A0A5Q2UZQ9 · A0A5Q2UZQ9_9REOV

  • Protein
    Non-structural protein 2
  • Gene
    NSP2
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Organism
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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

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

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
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
      )

Gene names

    • Name
      NSP2

Organism names

  • Taxonomic identifier
  • Organism
    Rotavirus A
  • Strain
    • RVA/Pig-wt/ESP/VT29/2018/G4P[6]
  • Taxonomic lineage
    Viruses > Riboviria > Orthornavirae > Duplornaviricota > Resentoviricetes > Reovirales > Sedoreoviridae > Rotavirus

Accessions

  • Primary accession
    A0A5Q2UZQ9

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

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.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain2-143Rotavirus non-structural protein 35 N-terminal
Domain144-316Rotavirus non-structural protein 35 C-terminal
Region205-241RNA-binding

Sequence similarities

Belongs to the rotavirus NSP2 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    317
  • Mass (Da)
    36,698
  • Last updated
    2020-02-26 v1
  • Checksum
    B1F0F12140C2299B
MAELACFCYPHLENDSYKFIPFNNLAIKCMLTAKVDKKDQDKFYNSIVYGIAPPPQFKKRYNTNDNSRGMNYETPMFNKVAILICEALNSIKVTQSDLANVLSRVVSVRHLENLVLRKENHQDVLFHSKELLLKSVLIAIGQSKEIETTATAEGGEIVFQNTAFTMWKLTYLDHKLMPILDQNFIEYKITLNEDKPISDMRIKELVSELRWQYNRFAAITHGKGHYRVVKYSSVANHADRVFATFKNNTKSGNVTEFNLLDQRIIWQNWYAFTSSMKQGNTLDVCKKLLFQKMKQEKNPFKGLSTDRKMDEVSHVGI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MK936381
EMBL· GenBank· DDBJ
QGH58776.1
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