Q2Y2M5 · PHOSP_AMPV1

Function

function

Plays critical roles in regulating RNA replication and transcription through its interactions with multiple proteins (By similarity).
Tethers the RNA-directed RNA polymerase L to the nucleoprotein-RNA complex (By similarity).
Recruits the M2-1 protein, a processivity factor that is required for efficient transcription of viral RNA. Acts as a chaperone for neo-synthesized nucleoprotein by forming an N-P complex that preserves N in a monomeric and RNA-free state and prevents the association of nascent N with host cell RNAs. Recruits the host phosphatase PP1 to inclusion bodies to regulate viral transcription (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
Cellular Componenthost cell cytoplasm
Cellular Componentvirion component
Molecular FunctionRNA-dependent RNA polymerase activity

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Phosphoprotein

Organism names

Accessions

  • Primary accession
    Q2Y2M5

Proteomes

Subcellular Location

Virion
Host cytoplasm
Note: Localizes in cytoplasmic inclusion bodies.

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00003903701-294Phosphoprotein
Modified residue106Phosphoserine
Modified residue148Phosphoserine
Modified residue157Phosphoserine
Modified residue158Phosphoserine
Modified residue168Phosphoserine
Modified residue171Phosphoserine

Post-translational modification

Constitutively phosphorylated by host.

Keywords

Interaction

Subunit

Homotetramer (By similarity).
Interacts with protein M2-1; the interaction between the two tetramers is required for the anti-termination and elongation transcriptional activities of protein M2-1. Interacts with host phosphatase PP1; this interaction recruits PP1 to the inclusion bodies. Formation of a complex PP1/M2-1/P allows P to target host PP1 phosphatase to the M2-1 substrate. Interacts with the nucleoprotein N; the phosphorylated phosphoprotein P binds to N-RNA complex. Interacts with the monomeric RNA-free nucleoprotein N (By similarity).
Interacts with RNA-directed RNA polymerase L (via N-terminus); the association of P and L forms the polymerase complex (By similarity).

Structure

3D structure databases

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region12-28Binding to monomeric RNA-free nucleoprotein
Region52-97Disordered
Compositional bias67-95Basic and acidic residues
Region123-128Binding to host phosphatase PP1
Region135-157Binding to protein M2-1
Region169-194Oligomerization and binding to RNA-directed RNA polymerase L
Region234-294Disordered
Region251-279Binding to RNA-directed RNA polymerase L
Compositional bias267-287Acidic residues
Region281-294Binding to the N-RNA complex

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    294
  • Mass (Da)
    32,541
  • Last updated
    2005-12-20 v1
  • Checksum
    9B82254688931B71
MSFPEGKDILLMGNEAAKAAEAFQRSLKKIGHRRTQSIVGDKIITVSETVEKPTISKSTKVTTPPERRNAWGEKPDTTRNQTEEARNEATLEDTSRLYEEVFAPTSDGKTPAEEGMETPEKPKKKVTFKNDESGRYTKLEMEALELLSDNEDDDAESSVLTFEEKDTSALSLEARLESIDEKLSMILGLLRTLNVATAGPTAARDGIRDAMVGLREELIADIIKEAKGKAAEMMKEEAKQKSKIGNGSVGLTEKAKELNKIVEDESTSGESEEEEEEEDEEESNPDDDLYSLTM

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias67-95Basic and acidic residues
Compositional bias267-287Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DQ009484
EMBL· GenBank· DDBJ
AAY81655.1
EMBL· GenBank· DDBJ
Viral cRNA

Similar Proteins

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