A0A5J6ACE5 · A0A5J6ACE5_RUBV
- ProteinNon-structural polyprotein p200
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids2116 (go to sequence)
- Protein existencePredicted
- Annotation score5/5
Function
function
Probable principal replicase for the negative-strand DNA, which replicates the 40S + genomic RNA into - antigenomic RNA. It cannot replicate the - into + until cleaved into p150 and p90 mature proteins.
Protease that cleaves the precursor polyprotein into two mature products. Together with RNA-directed RNA polymerase p90, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive-strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. Responsible for the mRNA-capping of the viral mRNAs. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. Forms fibers late in the infection that may be involved in cell-to-cell spread of the virus RNA in the absence of virus particle formation.
Together with protease/methyltransferase p150, replicates the 40S genomic and antigenomic RNA by recognizing replications specific signals. The heterodimer P150/p90 is probably the principal replicase for positive-strand genomic RNA and the 24S subgenomic RNA, which codes for structural proteins. A helicase activity is probably also present.
Catalytic activity
- ATP + H2O = ADP + phosphate + H+
Cofactor
Protein has several cofactor binding sites:
Note: Zn2+ is necessary for the protease activity. The protease can also function efficiently with Cd2+ and Co2+.
Features
Showing features for active site, binding site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 1152 | For cysteine protease activity | |||
Binding site | 1175 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 1178 | Zn2+ (UniProtKB | ChEBI) | |||
Binding site | 1227 | Zn2+ (UniProtKB | ChEBI) | |||
Active site | 1273 | For cysteine protease activity | |||
Binding site | 1273 | Zn2+ (UniProtKB | ChEBI) | |||
Site | 1301-1302 | Cleavage; autocatalytic | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | host cell cytoplasm | |
Cellular Component | host cell membrane | |
Cellular Component | membrane | |
Molecular Function | ATP binding | |
Molecular Function | cysteine-type endopeptidase activity | |
Molecular Function | metal ion binding | |
Molecular Function | mRNA methyltransferase activity | |
Molecular Function | ribonucleoside triphosphate phosphatase activity | |
Molecular Function | RNA binding | |
Molecular Function | RNA helicase activity | |
Molecular Function | RNA-dependent RNA polymerase activity | |
Biological Process | DNA-templated transcription | |
Biological Process | mRNA modification | |
Biological Process | proteolysis | |
Biological Process | RNA processing | |
Biological Process | viral RNA genome replication |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameNon-structural polyprotein p200
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Kitrinoviricota > Alsuviricetes > Hepelivirales > Matonaviridae > Rubivirus > Rubivirus rubellae
Accessions
- Primary accessionA0A5J6ACE5
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Post-translational modification
Non-structural polyprotein p200: Specific enzymatic cleavage by its own cysteine protease yield mature proteins p150 and p90.
Interaction
Subunit
Interacts with RNA-directed RNA polymerase p90. Interacts with host CALM1; this interaction is necessary for the protease activity and viral infectivity. Interacts with host C1QBP. Interacts with the capsid protein.
Interacts with human RB1/retinoblastoma protein. Interacts with protease/methyltransferase p150.
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 57-247 | Alphavirus-like MT | |||
Region | 458-478 | Disordered | |||
Region | 712-807 | Disordered | |||
Compositional bias | 747-772 | Pro residues | |||
Domain | 806-985 | Macro | |||
Region | 993-1029 | Disordered | |||
Domain | 1000-1301 | Peptidase C27 | |||
Region | 1152-1183 | Interaction with host CALM1 | |||
Region | 1193-1228 | EF-hand-like | |||
Domain | 1320-1609 | +RNA virus helicase C-terminal | |||
Domain | 1870-1981 | RdRp catalytic | |||
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length2,116
- Mass (Da)230,539
- Last updated2019-12-11 v1
- Checksum8B0BCB718E383AFD
Features
Showing features for compositional bias, sequence uncertainty.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 747-772 | Pro residues | |||
Sequence uncertainty | 1347 | I or L | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MK780810 EMBL· GenBank· DDBJ | QBZ68619.1 EMBL· GenBank· DDBJ | Genomic RNA |