A0A5Q2V415 · A0A5Q2V415_9REOV
- ProteinNon-structural protein 2
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids312 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Participates in replication and packaging of the viral genome. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms) which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Displays ssRNA binding, NTPase, RNA triphosphatase (RTPase) and ATP-independent helix-unwinding activities. The unwinding activity may prepare and organize plus-strand RNAs for packaging and replication by removing interfering secondary structures. The RTPase activity plays a role in the removal of the gamma-phosphate from the rotavirus RNA minus strands of dsRNA genome segments. 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, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | nucleoside diphosphate kinase activity | |
Molecular Function | ribonucleoside triphosphate phosphatase activity | |
Molecular Function | RNA binding | |
Biological Process | viral genome replication |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNon-structural protein 2
- EC number
- Short namesNSP2
- Alternative names
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Duplornaviricota > Resentoviricetes > Reovirales > Sedoreoviridae > Rotavirus
Accessions
- Primary accessionA0A5Q2V415
Subcellular Location
UniProt Annotation
GO Annotation
Note: Found in spherical cytoplasmic structures, called viral factories, that appear early after infection and are the site of viral replication and packaging.
Keywords
- Cellular component
Interaction
Subunit
Homooctamer. Interacts with VP1; this interaction is weak. Interacts with NSP5; this interaction leads to up-regulation of NSP5 phosphorylation and formation of viral factories. Interacts with host DCP1A, DCP1B, DDX6, EDC4 and EIF2S1/eIF2-alpha; these interactions are probably part of the sequestration of some host SGs and PBs proteins in viral factories.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-143 | Rotavirus non-structural protein 35 N-terminal | ||||
Sequence: AELACFVSFSLIEDKVRWFPINKKAIKTMLCAKVEKSQRSNYYDTVLFGIAPPPEFRNRFKTNERHGLDYECNEFGEVANLLAEVLNMVSMPTEKFSFDIVKTVVQVRHLENLLTRIKDTDDILNENVKLKVKAVMIACNLV | ||||||
Domain | 144-311 | Rotavirus non-structural protein 35 C-terminal | ||||
Sequence: NEIETTPLTESNDIVYQDPYFTVTKLDYTNHKILPLTTDEYKITINTKTDIPERDQTAFAAYLRYNYNKYAAISHGKQHWRLVLHSQLMSHAERLDRKIRSDKKHGRQFAYDDGDVAFIHPGWKACVGQLCGGTTFEVAKTSLYSVKTSKTVRTATNKIESDLISMVG | ||||||
Region | 202-238 | RNA-binding | ||||
Sequence: FAAYLRYNYNKYAAISHGKQHWRLVLHSQLMSHAERL |
Sequence similarities
Belongs to the rotavirus NSP2 family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length312
- Mass (Da)35,809
- Last updated2020-02-26 v1
- ChecksumF6A437C74901936B