Q9WMB4 · PHOSP_MEASC

Function

function

Essential cofactor of the RNA polymerase L that plays a central role in the transcription and replication by forming the polymerase complex with RNA polymerase L and recruiting L to the genomic N-RNA template for RNA synthesis (By similarity).
Plays also a central role in the encapsidation of nascent RNA chains by forming the encapsidation complex with the nucleocapsid protein N (N-P complex). Acts as a chaperone for newly synthesized free N protein, so-called N0, allowing encapsidation of nascent RNA chains during replication (By similarity).
The nucleoprotein protein N prevents excessive phosphorylation of P, which leads to down-regulation of viral transcription/ replication (By similarity).
Participates, together with N, in the formation of viral factories (viroplasms), which are large inclusions in the host cytoplasm where replication takes place (PubMed:32270045).

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
Molecular FunctionRNA binding
Molecular FunctionRNA-dependent RNA polymerase activity
Biological ProcessDNA-templated transcription
Biological Processviral genome replication

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Phosphoprotein
  • Short names
    Protein P

Gene names

    • Name
      P/V

Organism names

Accessions

  • Primary accession
    Q9WMB4

Proteomes

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00003947171-507Phosphoprotein
Modified residue86Phosphoserine
Modified residue151Phosphoserine

Post-translational modification

Phosphorylation on serines by host CK2 is necessary for the formation of viral factories.

Keywords

Interaction

Subunit

Homotetramer. Interacts (via multimerization domain) with polymerase L; this interaction forms the polymerase L-P complex (By similarity).
Interacts (via N-terminus) with N0 (via Ncore); this interaction allows P to chaperon N0 to avoid N polymerization before encapsidation (By similarity).
Interacts (via C-terminus) with N-RNA template (via C-terminus); this interaction positions the polymerase on the template for both transcription and replication (PubMed:32270045).

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region40-92Disordered
Region133-168Disordered
Compositional bias142-156Acidic residues
Region201-228Disordered
Region252-273Disordered
Region304-376Multimerization
Region459-507Interaction with the nucleocapsid (N-RNA)

Domain

The N-terminus consists of a long intrinsically disordered tail. The central part contains the coiled-coil multimerization domain (PMD) (By similarity).
Forms a four-stranded coiled coil structure (By similarity).
The C-terminus constitutes the alpha-helical domain that binds to the nucleocapsid (N-RNA complex) (By similarity).

Sequence similarities

Belongs to the morbillivirus P protein family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    507
  • Mass (Da)
    53,898
  • Last updated
    1999-11-01 v1
  • Checksum
    056474FC4452119A
MAEEQARHVKNGLECIRALKAEPIGSLAVEEAMAAWSEISDNPGQDRATCKEEEAGSSGLSKPCLSAIGSTEGGAPRIRGQGSGESDDDAETLGIPSRNLQASSTGLQCYHVYDHSGEAVKGIQDADSIMVQSGLDGDSTLSGGDDESENSDVDIGEPDTEGYAITDRGSAPISMGFRASDVETAEGGEIHELLKLQSRGNNFPKLGKTLNVPPPPNPSRASTSETPIKKGTDARLASFGTEIASLLTGGATQCARKSPSEPSGPGAPAGNVPECVSNAALIQEWTPESGTTISPRSQNNEEGGDYYDDELFSDVQDIKTALAKIHEDNQKIISKLESLLLLKGEVESIKKQINRQNISISTLEGHLSSIMIAIPGLGKDPNDPTADVELNPDLKPIIGRDSGRALAEVLKKPVASRQLQGMTNGRTSSRGQLLKEFQLKPIGKKVSSAVGFVPDTGPASRSVIRSIIKSSRLEEDRKRYLMTLLDDIKGANDLAKFHQMLMKIIMK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias142-156Acidic residues

RNA Editing

Edited at position 231
Partially edited. RNA editing at this position consists of an insertion of one guanine nucleotide. The sequence displayed here is the P protein, derived from the unedited RNA. The edited RNA gives rise to the V protein (AC P0C774) (By similarity)

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB016162
EMBL· GenBank· DDBJ
BAA34978.1
EMBL· GenBank· DDBJ
Genomic RNA

Genome annotation databases

Similar Proteins

Disclaimer

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