A0A7S7PNC7 · A0A7S7PNC7_PVMA
- ProteinGenome polyprotein
- GenePVAgp1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids3059 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Has helicase activity. It may be involved in replication.
Involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.
Mediates the cap-independent, EIF4E-dependent translation of viral genomic RNAs. Binds to the cap-binding site of host EIF4E and thus interferes with the host EIF4E-dependent mRNA export and translation. VPg-RNA directly binds EIF4E and is a template for transcription. Also forms trimeric complexes with EIF4E-EIF4G, which are templates for translation.
Catalytic activity
- Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.
Features
Showing features for active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 641 | For helper component proteinase activity | |||
Active site | 714 | For helper component proteinase activity | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | helical viral capsid | |
Cellular Component | host cell cytoplasmic vesicle | |
Cellular Component | host cell nucleus | |
Cellular Component | vesicle | |
Molecular Function | ATP binding | |
Molecular Function | cysteine-type endopeptidase activity | |
Molecular Function | helicase activity | |
Molecular Function | hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides | |
Molecular Function | RNA binding | |
Molecular Function | RNA-dependent RNA polymerase activity | |
Molecular Function | serine-type peptidase activity | |
Molecular Function | structural molecule activity | |
Biological Process | DNA-templated transcription | |
Biological Process | proteolysis | |
Biological Process | RNA-protein covalent cross-linking | |
Biological Process | viral RNA genome replication |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameGenome polyprotein
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Pisuviricota > Stelpaviricetes > Patatavirales > Potyviridae > Potyvirus
- Virus hosts
Accessions
- Primary accessionA0A7S7PNC7
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 154-298 | Peptidase S30 | |||
Domain | 633-755 | Peptidase C6 | |||
Domain | 1226-1378 | Helicase ATP-binding | |||
Domain | 1397-1556 | Helicase C-terminal | |||
Domain | 2032-2250 | Peptidase C4 | |||
Domain | 2516-2640 | RdRp catalytic | |||
Region | 2797-2816 | Disordered | |||
Compositional bias | 2801-2816 | Basic and acidic residues | |||
Sequence similarities
Belongs to the potyviridae genome polyprotein family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length3,059
- Mass (Da)346,058
- Last updated2021-06-02 v1
- Checksum32CC4295E742C51C
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 2801-2816 | Basic and acidic residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MT521082 EMBL· GenBank· DDBJ | QOZ05775.1 EMBL· GenBank· DDBJ | Genomic RNA |