A0A059V6V8 · A0A059V6V8_9RHAB

  • Protein
    Phosphoprotein
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA. Also inhibits host IFN-alpha and IFN-beta signaling by binding and retaining phosphorylated STAT1 in the cytoplasm or by inhibiting the DNA binding of STAT1 in the nucleus.

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 Componentcytoplasm
Cellular Componenthost cell cytoplasm
Cellular Componentvirion component
Molecular FunctionRNA-dependent RNA polymerase activity
Biological Processsymbiont-mediated suppression of host innate immune response
Biological Processsymbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity
Biological Processsymbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity
Biological Processsymbiont-mediated suppression of host type I interferon-mediated signaling pathway
Biological Processviral transcription
Biological Processvirus-mediated perturbation of host defense response

Keywords

Names & Taxonomy

Protein names

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

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • R2013-01
  • Taxonomic lineage
    Viruses > Riboviria > Orthornavirae > Negarnaviricota > Haploviricotina > Monjiviricetes > Mononegavirales > Rhabdoviridae > Alpharhabdovirinae > Lyssavirus

Accessions

  • Primary accession
    A0A059V6V8

Proteomes

Subcellular Location

Cytoplasm
Virion

Phosphoprotein

Virion
Host cytoplasm

Keywords

PTM/Processing

Keywords

Interaction

Subunit

Homotrimer when phosphorylated. This trimer is stabilized by binding to the L protein. Binds soluble protein N, and ribonucleocapsid.

Family & Domains

Features

Showing features for compositional bias, region.

TypeIDPosition(s)Description
Compositional bias137-185Polar residues
Region137-189Disordered

Sequence similarities

Belongs to the lyssavirus protein P family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    297
  • Mass (Da)
    33,270
  • Last updated
    2014-09-03 v1
  • Checksum
    2006039F8E9A63F5
MSKIFVNPSAIRAGLADLEMAEETVDLISRNIEDNQAHLQGEPIEVDNLPEDMRRLQLDDGKPSDPSEVAAVGGDKYREDFQMDEGEDPALLFQSYLDNVGVQMVRQMRSGERFLKIWSQTVEEIISYVTINFSNPLGRSSEDKSTQTAGGELKRETPSASSQKKSQSLKARTEVHTTSGPPALEWSATNEEDDLSVEAEIAHQIAESFSKKYKFPSRSSGIFLYNFEQLKMNLDDIVKESKNVPGITHLAHDGSKLPLRCILGWVALANSKKFQLLVEPDKLNKIMQDDLNRYTSC

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias137-185Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KF620489
EMBL· GenBank· DDBJ
AHZ89647.1
EMBL· GenBank· DDBJ
Viral cRNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp