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A2T3Q9

- NSP5_ROTSH

UniProt

A2T3Q9 - NSP5_ROTSH

Protein

Non-structural protein 5

Gene
N/A
Organism
Rotavirus A (isolate Monkey/South Africa/SA11-H96/1958 G3-P5B[2]-I2-R2-C5-M5-A5-N5-T5-E2-H5) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58))
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 19 (01 Oct 2014)
      Sequence version 1 (15 Jan 2008)
      Previous versions | rss
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    Functioni

    Involved in genome replication. Plays a crucial role, together with NSP2, in the formation of virus factories (viroplasms) which are large inclusions in the cytoplasm where core-like replication intermediates are assembled and RNA replication takes place. May regulate NSP2-RNA interactions during genome replication, since NSP5 competes with RNA for the same binding site on the NSP2 octamer. Binds to either ssRNA or dsRNA with similar affinities. Displays ATPase and autokinase activities.2 Publications

    Cofactori

    Magnesium for ATPase activity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi92 – 921MagnesiumSequence Analysis

    GO - Molecular functioni

    1. ATPase activity Source: InterPro
    2. magnesium ion binding Source: InterPro
    3. nucleotide binding Source: UniProtKB-KW
    4. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. viral genome replication Source: InterPro

    Keywords - Ligandi

    Magnesium, Metal-binding, Nucleotide-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Non-structural protein 5
    Short name:
    NSP5
    Alternative name(s):
    NS26
    OrganismiRotavirus A (isolate Monkey/South Africa/SA11-H96/1958 G3-P5B[2]-I2-R2-C5-M5-A5-N5-T5-E2-H5) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58))
    Taxonomic identifieri450149 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
    Virus hostiCercopithecus pygerythrus (Vervet monkey) [TaxID: 60710]
    ProteomesiUP000001119: Genome

    Subcellular locationi

    Host cytoplasm 3 Publications
    Note: Found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging.

    GO - Cellular componenti

    1. host cell cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi67 – 671S → A: Loss of hyperphosphorylation. 2 Publications
    Mutagenesisi67 – 671S → D: Constitutively hyperphosphorylated even in the absence of infection. 2 Publications
    Mutagenesisi154 – 16613SDSDD…DDSDS → ADADDYVLDDADA: Loss of phosphorylation. 1 PublicationAdd
    BLAST

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 198198Non-structural protein 5PRO_0000367825Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei67 – 671Phosphoserine; by host CK12 Publications
    Modified residuei154 – 1541Phosphoserine; by host2 Publications
    Modified residuei156 – 1561Phosphoserine; by host2 Publications
    Modified residuei164 – 1641Phosphoserine; by host2 Publications
    Modified residuei166 – 1661Phosphoserine; by host2 Publications

    Post-translational modificationi

    O-glycosylated.By similarity
    Hyperphosphorylated on serine residues, when in dimeric form. Ser-67 phosphorylation by CK1 is required for the hyperphosphorylation of NSP5 dimer. Impaired phosphorylation is associated with a profound morphological change in virus factories and a moderate decrease in virus replication.3 Publications

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Interactioni

    Subunit structurei

    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 By similarity.By similarity

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 4848Interaction with VP1Add
    BLAST
    Regioni189 – 19810Homodimerization and interaction with NSP6By similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2 – 101100Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the rotavirus A NSP5 family.Curated

    Family and domain databases

    InterProiIPR002512. Rotavirus_A/C_NSP5.
    [Graphical view]
    PfamiPF01525. Rota_NS26. 1 hit.
    [Graphical view]
    PIRSFiPIRSF004006. Rota_NS26. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    A2T3Q9-1 [UniParc]FASTAAdd to Basket

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    MSLSIDVTSL PSIPSTIYKN ESSSTTSTLS GKSIGRSEQY ISPDAEAFNK    50
    YMLSKSPEDI GPSDSASNDP LTSFSIRSNA VKTNADAGVS MDSSAQSRPS 100
    SNVGCDQVDF SLNKGLKVKA NLDSSISIST DTKKEKSKQN HKSRKHYPRI 150
    EAESDSDDYV LDDSDSDDGK CKNCKYKKKY FALRMRMKQV AMQLIEDL 198
    Length:198
    Mass (Da):21,722
    Last modified:January 15, 2008 - v1
    Checksum:i1DE1EC4A803E1D57
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ838630 Genomic RNA. Translation: ABG75808.1.
    RefSeqiYP_002302224.1. NC_011505.2.

    Genome annotation databases

    GeneIDi7011364.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ838630 Genomic RNA. Translation: ABG75808.1 .
    RefSeqi YP_002302224.1. NC_011505.2.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 7011364.

    Family and domain databases

    InterProi IPR002512. Rotavirus_A/C_NSP5.
    [Graphical view ]
    Pfami PF01525. Rota_NS26. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF004006. Rota_NS26. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Genome heterogeneity of SA11 rotavirus due to reassortment with 'O' agent."
      Small C., Barro M., Brown T.L., Patton J.T.
      Virology 359:415-424(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Phosphorylation generates different forms of rotavirus NSP5."
      Afrikanova I., Miozzo M.C., Giambiagi S., Burrone O.R.
      J. Gen. Virol. 77:2059-2065(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    3. "RNA-binding activity of the rotavirus phosphoprotein NSP5 includes affinity for double-stranded RNA."
      Vende P., Taraporewala Z.F., Patton J.T.
      J. Virol. 76:5291-5299(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING.
    4. "Rotavirus NSP5: mapping phosphorylation sites and kinase activation and viroplasm localization domains."
      Eichwald C., Vascotto F., Fabbretti E., Burrone O.R.
      J. Virol. 76:3461-3470(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-154; SER-156; SER-164 AND SER-166, MUTAGENESIS OF 154-SER--SER-166.
    5. "Uncoupling substrate and activation functions of rotavirus NSP5: phosphorylation of Ser-67 by casein kinase 1 is essential for hyperphosphorylation."
      Eichwald C., Jacob G., Muszynski B., Allende J.E., Burrone O.R.
      Proc. Natl. Acad. Sci. U.S.A. 101:16304-16309(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-67 BY CK1, MUTAGENESIS OF SER-67.
    6. "Characterization of rotavirus NSP2/NSP5 interactions and the dynamics of viroplasm formation."
      Eichwald C., Rodriguez J.F., Burrone O.R.
      J. Gen. Virol. 85:625-634(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NSP2.
    7. "Impaired hyperphosphorylation of rotavirus NSP5 in cells depleted of casein kinase 1alpha is associated with the formation of viroplasms with altered morphology and a moderate decrease in virus replication."
      Campagna M., Budini M., Arnoldi F., Desselberger U., Allende J.E., Burrone O.R.
      J. Gen. Virol. 88:2800-2810(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE OF PHOSPHORYLATION BY CK1.
    8. "An ATPase activity associated with the rotavirus phosphoprotein NSP5."
      Bar-Magen T., Spencer E., Patton J.T.
      Virology 369:389-399(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Interaction of rotavirus polymerase VP1 with nonstructural protein NSP5 is stronger than that with NSP2."
      Arnoldi F., Campagna M., Eichwald C., Desselberger U., Burrone O.R.
      J. Virol. 81:2128-2137(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VP1, SUBCELLULAR LOCATION.
    10. "Cryoelectron microscopy structures of rotavirus NSP2-NSP5 and NSP2-RNA complexes: implications for genome replication."
      Jiang X., Jayaram H., Kumar M., Ludtke S.J., Estes M.K., Prasad B.V.V.
      J. Virol. 80:10829-10835(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY (9.0 ANGSTROMS) IN COMPLEX WITH NSP2.

    Entry informationi

    Entry nameiNSP5_ROTSH
    AccessioniPrimary (citable) accession number: A2T3Q9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 19 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3