A2T3Q9 · NSP5_ROTSH

Function

function

Plays an essential role in the viral genome replication. Participates, together with NSP2, in the formation of viral factories (viroplasms), which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Orchestrates the recruitment of viroplasmic proteins such as capsid proteins to these factories (PubMed:11884570, PubMed:17825341).
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 (By similarity).

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for binding site.

119820406080100120140160180
TypeIDPosition(s)Description
Binding site92Mg2+ (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 hydrolysis activity
Molecular Functionmagnesium ion binding
Molecular Functionnucleotide binding
Molecular FunctionRNA binding
Biological Processviral genome replication

Keywords

Community curation (1)

Serine protein kinase activity. Has weak autophosphorylating activity.

Names & Taxonomy

Protein names

  • Recommended name
    Non-structural protein 5
  • Short names
    NSP5
  • Alternative names
    • NS26

Organism names

Accessions

  • Primary accession
    A2T3Q9

Proteomes

Subcellular Location

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

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis67Loss of hyperphosphorylation.
Mutagenesis67Constitutively hyperphosphorylated even in the absence of infection.
Mutagenesis154-166Loss of phosphorylation.

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00003678251-198Non-structural protein 5
Modified residue67Phosphoserine; by host CK1
Modified residue154Phosphoserine; by host
Modified residue156Phosphoserine; by host
Modified residue164Phosphoserine; by host
Modified residue166Phosphoserine; by host

Post-translational modification

O-glycosylated.
Hyperphosphorylated on serine residues, when in dimeric form. Phosphorylation by host CK1 is required for the hyperphosphorylation of NSP5 dimer.

Keywords

PTM databases

Interaction

Subunit

Homodimer. Interacts with VP1 (PubMed:17182692).
Interacts with VP2. Interacts with NSP2; this interaction leads to up-regulation of NSP5 hyperphosphorylation and formation of virus factories (PubMed:14993647, PubMed:16928740).
Interacts with NSP6. Interacts with host DCP1A, DCP1B, DDX6, EDC4, EIF2S1/eIF2-alpha, AGO2 and CAPRIN1; these interactions are probably part of the sequestration of some host SGs and PBs proteins in viral factories (By similarity).

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region1-48Interaction with VP1
Region13-37Disordered
Region53-72Disordered
Region129-167Disordered

Sequence similarities

Belongs to the rotavirus NSP5 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    198
  • Mass (Da)
    21,722
  • Last updated
    2008-01-15 v1
  • Checksum
    1DE1EC4A803E1D57
MSLSIDVTSLPSIPSTIYKNESSSTTSTLSGKSIGRSEQYISPDAEAFNKYMLSKSPEDIGPSDSASNDPLTSFSIRSNAVKTNADAGVSMDSSAQSRPSSNVGCDQVDFSLNKGLKVKANLDSSISISTDTKKEKSKQNHKSRKHYPRIEAESDSDDYVLDDSDSDDGKCKNCKYKKKYFALRMRMKQVAMQLIEDL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ838630
EMBL· GenBank· DDBJ
ABG75808.1
EMBL· GenBank· DDBJ
Genomic RNA

Genome annotation databases

Similar Proteins

Disclaimer

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