Q03242 (NSP2_ROTSP) Reviewed, UniProtKB/Swiss-Prot
Last modified February 19, 2014. Version 55. History...
Names and origin
|Protein names||Recommended name:|
Non-structural protein 2
Non-structural RNA-binding protein 35
|Organism||Rotavirus A (strain SA11-Patton G3-Px[x]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-Ex-Hx) (RV-A) (Simian Agent 11 (strain Patton))|
|Taxonomic identifier||36434 [NCBI]|
|Taxonomic lineage||Viruses › dsRNA viruses › Reoviridae › Sedoreovirinae › Rotavirus › Rotavirus A ›|
|Virus host||Macaca mulatta (Rhesus macaque) [TaxID: 9544]|
|Sequence length||317 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
Involved in genome replication and packaging. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms) which are large inclusions in the cytoplasm where replication intermediates are assembled and RNA replication takes place. Displays ssRNA binding, NTPase, RNA triphosphatase (RTPase), ATP-independent helix-unwinding and nucleoside diphosphate kinase-like activities. The unwiding activity may prepare and organize plus-strand RNAs for packaging and replication by removing interfering secondary structures. Unlike typical helicases, NSP2 requires neither a divalent cation nor a nucleotide energy source for helix destabilization. The RTPase activity may account for the absence of the 5'-terminal gamma-phosphate on the minus-strands of dsRNA genome segments. Ref.5 Ref.6
Magnesium for NTPase activity By similarity.
Homooctamer. Interacts with VP1; this interaction is weak. Interacts with NSP5; this interaction leads to up-regulation of NSP5 hyperphosphorylation and formation of virus factories By similarity. Ref.3 Ref.4 Ref.5
Host cytoplasm Potential. Note: Found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging.
Belongs to the rotavirus NSP2 family.
|Cellular component||Host cytoplasm|
|Gene Ontology (GO)|
Inferred from electronic annotation. Source: GOCviral genome replication
Inferred from electronic annotation. Source: InterPro
|Cellular_component||host cell cytoplasm|
Inferred from electronic annotation. Source: UniProtKB-SubCell
Inferred from electronic annotation. Source: UniProtKB-KWhydrolase activity, acting on acid anhydrides
Inferred from electronic annotation. Source: InterPrometal ion binding
Inferred from electronic annotation. Source: UniProtKB-KWnucleotide binding
Inferred from electronic annotation. Source: UniProtKB-KW
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 317||317||Non-structural protein 2||PRO_0000149551|
|Region||205 – 241||37||RNA-binding Potential|
|Active site||225||1||For NTPase/RTPase activity By similarity|
|Metal binding||153||1||Magnesium Potential|
|Metal binding||171||1||Magnesium Potential|
|||"Nucleotide and amino acid sequence analysis of the rotavirus nonstructural RNA-binding protein NS35."|
Patton J.T., Salter-Cid L., Kalbach A.N., Mansell E.A., Kattoura M.D.
Virology 192:438-446(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|||"The rotavirus nonstructural protein, NS35, possesses RNA-binding activity in vitro and in vivo."|
Kattoura M.D., Clapp L.L., Patton J.T.
Virology 191:698-708(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING.
|||"The rotavirus RNA-binding protein NS35 (NSP2) forms 10S multimers and interacts with the viral RNA polymerase."|
Kattoura M.D., Chen X., Patton J.T.
Virology 202:803-813(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VP1.
|||"Multimers formed by the rotavirus nonstructural protein NSP2 bind to RNA and have nucleoside triphosphatase activity."|
Taraporewala Z.F., Chen D., Patton J.T.
J. Virol. 73:9934-9943(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, RNA-BINDING.
|||"Rotavirus nonstructural protein NSP2 self-assembles into octamers that undergo ligand-induced conformational changes."|
Schuck P., Taraporewala Z.F., McPhie P., Patton J.T.
J. Biol. Chem. 276:9679-9687(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, FUNCTION.
|||"Identification and characterization of the helix-destabilizing activity of rotavirus nonstructural protein NSP2."|
Taraporewala Z.F., Patton J.T.
J. Virol. 75:4519-4527(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
|L04531 Genomic RNA. Translation: AAA47298.1.|
3D structure databases
|SMR||Q03242. Positions 1-313. |
Protocols and materials databases
Family and domain databases
|Gene3D||3.30.428.20. 1 hit. |
3.90.1400.10. 1 hit.
|InterPro||IPR003668. Rotavirus_NSP2. |
|Pfam||PF02509. Rota_NS35. 1 hit. |
|SUPFAM||SSF75347. SSF75347. 1 hit. |
SSF75574. SSF75574. 1 hit.
|Accession||Primary (citable) accession number: Q03242|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|
Index of protein domains and families