P17595 · ALPHA_BSMV
- ProteinReplication protein alpha-A
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1139 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Probably contains methyltransferase and helicase activities (PubMed:2209552).
Methyltransferase displays a cytoplasmic capping enzyme activity (Probable). This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus (Probable). Helicase region probably exhibits NTPase and RNA unwinding activities (Probable)
Methyltransferase displays a cytoplasmic capping enzyme activity (Probable). This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus (Probable). Helicase region probably exhibits NTPase and RNA unwinding activities (Probable)
Miscellaneous
The genome of this virus consists of three linear, positive, single-stranded RNAs encapsidated in separate virions designated RNA-alpha, RNA-beta and RNA-gamma. Three proteins (alpha-A, beta-A and gamma-A) are translated directly from these genomic RNAs and the remaining proteins encoded on RNA-beta (beta-B, beta-C and beta-D) and RNA-gamma (gamma-B) are expressed via three subgenomic messenger RNAs.
Catalytic activity
- ATP + H2O = ADP + phosphate + H+
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 838-845 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | mRNA methyltransferase activity | |
Molecular Function | RNA binding | |
Molecular Function | RNA helicase activity | |
Biological Process | methylation | |
Biological Process | mRNA modification | |
Biological Process | RNA processing |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameReplication protein alpha-A
Including 2 domains:
- Recommended nameMethyltransferase
- EC number
- Recommended nameNTPase/helicase
- EC number
Organism names
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Kitrinoviricota > Alsuviricetes > Martellivirales > Virgaviridae > Hordeivirus
- Virus hosts
Accessions
- Primary accessionP17595
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: The viral replication sites are located at the host chloroplast membrane.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000222492 | 1-1139 | Replication protein alpha-A | ||
Interaction
Subunit
Interacts with the suppressor of RNA silencing Gamma-B (via C-terminus).
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 60-438 | Methyltransferase | |||
Domain | 81-305 | Alphavirus-like MT | |||
Region | 611-637 | Disordered | |||
Compositional bias | 614-637 | Polar residues | |||
Domain | 805-969 | +RNA virus helicase ATP-binding | |||
Region | 835-1109 | Helicase | |||
Domain | 970-1139 | +RNA virus helicase C-terminal | |||
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,139
- Mass (Da)129,628
- Last updated1990-08-01 v1
- Checksum24B1500FD05362D9
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 614-637 | Polar residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J04342 EMBL· GenBank· DDBJ | AAA46336.1 EMBL· GenBank· DDBJ | Genomic RNA |