A0A0E3VNW4 · A0A0E3VNW4_9CALI
- ProteinGenome polyprotein
- GenePOL
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1696 (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 | 1035 | For 3CLpro activity | ||||
Sequence: H | ||||||
Active site | 1059 | For 3CLpro activity | ||||
Sequence: E | ||||||
Active site | 1144 | 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
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Picornavirales > Caliciviridae > Norovirus > Norwalk virus
Accessions
- Primary accessionA0A0E3VNW4
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 | 1-29 | Polar residues | ||||
Sequence: DASAAVAGKNNNNDKEKSSSDSLFSNMTV | ||||||
Region | 1-77 | Disordered | ||||
Sequence: DASAAVAGKNNNNDKEKSSSDSLFSNMTVTFKKALGARPKQPPPGETKQIQKPPRPPTPELVKRIPPPPPNGEDEPK | ||||||
Compositional bias | 46-74 | Pro residues | ||||
Sequence: ETKQIQKPPRPPTPELVKRIPPPPPNGED | ||||||
Region | 97-118 | Disordered | ||||
Sequence: QPDAQNTAYSVPPLSQREVGEA | ||||||
Domain | 462-629 | SF3 helicase | ||||
Sequence: LARIAAARSLVHKAKEELSSRQRPVVVMISGRPGIGKTHLARELAKKVASTLSGDQRIGLIPRNGVDHWDAYKGERVVLWDDYGMSNPIQDALRLQELADTCPLTLNCDRIENKGKVFDSDAIIITTNLANPAPLDYVNFEACSRRIDFLVYADAPDIEKAKRDFPGQ | ||||||
Region | 837-891 | Disordered | ||||
Sequence: SKPPIEEGDEPEDKGGCPKPRDEDDLTIDSRDIKVEGKKGKNKSGRGKKHTAFSS | ||||||
Compositional bias | 841-876 | Basic and acidic residues | ||||
Sequence: IEEGDEPEDKGGCPKPRDEDDLTIDSRDIKVEGKKG | ||||||
Domain | 1006-1186 | Peptidase C37 | ||||
Sequence: APPSVWSRIVNFGTGWGFWVSPSLFITSTHVIPKGITEAFGVPINQIQIHKSGEFCRLRFPKPIRPDVSGMILEEGAPEGTVVSILIKRTTGELMPLAVRMGTHATMKIQGRTVGGQMGMLLTGSNAKSMDLGTTPGDCGCPYIYKRGNDFVAIGVHTAAARGGNTVICATQGSEGEATLE | ||||||
Domain | 1422-1543 | RdRp catalytic | ||||
Sequence: RYHYDADYSRWDSTQQRAVLEAALEIMVRFSAEPQLAQIVAEDLLSPSVVDVGDFKIAINEGLPSGVPCTSQWNSIAHWLLTLCALSEVTGLGPDIIQANSMYSFYGDDEIVSTDIKLDPEK |
Family and domain databases
Sequence
- Sequence statusFragment
- Length1,696
- Mass (Da)189,018
- Last updated2015-06-24 v1
- Checksum5F961B371493DFC6
Features
Showing features for non-terminal residue, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: D | ||||||
Compositional bias | 1-29 | Polar residues | ||||
Sequence: DASAAVAGKNNNNDKEKSSSDSLFSNMTV | ||||||
Compositional bias | 46-74 | Pro residues | ||||
Sequence: ETKQIQKPPRPPTPELVKRIPPPPPNGED | ||||||
Compositional bias | 841-876 | Basic and acidic residues | ||||
Sequence: IEEGDEPEDKGGCPKPRDEDDLTIDSRDIKVEGKKG |