Q2Y2M5 · PHOSP_AMPV1
- ProteinPhosphoprotein
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids294 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
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).
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 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 | |
Molecular Function | RNA-dependent RNA polymerase activity |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended namePhosphoprotein
Organism names
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Negarnaviricota > Haploviricotina > Monjiviricetes > Mononegavirales > Pneumoviridae > Metapneumovirus > Metapneumovirus avis
- Virus hosts
Accessions
- Primary accessionQ2Y2M5
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes in cytoplasmic inclusion bodies.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000390370 | 1-294 | Phosphoprotein | |||
Sequence: MSFPEGKDILLMGNEAAKAAEAFQRSLKKIGHRRTQSIVGDKIITVSETVEKPTISKSTKVTTPPERRNAWGEKPDTTRNQTEEARNEATLEDTSRLYEEVFAPTSDGKTPAEEGMETPEKPKKKVTFKNDESGRYTKLEMEALELLSDNEDDDAESSVLTFEEKDTSALSLEARLESIDEKLSMILGLLRTLNVATAGPTAARDGIRDAMVGLREELIADIIKEAKGKAAEMMKEEAKQKSKIGNGSVGLTEKAKELNKIVEDESTSGESEEEEEEEDEEESNPDDDLYSLTM | ||||||
Modified residue | 106 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 148 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 157 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 158 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 168 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 171 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Constitutively phosphorylated by host.
Keywords
- PTM
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).
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).
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 12-28 | Binding to monomeric RNA-free nucleoprotein | ||||
Sequence: MGNEAAKAAEAFQRSLK | ||||||
Region | 52-97 | Disordered | ||||
Sequence: KPTISKSTKVTTPPERRNAWGEKPDTTRNQTEEARNEATLEDTSRL | ||||||
Compositional bias | 67-95 | Basic and acidic residues | ||||
Sequence: RRNAWGEKPDTTRNQTEEARNEATLEDTS | ||||||
Region | 123-128 | Binding to host phosphatase PP1 | ||||
Sequence: KKKVTF | ||||||
Region | 135-157 | Binding to protein M2-1 | ||||
Sequence: RYTKLEMEALELLSDNEDDDAES | ||||||
Region | 169-194 | Oligomerization and binding to RNA-directed RNA polymerase L | ||||
Sequence: ALSLEARLESIDEKLSMILGLLRTLN | ||||||
Region | 234-294 | Disordered | ||||
Sequence: MKEEAKQKSKIGNGSVGLTEKAKELNKIVEDESTSGESEEEEEEEDEEESNPDDDLYSLTM | ||||||
Region | 251-279 | Binding to RNA-directed RNA polymerase L | ||||
Sequence: LTEKAKELNKIVEDESTSGESEEEEEEED | ||||||
Compositional bias | 267-287 | Acidic residues | ||||
Sequence: TSGESEEEEEEEDEEESNPDD | ||||||
Region | 281-294 | Binding to the N-RNA complex | ||||
Sequence: EESNPDDDLYSLTM |
Sequence similarities
Belongs to the pneumoviridae phosphoprotein P family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length294
- Mass (Da)32,541
- Last updated2005-12-20 v1
- Checksum9B82254688931B71
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 67-95 | Basic and acidic residues | ||||
Sequence: RRNAWGEKPDTTRNQTEEARNEATLEDTS | ||||||
Compositional bias | 267-287 | Acidic residues | ||||
Sequence: TSGESEEEEEEEDEEESNPDD |
Keywords
- Technical term