R9TFZ8 · R9TFZ8_EMCV
- ProteinGenome polyprotein
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids2292 (go to sequence)
- Protein existencePredicted
- Annotation score5/5
Function
function
Affects membrane integrity and causes an increase in membrane permeability.
Forms a primer, VPg-pU, which is utilized by the polymerase for the initiation of RNA chains.
Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes.
Serves as membrane anchor via its hydrophobic domain.
VP0 precursor is a component of immature procapsids.
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
Features
Showing features for site, binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 393-394 | Cleavage; by protease 3C | ||||
Sequence: QS | ||||||
Site | 624-625 | Cleavage; by protease 3C | ||||
Sequence: QG | ||||||
Site | 901-902 | Cleavage; by protease 3C | ||||
Sequence: ES | ||||||
Site | 1044-1045 | Cleavage; by ribosomal skip | ||||
Sequence: GP | ||||||
Site | 1194-1195 | Cleavage; by protease 3C | ||||
Sequence: QS | ||||||
Binding site | 1313-1320 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GDAGQGKS | ||||||
Site | 1607-1608 | Cleavage; by protease 3C | ||||
Sequence: QG | ||||||
Site | 1627-1628 | Cleavage; by protease 3C | ||||
Sequence: QG | ||||||
Active site | 1673 | For protease 3C activity | ||||
Sequence: H | ||||||
Active site | 1707 | For protease 3C activity | ||||
Sequence: D | ||||||
Active site | 1786 | For protease 3C activity | ||||
Sequence: C | ||||||
Site | 1832-1833 | Cleavage; by protease 3C | ||||
Sequence: QG | ||||||
Active site | 2067 | For RdRp activity | ||||
Sequence: D | ||||||
Active site | 2165 | For RdRp activity | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasmic vesicle membrane | |
Cellular Component | host cell cytoplasmic vesicle membrane | |
Cellular Component | host cell nucleolus | |
Cellular Component | T=pseudo3 icosahedral viral capsid | |
Molecular Function | ATP binding | |
Molecular Function | channel activity | |
Molecular Function | cysteine-type endopeptidase 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 | symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity | |
Biological Process | viral RNA genome replication | |
Biological Process | virion attachment to host cell |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameGenome polyprotein
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Picornavirales > Picornaviridae > Caphthovirinae > Cardiovirus > Cardiovirus A
- Virus hosts
Accessions
- Primary accessionR9TFZ8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cytoplasmic vesicle membrane ; Peripheral membrane protein
Host cytoplasmic vesicle membrane ; Peripheral membrane protein
Membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for lipidation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Lipidation | 68 | N-myristoyl glycine; by host | ||||
Sequence: G | ||||||
Disulfide bond | 479↔481 | |||||
Sequence: CSC |
Keywords
- PTM
Family & Domains
Features
Showing features for zinc finger, motif, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 10-22 | |||||
Sequence: CAHPLTFEECPKC | ||||||
Motif | 995-1003 | Nuclear localization signal | ||||
Sequence: KRVRPFRLP | ||||||
Domain | 1281-1447 | SF3 helicase | ||||
Sequence: EKRTGIAAVCEKFRQKHDHATARCEPVVIVLRGDAGQGKSLSSQVIAQAVSKTIFGRQSVYSLPPDSDFFDGYENQFAAIMDDLGQNPDGSDFTTFCQMVSTTNFLPNMASLERKGTPFTSQLVVATTNLPEFRPVTIAHYPAVERRITFDYSVSAGPVCSKTEAGY | ||||||
Coiled coil | 1531-1558 | |||||
Sequence: VQQLKTRQEATDEQLEELQEAFAKVQER | ||||||
Domain | 1630-1822 | Peptidase C3 | ||||
Sequence: NPVMDFEKYVAKHVTAPIDFVYPTGVSTQTCLLVRGRTLAVNRHMAESDWTSIVVRGVTHARSTVKILAIAKAGKETDVSFIRLSSGPLFRDNTSKFVKAGDVLPTGAAPVTGIMNTDIPMMYTGTFLKAGVSVPVETGQTFNHCIHYKANTRKGWCGSALLADLGGSKKILGIHSAGSMGIAAASIVSQEMI | ||||||
Domain | 2061-2179 | RdRp catalytic | ||||
Sequence: ERVYDVDYSNFDSTHSVAMFRLLAEEFFTPENGFDPLTREYLESLAISTHAFEEKRFLITGGLPSGCAATSMLNTIMNNIIIRAGLYLTYKNFEFDDVKVLSYGDDLLVATNYQLDFDK |
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,292
- Mass (Da)255,569
- Last updated2013-09-18 v1
- Checksum27D8E1B756F5B3AD