P28054 · PHOSP_PI1HC
- ProteinPhosphoprotein
- GeneP/C
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids568 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score2/5
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).
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 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 | |
---|---|---|
Molecular Function | RNA binding | |
Molecular Function | RNA-dependent RNA polymerase activity | |
Biological Process | DNA-templated transcription | |
Biological Process | viral genome replication |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended namePhosphoprotein
- Short namesProtein P
Gene names
Organism names
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Negarnaviricota > Haploviricotina > Monjiviricetes > Mononegavirales > Paramyxoviridae > Feraresvirinae > Respirovirus > Respirovirus laryngotracheitidis
- Virus hosts
Accessions
- Primary accessionP28054
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000142700 | 1-568 | Phosphoprotein | |||
Sequence: MDQDAFFFERDPEAEGEAPRKQESLSGVIGLLDVVLSYKPTEIGEDRSWLHGIIDNPEENKPSCKADDNNKDRAISTPTQDHRSGEESGISRRTSESKTETHARLLDQQSIHRASRRGTSPNPLPENMGNERNTRIDEDSPNERRHQRSVLTDEDRKMAEDSNKREEDQVEGFPEEIRRSTPLSDDGESRTNNNGRSMETSSTHSTRITDVIINPSPELEDAVLQRNKRRPTIIRRNQTRSERTQNSELHKSTSENSSNLEDHNTKTSPKGLPPKNEESAATPKNNHNHRKTKYTMNNANNNTKSPPTPEHDTTANEEETSNTSVDEMAKLLVSLGVMKSQHEFELSRSASHVFAKRMLKSANYKEMTFNLCGMLISVEKSLENKVEENRTLLKQIQEEINSSRDLHKRFSEYQKEQNSLMMANLSTLHIITDRGGKTGDPSDTTRSPSVFTKGKDNKVKKTRFDPSMEALGGQEFKPDLIREDELRDDIKNPVLEENNNDLQASNASRLIPSTEKHTLHSLKLVIENSPLSRVEKKAYIKSLYKCRTNQEVKNVMELFEEDIDSLTN |
Keywords
- PTM
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.
Family & Domains
Features
Showing features for compositional bias, region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-20 | Basic and acidic residues | ||||
Sequence: MDQDAFFFERDPEAEGEAPR | ||||||
Region | 1-24 | Disordered | ||||
Sequence: MDQDAFFFERDPEAEGEAPRKQES | ||||||
Region | 33-41 | N0 binding | ||||
Sequence: DVVLSYKPT | ||||||
Compositional bias | 45-111 | Basic and acidic residues | ||||
Sequence: EDRSWLHGIIDNPEENKPSCKADDNNKDRAISTPTQDHRSGEESGISRRTSESKTETHARLLDQQSI | ||||||
Region | 45-324 | Disordered | ||||
Sequence: EDRSWLHGIIDNPEENKPSCKADDNNKDRAISTPTQDHRSGEESGISRRTSESKTETHARLLDQQSIHRASRRGTSPNPLPENMGNERNTRIDEDSPNERRHQRSVLTDEDRKMAEDSNKREEDQVEGFPEEIRRSTPLSDDGESRTNNNGRSMETSSTHSTRITDVIINPSPELEDAVLQRNKRRPTIIRRNQTRSERTQNSELHKSTSENSSNLEDHNTKTSPKGLPPKNEESAATPKNNHNHRKTKYTMNNANNNTKSPPTPEHDTTANEEETSNTS | ||||||
Compositional bias | 112-129 | Polar residues | ||||
Sequence: HRASRRGTSPNPLPENMG | ||||||
Compositional bias | 131-185 | Basic and acidic residues | ||||
Sequence: ERNTRIDEDSPNERRHQRSVLTDEDRKMAEDSNKREEDQVEGFPEEIRRSTPLSD | ||||||
Compositional bias | 186-212 | Polar residues | ||||
Sequence: DGESRTNNNGRSMETSSTHSTRITDVI | ||||||
Compositional bias | 235-249 | Basic and acidic residues | ||||
Sequence: RRNQTRSERTQNSEL | ||||||
Compositional bias | 250-272 | Polar residues | ||||
Sequence: HKSTSENSSNLEDHNTKTSPKGL | ||||||
Compositional bias | 292-310 | Polar residues | ||||
Sequence: TKYTMNNANNNTKSPPTPE | ||||||
Region | 344-411 | Multimerization | ||||
Sequence: FELSRSASHVFAKRMLKSANYKEMTFNLCGMLISVEKSLENKVEENRTLLKQIQEEINSSRDLHKRFS | ||||||
Coiled coil | 387-416 | |||||
Sequence: EENRTLLKQIQEEINSSRDLHKRFSEYQKE | ||||||
Region | 412-445 | L protein binding | ||||
Sequence: EYQKEQNSLMMANLSTLHIITDRGGKTGDPSDTT | ||||||
Region | 434-455 | Disordered | ||||
Sequence: RGGKTGDPSDTTRSPSVFTKGK | ||||||
Region | 479-568 | Interaction with the nucleocapsid (N-RNA) | ||||
Sequence: DLIREDELRDDIKNPVLEENNNDLQASNASRLIPSTEKHTLHSLKLVIENSPLSRVEKKAYIKSLYKCRTNQEVKNVMELFEEDIDSLTN |
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).
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
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length568
- Mass (Da)64,660
- Last updated1992-08-01 v1
- ChecksumC5E3CE2B83AE197A
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-20 | Basic and acidic residues | ||||
Sequence: MDQDAFFFERDPEAEGEAPR | ||||||
Compositional bias | 45-111 | Basic and acidic residues | ||||
Sequence: EDRSWLHGIIDNPEENKPSCKADDNNKDRAISTPTQDHRSGEESGISRRTSESKTETHARLLDQQSI | ||||||
Compositional bias | 112-129 | Polar residues | ||||
Sequence: HRASRRGTSPNPLPENMG | ||||||
Compositional bias | 131-185 | Basic and acidic residues | ||||
Sequence: ERNTRIDEDSPNERRHQRSVLTDEDRKMAEDSNKREEDQVEGFPEEIRRSTPLSD | ||||||
Compositional bias | 186-212 | Polar residues | ||||
Sequence: DGESRTNNNGRSMETSSTHSTRITDVI | ||||||
Compositional bias | 235-249 | Basic and acidic residues | ||||
Sequence: RRNQTRSERTQNSEL | ||||||
Compositional bias | 250-272 | Polar residues | ||||
Sequence: HKSTSENSSNLEDHNTKTSPKGL | ||||||
Compositional bias | 292-310 | Polar residues | ||||
Sequence: TKYTMNNANNNTKSPPTPE |