B3SRX0 (NSP2_ROTHT) Reviewed, UniProtKB/Swiss-Prot
Last modified April 16, 2014. Version 23. History...
Names and origin
|Protein names||Recommended name:|
Non-structural protein 2
Non-structural RNA-binding protein 35
|Organism||Rotavirus A (strain Human/United Kingdom/ST3/1975 G4-P2A-I1-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A) (Rotavirus A (strain St. Thomas 3)) [Complete proteome]|
|Taxonomic identifier||10960 [NCBI]|
|Taxonomic lineage||Viruses › dsRNA viruses › Reoviridae › Sedoreovirinae › Rotavirus › Rotavirus A ›|
|Virus host||Homo sapiens (Human) [TaxID: 9606]|
|Sequence length||317 AA.|
|Protein existence||Inferred from homology|
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) and ATP-independent helix-unwinding activity 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 By similarity.
Magnesium for NTPase activity By similarity.
Homooctamer By similarity. 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.
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 By similarity.
Belongs to the rotavirus NSP2 family.
|Cellular component||Host cytoplasm|
|Technical term||Complete proteome|
|Gene Ontology (GO)|
|Biological_process||viral 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_0000369538|
|Region||205 – 241||37||RNA-binding Potential|
|Active site||225||1||For NTPase activity By similarity|
|Metal binding||153||1||Magnesium Potential|
|Metal binding||171||1||Magnesium Potential|
|||"Group A human rotavirus genomics: evidence that gene constellations are influenced by viral protein interactions."|
Heiman E.M., McDonald S.M., Barro M., Taraporewala Z.F., Bar-Magen T., Patton J.T.
J. Virol. 82:11106-11116(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
|EF672615 Genomic RNA. Translation: ABV53295.1.|
3D structure databases
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: B3SRX0|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|
Index of protein domains and families