A0A5B8YW25 · A0A5B8YW25_9CALI
- ProteinGenome polyprotein
- GeneORF1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1663 (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 + H+ + phosphate
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 1002 | For 3CLpro activity | ||||
Sequence: H | ||||||
Active site | 1026 | For 3CLpro activity | ||||
Sequence: E | ||||||
Active site | 1111 | For 3CLpro activity | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell membrane | |
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 | viral RNA genome replication |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameGenome polyprotein
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Picornavirales > Caliciviridae > Norovirus > Norwalk virus
Accessions
- Primary accessionA0A5B8YW25
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 region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-42 | Disordered | ||||
Sequence: RALGARPKQPPPKEIPPRPPRPPTPELVKKIPPPPPNGEDEL | ||||||
Compositional bias | 9-39 | Pro residues | ||||
Sequence: QPPPKEIPPRPPRPPTPELVKKIPPPPPNGE | ||||||
Compositional bias | 62-76 | Polar residues | ||||
Sequence: RQPEETNTAFSVPPL | ||||||
Region | 62-84 | Disordered | ||||
Sequence: RQPEETNTAFSVPPLNQRESRDA | ||||||
Domain | 428-595 | SF3 helicase | ||||
Sequence: LARIAAARSLVHRAKEELSSRPRAVVVMISGRPGIGKTHLARELAKKIAASLTGDQRVGLIPRNGVDHWDAYKGERVVLWDDYGMSNPIHDALRLQELADTCPLTLNCDRIENKGKVFDSDAIIITTNLANPAPLDYVNFEACSRRIDFLVYAEAPEVEKAKRDFPGQ | ||||||
Region | 834-854 | Disordered | ||||
Sequence: DIKTEGKKGKNKSHRTPHHWA | ||||||
Domain | 973-1153 | Peptidase C37 | ||||
Sequence: APPSIWSRIVNFGSGWGFWVSPSLFITSTHVIPHGAKEFFGVPIKQIQIHKLGEFCRLRFPKPIRTGVTGMILEEGAPEGTVATLLIKRPTGELMPLAARMGTHATMKIQGRTVGGQMGMLLTGSNAKSMDLGTTPGDCGCPYIYKRGNDYVVIGVHTAAARGGNTVICATQGSEGEATLE | ||||||
Domain | 1389-1510 | RdRp catalytic | ||||
Sequence: RYHYDADYSRWDSTQQRDVLAAALEIMVKFSPEPHLAQVVAEDLLSPSVMDVGDFQISISEGLPSGVPCTSQWNSIAHWLLTLCALSEVTDLSPDIIQANSLFSFYGDDEIVSTDIKLDPEK |
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,663
- Mass (Da)185,465
- Last updated2019-11-13 v1
- Checksum4006DDF9C3989FD3
Features
Showing features for non-terminal residue, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: R | ||||||
Compositional bias | 9-39 | Pro residues | ||||
Sequence: QPPPKEIPPRPPRPPTPELVKKIPPPPPNGE | ||||||
Compositional bias | 62-76 | Polar residues | ||||
Sequence: RQPEETNTAFSVPPL |