A0A0B6VNV2 · A0A0B6VNV2_9REOV
- ProteinNon-structural protein 5
- GeneNSP5
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids197 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Plays an essential role in the viral genome replication. Participates, together with NSP2, in the formation of viral factories (viroplasms) which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Orchestrates the recruitment of viroplasmic proteins such as capsid proteins to these factories. Participates in the selective exclusion of host proteins from stress granules (SG) and P bodies (PB). Participates also in the sequestration of these remodeled organelles in viral factories.
Cofactor
Features
Showing features for binding site.
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 | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | nucleotide binding | |
Molecular Function | RNA binding | |
Biological Process | viral genome replication |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameNon-structural protein 5
- Short namesNSP5
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Orthornavirae > Duplornaviricota > Resentoviricetes > Reovirales > Sedoreoviridae > Rotavirus > Rotavirus A
Accessions
- Primary accessionA0A0B6VNV2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 67 | Phosphoserine; by host CK1 | ||||
Sequence: S | ||||||
Modified residue | 153 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Modified residue | 155 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Modified residue | 163 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Modified residue | 165 | Phosphoserine; by host | ||||
Sequence: S |
Post-translational modification
Hyperphosphorylated on serine residues, when in dimeric form. Phosphorylation by host CK1 is required for the hyperphosphorylation of NSP5 dimer.
O-glycosylated.
Keywords
- PTM
Interaction
Subunit
Homodimer. Interacts with VP1. Interacts with VP2. Interacts with NSP2; this interaction leads to up-regulation of NSP5 hyperphosphorylation and formation of virus factories. Interacts with NSP6. Interacts with host DCP1A, DCP1B, DDX6, EDC4, EIF2S1/eIF2-alpha, AGO2 and CAPRIN1; these interactions are probably part of the sequestration of some host SGs and PBs proteins in viral factories.
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 17-37 | Disordered | ||||
Sequence: IFKNESSSTTSTLSGKSIGRS | ||||||
Region | 53-72 | Disordered | ||||
Sequence: LSKSPEDIGPSDSASNDPLT | ||||||
Region | 85-104 | Disordered | ||||
Sequence: ADAGVSMDSSTQSRPSSNVG | ||||||
Region | 130-166 | Disordered | ||||
Sequence: TDHKKEKSKKDKSRKHYPRIEADSDSEDYVLDDSDSD |
Sequence similarities
Belongs to the rotavirus NSP5 family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length197
- Mass (Da)21,561
- Last updated2015-04-01 v1
- ChecksumDC11F551FE3A54B8