K4HTT3 · K4HTT3_9CALI
- ProteinGenome polyprotein
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1686 (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 | 1025 | For 3CLpro activity | |||
Active site | 1049 | For 3CLpro activity | |||
Active site | 1134 | 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 accessionK4HTT3
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 | 1-18 | Polar residues | |||
Region | 1-65 | Disordered | |||
Compositional bias | 36-63 | Pro residues | |||
Domain | 452-619 | SF3 helicase | |||
Region | 830-882 | Disordered | |||
Compositional bias | 834-866 | Basic and acidic residues | |||
Domain | 996-1176 | Peptidase C37 | |||
Domain | 1412-1533 | RdRp catalytic | |||
Family and domain databases
Sequence
- Sequence statusFragment
- Length1,686
- Mass (Da)187,915
- Last updated2013-01-09 v1
- MD5 Checksum8FAB4A8766CBFB056EE9433FA683095A
Features
Showing features for non-terminal residue, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Non-terminal residue | 1 | ||||
Compositional bias | 1-18 | Polar residues | |||
Compositional bias | 36-63 | Pro residues | |||
Compositional bias | 834-866 | Basic and acidic residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JX445154 EMBL· GenBank· DDBJ | AFU55691.1 EMBL· GenBank· DDBJ | Genomic RNA |