K4HTU8 · K4HTU8_9CALI
- ProteinGenome polyprotein
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1688 (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 | 1027 | For 3CLpro activity | |||
Active site | 1051 | For 3CLpro activity | |||
Active site | 1136 | 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 accessionK4HTU8
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 | 1-20 | Polar residues | |||
Region | 1-67 | Disordered | |||
Compositional bias | 35-65 | Pro residues | |||
Domain | 454-621 | SF3 helicase | |||
Region | 862-884 | Disordered | |||
Domain | 998-1178 | Peptidase C37 | |||
Domain | 1414-1535 | RdRp catalytic | |||
Family and domain databases
Sequence
- Sequence statusFragment
- Length1,688
- Mass (Da)188,077
- Last updated2013-01-09 v1
- MD5 ChecksumD0DC6195F008DE040D8788749FDA6752
Features
Showing features for non-terminal residue, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Non-terminal residue | 1 | ||||
Compositional bias | 1-20 | Polar residues | |||
Compositional bias | 35-65 | Pro residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JX445159 EMBL· GenBank· DDBJ | AFU55706.1 EMBL· GenBank· DDBJ | Genomic RNA |