P28054 · PHOSP_PI1HC

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. 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. Participates, together with N, in the formation of viral factories (viroplasms), which are large inclusions in the host cytoplasm where replication takes place (By similarity).
Recruits host PI4KB and remodel the host endoplasmic reticulum membrane to form viral replication factories (By similarity).

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/C

Organism names

Accessions

  • Primary accession
    P28054

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001427001-568Phosphoprotein

Keywords

Interaction

Subunit

Homotetramer. Interacts (via multimerization domain) with polymerase L; this interaction forms the polymerase complex. Interacts (via N-terminus) with N0; this interaction allows P to chaperon N0 before encapsidation and form the N-P complex. Interacts (via C-terminus) with N-RNA template; this interaction positions the polymerase on the template.

Structure

3D structure databases

Family & Domains

Features

Showing features for compositional bias, region, coiled coil.

TypeIDPosition(s)Description
Compositional bias1-20Basic and acidic residues
Region1-24Disordered
Region33-41N0 binding
Compositional bias45-111Basic and acidic residues
Region45-324Disordered
Compositional bias112-129Polar residues
Compositional bias131-185Basic and acidic residues
Compositional bias186-212Polar residues
Compositional bias235-249Basic and acidic residues
Compositional bias250-272Polar residues
Compositional bias292-310Polar residues
Region344-411Multimerization
Coiled coil387-416
Region412-445L protein binding
Region434-455Disordered
Region479-568Interaction with the nucleocapsid (N-RNA)

Domain

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

Sequence similarities

Belongs to the respirovirus P protein family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    568
  • Mass (Da)
    64,660
  • Last updated
    1992-08-01 v1
  • Checksum
    C5E3CE2B83AE197A
MDQDAFFFERDPEAEGEAPRKQESLSGVIGLLDVVLSYKPTEIGEDRSWLHGIIDNPEENKPSCKADDNNKDRAISTPTQDHRSGEESGISRRTSESKTETHARLLDQQSIHRASRRGTSPNPLPENMGNERNTRIDEDSPNERRHQRSVLTDEDRKMAEDSNKREEDQVEGFPEEIRRSTPLSDDGESRTNNNGRSMETSSTHSTRITDVIINPSPELEDAVLQRNKRRPTIIRRNQTRSERTQNSELHKSTSENSSNLEDHNTKTSPKGLPPKNEESAATPKNNHNHRKTKYTMNNANNNTKSPPTPEHDTTANEEETSNTSVDEMAKLLVSLGVMKSQHEFELSRSASHVFAKRMLKSANYKEMTFNLCGMLISVEKSLENKVEENRTLLKQIQEEINSSRDLHKRFSEYQKEQNSLMMANLSTLHIITDRGGKTGDPSDTTRSPSVFTKGKDNKVKKTRFDPSMEALGGQEFKPDLIREDELRDDIKNPVLEENNNDLQASNASRLIPSTEKHTLHSLKLVIENSPLSRVEKKAYIKSLYKCRTNQEVKNVMELFEEDIDSLTN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-20Basic and acidic residues
Compositional bias45-111Basic and acidic residues
Compositional bias112-129Polar residues
Compositional bias131-185Basic and acidic residues
Compositional bias186-212Polar residues
Compositional bias235-249Basic and acidic residues
Compositional bias250-272Polar residues
Compositional bias292-310Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M37792
EMBL· GenBank· DDBJ
AAA46868.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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