P23046 · NSP5_ROTBV
- ProteinNon-structural protein 5
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids198 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Plays an essential role in the viral genome replication. Participates, together with NSP2, in the formation of viral factories (viroplasms), which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Orchestrates the recruitment of viroplasmic proteins such as capsid proteins to these factories. Participates in the selective exclusion of host proteins from stress granules (SG) and P bodies (PB). Participates also in the sequestration of these remodeled organelles in viral factories.
Cofactor
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell cytoplasm | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | nucleotide binding | |
Molecular Function | RNA binding | |
Biological Process | viral genome replication |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameNon-structural protein 5
- Short namesNSP5
- Alternative names
Organism names
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Duplornaviricota > Resentoviricetes > Reovirales > Sedoreoviridae > Rotavirus > Rotavirus A
- Virus hosts
Accessions
- Primary accessionP23046
Subcellular Location
UniProt Annotation
GO Annotation
Note: Found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000149632 | 1-198 | Non-structural protein 5 | |||
Sequence: MSLSIDVTSLPSFSSSIYKNESSATASTLSGKSIGRSVQYVSPDAEAFSKYMLSKSPEDIGPSDSASNDPLTSFSIRSNAVKTNADAGVSMDSSVQSRPSINVGCDQVDFSFNKGIKVNANLDSSISVSTNSRKEKSKGDRKSRKHYPKIEAESDSDEYVLDDSDSDDGKCRNCKYKRKYFALRMRMKQVAMQLIEDL | ||||||
Modified residue | 67 | Phosphoserine; by host CK1 | ||||
Sequence: S | ||||||
Modified residue | 154 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Modified residue | 156 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Modified residue | 164 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Modified residue | 166 | Phosphoserine; by host | ||||
Sequence: S |
Post-translational modification
O-glycosylated.
Hyperphosphorylated on serine residues, when in dimeric form. Phosphorylation by host CK1 is required for the hyperphosphorylation of NSP5 dimer.
Keywords
- PTM
Interaction
Subunit
Homodimer. Interacts with VP1. Interacts with VP2. Interacts with NSP2; this interaction leads to up-regulation of NSP5 hyperphosphorylation and formation of virus factories. Interacts with NSP6. Participates in the selective exclusion of host proteins from stress granules (SG) and P bodies (PB). Participates also in the sequestration of these remodeled organelles in viral factories.
Sequence
- Sequence statusComplete
- Length198
- Mass (Da)21,679
- Last updated1991-11-01 v1
- Checksum28B8F0095A7C4595