B3SRV4 · NSP2_ROTHP

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

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for binding site, active site.

131720406080100120140160180200220240260280300
TypeIDPosition(s)Description
Binding site107-109ATP (UniProtKB | ChEBI)
Binding site188ATP (UniProtKB | ChEBI)
Binding site221-223ATP (UniProtKB | ChEBI)
Active site225For NTPase and RTPase activities
Binding site227ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componenthost cell cytoplasm
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionnucleoside diphosphate kinase activity
Molecular Functionribonucleoside triphosphate phosphatase activity
Molecular FunctionRNA binding
Biological Processviral genome replication

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Non-structural protein 2
  • EC number
  • Short names
    NSP2
  • Alternative names
    • NCVP3
    • Non-structural RNA-binding protein 35
      (NS35
      )

Organism names

Accessions

  • Primary accession
    B3SRV4

Proteomes

Subcellular Location

Host cytoplasm
Note: Found in spherical cytoplasmic structures, called viral factories, that appear early after infection and are the site of viral replication and packaging.

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003695401-317Non-structural protein 2

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

3D structure databases

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region205-241RNA-binding

Sequence similarities

Belongs to the rotavirus NSP2 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    317
  • Mass (Da)
    36,510
  • Last updated
    2008-09-02 v1
  • Checksum
    99F775280F3D5A39
MAELACFCYPHLENDSYKFIPFNSLAIKCMLTAKVDKKDQDKFYNSIVYGIAPPPQFKKRYNTNDNSRGMNYETPMFNKVAILICEALNSIKVTQSDVANVLSRVVSVRHLENLVLRKENHQDVLFHSKELLLKAVLIAIGQSKEIETTATAEGGEIVFQNAAFTMWKLTYLDHKLMPILDQNFIEYKITLNEDKPISDICVKELVAELRWQYNRFAVITHGKGHYRVVKYSSVANHADRVFATYKNNAKSGNVTDFNLLDQRIIWQNWYAFTSSMKQGNTLDVCKKLLFQKMKQEKNPFKGLSTDRKMDEVSHVGI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
EF672601
EMBL· GenBank· DDBJ
ABV53279.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp