Q8BB23 · NCAP_CVP67
- ProteinNucleoprotein
- GeneN
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids449 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 106 | RNA (UniProtKB | ChEBI) | |||
Binding site | 122 | RNA (UniProtKB | ChEBI) | |||
Binding site | 164 | RNA (UniProtKB | ChEBI) | |||
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 endoplasmic reticulum-Golgi intermediate compartment | |
Cellular Component | host cell Golgi apparatus | |
Cellular Component | ribonucleoprotein complex | |
Cellular Component | viral nucleocapsid | |
Molecular Function | RNA binding |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameNucleoprotein
- Alternative names
Gene names
Organism names
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Pisuviricota > Pisoniviricetes > Nidovirales > Cornidovirineae > Coronaviridae > Orthocoronavirinae > Betacoronavirus > Embecovirus > Betacoronavirus 1
- Virus hosts
Accessions
- Primary accessionQ8BB23
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Located inside the virion, complexed with the viral RNA. Probably associates with ER-derived membranes where it participates in viral RNA synthesis and virus budding.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000106011 | 1-449 | Nucleoprotein | ||
Modified residue | 167 | Phosphoserine; by host | |||
Modified residue | 174 | Phosphothreonine; by host | |||
Modified residue | 191 | Phosphoserine; by host | |||
Modified residue | 391 | Phosphoserine; by host | |||
Modified residue | 424 | Phosphoserine; by host | |||
Modified residue | 428 | Phosphothreonine; by host | |||
Post-translational modification
ADP-ribosylated. The ADP-ribosylation is retained in the virion during infection.
Phosphorylated on serine and threonine residues.
Keywords
- PTM
Interaction
Subunit
Homooligomer. Both monomeric and oligomeric forms interact with RNA. Interacts with protein M. Interacts with NSP3; this interaction serves to tether the genome to the newly translated replicase-transcriptase complex at a very early stage of infection.
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-55 | Disordered | |||
Region | 52-194 | RNA-binding | |||
Domain | 61-190 | CoV N NTD | |||
Region | 158-231 | Disordered | |||
Compositional bias | 191-231 | Polar residues | |||
Domain | 259-384 | CoV N CTD | |||
Region | 266-297 | Disordered | |||
Region | 266-385 | Dimerization | |||
Compositional bias | 273-290 | Polar residues | |||
Compositional bias | 387-422 | Polar residues | |||
Region | 387-449 | Disordered | |||
Compositional bias | 423-449 | Basic and acidic residues | |||
Sequence similarities
Belongs to the betacoronavirus nucleocapsid protein family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length449
- Mass (Da)49,514
- Last updated2003-03-01 v1
- ChecksumA9C486B39831F733
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 191-231 | Polar residues | |||
Compositional bias | 273-290 | Polar residues | |||
Compositional bias | 387-422 | Polar residues | |||
Compositional bias | 423-449 | Basic and acidic residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY078417 EMBL· GenBank· DDBJ | AAL80036.1 EMBL· GenBank· DDBJ | Genomic RNA |