A0A1L3THP5 · A0A1L3THP5_9POTV
- ProteinGenome polyprotein
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids3202 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
An RNA-dependent RNA polymerase that plays an essential role in the virus replication.
Has RNA-binding and proteolytic activities.
Has helicase activity. It may be involved in replication.
Indispensable for virus 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 (By similarity).
Binds to the cap-binding site of host EIF4E and thus interferes with the host EIF4E-dependent mRNA export and translation (By similarity).
VPg-RNA directly binds EIF4E and is a template for transcription (By similarity).
Also forms trimeric complexes with EIF4E-EIF4G, which are templates for translation
Binds to the cap-binding site of host EIF4E and thus interferes with the host EIF4E-dependent mRNA export and translation (By similarity).
VPg-RNA directly binds EIF4E and is a template for transcription (By similarity).
Also forms trimeric complexes with EIF4E-EIF4G, which are templates for translation
Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. 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 RNAs. May have RNA-binding activity.
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 | 787 | For helper component proteinase activity | ||||
Sequence: C | ||||||
Active site | 860 | For helper component proteinase activity | ||||
Sequence: H |
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 | viral RNA genome replication |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameGenome polyprotein
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Pisuviricota > Stelpaviricetes > Patatavirales > Potyviridae > Potyvirus
Accessions
- Primary accessionA0A1L3THP5
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for coiled coil, domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 193-261 | |||||
Sequence: YDLAIKKMDEAMQQNSVLQKQLFIRQQSTIQQKPKGAVQLRHMSFEQAKKRVELARKRQEEEKDFLSGK | ||||||
Domain | 303-444 | Peptidase S30 | ||||
Sequence: APQCRELTYVLEEVLSLASRSGKLVEFITGGKGKSVKVCYMQKHGAILPKFSLPHEEGKYIHQELQYESIYEFLPYICMFAKYKSISANDITYGDSGLLFDERSSITTNHTKLPYFVVRGRENGKLINALEMVASMRDIQHY | ||||||
Domain | 779-901 | Peptidase C6 | ||||
Sequence: MYIAKEGFCYLNIFLAMLVNVNEDEAKDFTKMVRDVIVPRLGKWPTMLDVATAAYMLTVFHPETRNAELPRILVDHACQTMHVIDSFGSLTVGYHVLKAGTVNQLIQFASNDLQSEMKFYRVG | ||||||
Domain | 1372-1524 | Helicase ATP-binding | ||||
Sequence: LVATSSHTEFLIRGAVGSGKSTGLPHHLSKKGKVLLLEPTRPLAENVSKQLSFEPFYHNVTLRMRGLSKFGSSNIVVMTSGFAFHYYVNNPQQLSDFDFIIIDECHVQDSPTIAFNCALKEFEFSGKLIKVSATPPGRECEFTTQHPVKLKVE | ||||||
Domain | 1543-1702 | Helicase C-terminal | ||||
Sequence: DMIQHGNNLLVYVASYNEVDQLSRLLTEKHYKVTKVDGRTMQMGNVEIATTGTEGKPHFIVATNIIENGVTLDIDCVIDFGLKVVATLDTDNRCVRYNKQSVSYGERIQRLGRVGRCKPGFALRIGHTGKGVEEVPEFIATEAAFLSFAYGLPVTTQSVS | ||||||
Domain | 2178-2396 | Peptidase C4 | ||||
Sequence: SKSVYKGLRDYSGISTLICQLTNSSDGHKETMFGVGYGSFIITNGHLFRRNNGMLTVKTWHGEFVVHNTTQLKIHFIQGKDVILIRMPKDFPPFGKRNLFRQPKREERVCMVGTNFQEKSLRATVSESSMILPEGKGSFWIHWITTQDGFCGLPLVSVNDGHIVGIHGLTSNDSEKNFFVPLTDGFEKEYLENADNLSWDKHWFWEPSKIAWGSLNLVE | ||||||
Domain | 2662-2786 | RdRp catalytic | ||||
Sequence: WVYCHADGSQFDSSLTPLLLNAVLDVRSFFMEDWWVGREMLENLYAEIVYTPILTPDGTIFKKFRGNNSGQPSTVVDNTLMVVIAMYYSCCKQGWSEEDIQERLVFFANGDDIILAVSDKDTWLY | ||||||
Compositional bias | 2935-2954 | Basic and acidic residues | ||||
Sequence: SLQSGKEKEGDMDAGKDPKK | ||||||
Region | 2935-2972 | Disordered | ||||
Sequence: SLQSGKEKEGDMDAGKDPKKSTSSSKGAGTSSKDVNVG | ||||||
Compositional bias | 2955-2971 | Polar residues | ||||
Sequence: STSSSKGAGTSSKDVNV |
Sequence similarities
Belongs to the potyviridae genome polyprotein family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length3,202
- Mass (Da)365,312
- Last updated2017-03-15 v1
- ChecksumDF6BA0F0489583DD
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 2935-2954 | Basic and acidic residues | ||||
Sequence: SLQSGKEKEGDMDAGKDPKK | ||||||
Compositional bias | 2955-2971 | Polar residues | ||||
Sequence: STSSSKGAGTSSKDVNV |