A0A059V6V8 · A0A059V6V8_9RHAB
- ProteinPhosphoprotein
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids297 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | host cell cytoplasm | |
Cellular Component | virion component | |
Molecular Function | RNA-dependent RNA polymerase activity | |
Biological Process | symbiont-mediated suppression of host innate immune response | |
Biological Process | symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity | |
Biological Process | symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity | |
Biological Process | symbiont-mediated suppression of host type I interferon-mediated signaling pathway | |
Biological Process | viral transcription | |
Biological Process | virus-mediated perturbation of host defense response |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended namePhosphoprotein
- Short namesProtein P
- Alternative names
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Negarnaviricota > Haploviricotina > Monjiviricetes > Mononegavirales > Rhabdoviridae > Alpharhabdovirinae > Lyssavirus
Accessions
- Primary accessionA0A059V6V8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Phosphoprotein
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Interaction
Subunit
Homotrimer when phosphorylated. This trimer is stabilized by binding to the L protein. Binds soluble protein N, and ribonucleocapsid.
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 137-185 | Polar residues | ||||
Sequence: LGRSSEDKSTQTAGGELKRETPSASSQKKSQSLKARTEVHTTSGPPALE | ||||||
Region | 137-189 | Disordered | ||||
Sequence: LGRSSEDKSTQTAGGELKRETPSASSQKKSQSLKARTEVHTTSGPPALEWSAT |
Sequence similarities
Belongs to the lyssavirus protein P family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length297
- Mass (Da)33,270
- Last updated2014-09-03 v1
- Checksum2006039F8E9A63F5
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 137-185 | Polar residues | ||||
Sequence: LGRSSEDKSTQTAGGELKRETPSASSQKKSQSLKARTEVHTTSGPPALE |