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A2T3P0

- NSP2_ROTSH

UniProt

A2T3P0 - NSP2_ROTSH

Protein

Non-structural protein 2

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 29 (01 Oct 2014)
      Sequence version 1 (15 Jan 2008)
      Previous versions | rss
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    Functioni

    Involved in genome replication and packaging. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms) which are large inclusions in the cytoplasm where replication intermediates are assembled and RNA replication takes place. Displays ssRNA binding, NTPase, RNA triphosphatase (RTPase) and ATP-independent helix-unwinding activity activities. The unwiding activity may prepare and organize plus-strand RNAs for packaging and replication by removing interfering secondary structures. Unlike typical helicases, NSP2 requires neither a divalent cation nor a nucleotide energy source for helix destabilization. The RTPase activity may account for the absence of the 5'-terminal gamma-phosphate on the minus-strands of dsRNA genome segments By similarity.By similarity

    Cofactori

    Magnesium for NTPase activity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi153 – 1531MagnesiumSequence Analysis
    Metal bindingi171 – 1711MagnesiumSequence Analysis
    Active sitei225 – 2251For NTPase activityBy similarity

    GO - Molecular functioni

    1. hydrolase activity, acting on acid anhydrides Source: InterPro
    2. metal ion binding Source: UniProtKB-KW
    3. nucleotide binding Source: UniProtKB-KW
    4. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. viral genome replication Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Non-structural protein 2 (EC:3.6.4.-)
    Short name:
    NSP2
    Alternative name(s):
    NCVP3
    Non-structural RNA-binding protein 35
    Short name:
    NS35
    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 Curated
    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
    Mutagenesisi110 – 1101H → A: 35% loss of NTPase activity. 1 Publication
    Mutagenesisi153 – 1531E → A: Almost complete loss of NTPase activity. Unable to induce NSP5 phosphorylation. 1 Publication
    Mutagenesisi171 – 1711Y → A: Almost complete loss of NTPase activity. 1 Publication
    Mutagenesisi188 – 1881K → A: Almost complete loss of NTPase activity. Unable to induce NSP5 phosphorylation. 1 Publication
    Mutagenesisi221 – 2211H → A: Almost complete loss of NTPase activity. 1 Publication
    Mutagenesisi223 – 2231K → A: 75% loss of NTPase activity. 1 Publication
    Mutagenesisi225 – 2251H → A: Almost complete loss of NTPase activity. Unable to induce NSP5 phosphorylation. 1 Publication
    Mutagenesisi227 – 2271R → A: Almost complete loss of NTPase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 317317Non-structural protein 2PRO_0000367818Add
    BLAST

    Interactioni

    Subunit structurei

    Homooctamer By similarity. Interacts with VP1; this interaction is weak. Interacts with NSP5; this interaction leads to up-regulation of NSP5 hyperphosphorylation and formation of virus factories.By similarity2 Publications

    Structurei

    3D structure databases

    ProteinModelPortaliA2T3P0.
    SMRiA2T3P0. Positions 1-313.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni205 – 24137RNA-bindingSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the rotavirus NSP2 family.Curated

    Family and domain databases

    Gene3Di3.30.428.20. 1 hit.
    3.90.1400.10. 1 hit.
    InterProiIPR003668. Rotavirus_NSP2.
    IPR024076. Rotavirus_NSP2_C-term.
    IPR024068. Rotavirus_NSP2_N.
    [Graphical view]
    PfamiPF02509. Rota_NS35. 1 hit.
    [Graphical view]
    SUPFAMiSSF75347. SSF75347. 1 hit.
    SSF75574. SSF75574. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    A2T3P0-1 [UniParc]FASTAAdd to Basket

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    MAELACFCYP HLENDSYKFI PFNNLAIKAM LTAKVDKKDM DKFYDSIIYG    50
    IAPPPQFKKR YNTNDNSRGM NFETIMFTKV AMLICEALNS LKVTQANVSN 100
    VLSRVVSIRH LENLVIRKEN PQDILFHSKD LLLKSTLIAI GQSKEIETTI 150
    TAEGGEIVFQ NAAFTMWKLT YLEHQLMPIL DQNFIEYKVT LNEDKPISDV 200
    HVKELVAELR WQYNKFAVIT HGKGHYRIVK YSSVANHADR VYATFKSNVK 250
    TGVNNDFNLL DQRIIWQNWY AFTSSMKQGN TLDVCKRLLF QKMKPEKNPF 300
    KGLSTDRKMD EVSQVGV 317
    Length:317
    Mass (Da):36,569
    Last modified:January 15, 2008 - v1
    Checksum:i3D7BEA9514934E62
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ838615 Genomic RNA. Translation: ABG75789.1.
    RefSeqiYP_002302221.1. NC_011502.2.

    Genome annotation databases

    GeneIDi7011357.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ838615 Genomic RNA. Translation: ABG75789.1 .
    RefSeqi YP_002302221.1. NC_011502.2.

    3D structure databases

    ProteinModelPortali A2T3P0.
    SMRi A2T3P0. Positions 1-313.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 7011357.

    Family and domain databases

    Gene3Di 3.30.428.20. 1 hit.
    3.90.1400.10. 1 hit.
    InterProi IPR003668. Rotavirus_NSP2.
    IPR024076. Rotavirus_NSP2_C-term.
    IPR024068. Rotavirus_NSP2_N.
    [Graphical view ]
    Pfami PF02509. Rota_NS35. 1 hit.
    [Graphical view ]
    SUPFAMi SSF75347. SSF75347. 1 hit.
    SSF75574. SSF75574. 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. "Role of the histidine triad-like motif in nucleotide hydrolysis by the rotavirus RNA-packaging protein NSP2."
      Carpio R.V., Gonzalez-Nilo F.D., Jayaram H., Spencer E., Prasad B.V.V., Patton J.T., Taraporewala Z.F.
      J. Biol. Chem. 279:10624-10633(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF HIS-110; GLU-153; TYR-171; LYS-188; HIS-221; LYS-223; HIS-225 AND ARG-227.
    3. "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: INTERACTION WITH NSP5.
    4. "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.
    5. "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 NSP5 OR RNA.

    Entry informationi

    Entry nameiNSP2_ROTSH
    AccessioniPrimary (citable) accession number: A2T3P0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 29 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