Q91DS2 · PHOSP_SVCV
- ProteinPhosphoprotein
- GeneP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids309 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template. May act as a chaperone for newly synthesized free N protein, so-called N0. Plays a role in virion assembly.
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 | host cell cytoplasm | |
Cellular Component | virion component | |
Biological Process | viral transcription |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended namePhosphoprotein
- Short namesP protein; Protein P
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Negarnaviricota > Haploviricotina > Monjiviricetes > Mononegavirales > Rhabdoviridae > Alpharhabdovirinae > Sprivivirus
- Virus hosts
Accessions
- Primary accessionQ91DS2
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000287351 | 1-309 | Phosphoprotein | |||
Sequence: MSLHSKLSESLKAYADLDKTVKEIEEQVSSMEEPVPKTVKYVTFEENLSEEEWESDSGDDDEDSIDDSLIPDYLRESSSITVDEDEEDQKEDMEEHLPTVSWEEEPTGIDIGFGPGIVMPSVSNHEGGTYVRYNGLGGVDPNCKDLISKMMRSLIGQIGNKYGYDIDLFDYQGDFLEVFLPHKPSKEDVRPDIRIGKKNEEGTSKQVSKPRGKEKIVLKTGDECGRFPMNKEAKKREPEGLWEVMKVLSVQFDPWKEDEPPLSLTIRDLFISESEFRLHCNHSQTEREMALVGIKLRRLYNKLYQKYRL | ||||||
Modified residue | 14 | Phosphotyrosine; by host | ||||
Sequence: Y | ||||||
Modified residue | 272 | Phosphoserine; by host | ||||
Sequence: S |
Post-translational modification
Phosphorylated by host kinases. Phosphorylation play an important role in facilitating trimerization and possibly P-L complex formation.
Keywords
- PTM
Interaction
Subunit
Homotrimer. This trimer is stabilized by binding to the L protein. Binds N0, and N in ribonucleocapsid (By similarity).
May bind to host ref2P (PubMed:7684462).
May bind to host ref2P (PubMed:7684462).
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 38-98 | Disordered | ||||
Sequence: TVKYVTFEENLSEEEWESDSGDDDEDSIDDSLIPDYLRESSSITVDEDEEDQKEDMEEHLP | ||||||
Compositional bias | 48-67 | Acidic residues | ||||
Sequence: LSEEEWESDSGDDDEDSIDD |
Sequence similarities
Belongs to the vesiculovirus protein P family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length309
- Mass (Da)35,513
- Last updated2001-12-01 v1
- Checksum1D0E682F23E8E8DA
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 48-67 | Acidic residues | ||||
Sequence: LSEEEWESDSGDDDEDSIDD |
Keywords
- Technical term