD829687E1ED30D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ225173 EMBL· GenBank· DDBJ | CAA12416.1 EMBL· GenBank· DDBJ | mRNA |