Q91DS2 · PHOSP_SVCV

Function

function

Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template. May act as a chaperone for newly synthesized free N protein, so-called N0. Plays a role in virion assembly.

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
Cellular Componentvirion component
Biological Processviral transcription

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Phosphoprotein
  • Short names
    P protein; Protein P
  • Alternative names
    • Protein M1

Gene names

    • Name
      P

Organism names

Accessions

  • Primary accession
    Q91DS2

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002873511-309Phosphoprotein
Modified residue14Phosphotyrosine; by host
Modified residue272Phosphoserine; by host

Post-translational modification

Phosphorylated by host kinases. Phosphorylation play an important role in facilitating trimerization and possibly P-L complex formation.

Keywords

Interaction

Subunit

Homotrimer. This trimer is stabilized by binding to the L protein. Binds N0, and N in ribonucleocapsid (By similarity).
May bind to host ref2P (PubMed:7684462).

Structure

3D structure databases

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region38-98Disordered
Compositional bias48-67Acidic residues

Sequence similarities

Belongs to the vesiculovirus protein P family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    309
  • Mass (Da)
    35,513
  • Last updated
    2001-12-01 v1
  • Checksum
    1D0E682F23E8E8DA
MSLHSKLSESLKAYADLDKTVKEIEEQVSSMEEPVPKTVKYVTFEENLSEEEWESDSGDDDEDSIDDSLIPDYLRESSSITVDEDEEDQKEDMEEHLPTVSWEEEPTGIDIGFGPGIVMPSVSNHEGGTYVRYNGLGGVDPNCKDLISKMMRSLIGQIGNKYGYDIDLFDYQGDFLEVFLPHKPSKEDVRPDIRIGKKNEEGTSKQVSKPRGKEKIVLKTGDECGRFPMNKEAKKREPEGLWEVMKVLSVQFDPWKEDEPPLSLTIRDLFISESEFRLHCNHSQTEREMALVGIKLRRLYNKLYQKYRL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias48-67Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ318079
EMBL· GenBank· DDBJ
CAC51334.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

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