K4HS47 · K4HS47_9CALI
- ProteinGenome polyprotein
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1693 (go to sequence)
- Protein existencePredicted
- Annotation score3/5
Function
function
3C-like protease processes the polyprotein: 3CLpro-RdRp is first released by autocleavage, then all other proteins are cleaved. May cleave polyadenylate-binding protein thereby inhibiting cellular translation.
Catalytic activity
- a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + phosphate + H+
Features
Showing features for active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 1032 | For 3CLpro activity | |||
Active site | 1056 | For 3CLpro activity | |||
Active site | 1141 | For 3CLpro activity | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | cysteine-type endopeptidase activity | |
Molecular Function | RNA binding | |
Molecular Function | RNA helicase activity | |
Molecular Function | RNA-dependent RNA polymerase 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
Organism names
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Picornavirales > Caliciviridae > Norovirus > Norwalk virus
Accessions
- Primary accessionK4HS47
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Post-translational modification
Specific enzymatic cleavages in vivo yield mature proteins. 3CLpro is first autocatalytically cleaved, then processes the whole polyprotein.
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 1-25 | Polar residues | |||
Region | 1-71 | Disordered | |||
Compositional bias | 43-70 | Pro residues | |||
Domain | 459-626 | SF3 helicase | |||
Region | 867-889 | Disordered | |||
Domain | 1003-1183 | Peptidase C37 | |||
Domain | 1419-1540 | RdRp catalytic | |||
Family and domain databases
Sequence
- Sequence statusFragment
- Length1,693
- Mass (Da)188,420
- Last updated2013-01-09 v1
- MD5 Checksum161A5E0213641C1CEFA975E2BB490CEA
Features
Showing features for non-terminal residue, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Non-terminal residue | 1 | ||||
Compositional bias | 1-25 | Polar residues | |||
Compositional bias | 43-70 | Pro residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JX445152 EMBL· GenBank· DDBJ | AFU55685.1 EMBL· GenBank· DDBJ | Genomic RNA |