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Q03242

- NSP2_ROTSP

UniProt

Q03242 - NSP2_ROTSP

Protein

Non-structural protein 2

Gene
N/A
Organism
Rotavirus A (strain SA11-Patton G3-Px[x]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-Ex-Hx) (RV-A) (Simian Agent 11 (strain Patton))
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      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), ATP-independent helix-unwinding and nucleoside diphosphate kinase-like 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.2 Publications

    Cofactori

    Magnesium for NTPase activity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi153 – 1531MagnesiumSequence Analysis
    Metal bindingi171 – 1711MagnesiumSequence Analysis
    Active sitei225 – 2251For NTPase/RTPase 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 (strain SA11-Patton G3-Px[x]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-Ex-Hx) (RV-A) (Simian Agent 11 (strain Patton))
    Taxonomic identifieri36434 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirusRotavirus A
    Virus hostiMacaca mulatta (Rhesus macaque) [TaxID: 9544]

    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 317317Non-structural protein 2PRO_0000149551Add
    BLAST

    Interactioni

    Subunit structurei

    Homooctamer. 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 similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ03242.
    SMRiQ03242. 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.

    Q03242-1 [UniParc]FASTAAdd to Basket

    « Hide

    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 AFTSTMKQGN TLDVCKRLLF QKMKPEKNPF 300
    KGLSTDRKMD EVSQVGV 317
    Length:317
    Mass (Da):36,583
    Last modified:June 1, 1994 - v1
    Checksum:i3D7BEC23CFF84E62
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04531 Genomic RNA. Translation: AAA47298.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04531 Genomic RNA. Translation: AAA47298.1 .

    3D structure databases

    ProteinModelPortali Q03242.
    SMRi Q03242. Positions 1-313.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Nucleotide and amino acid sequence analysis of the rotavirus nonstructural RNA-binding protein NS35."
      Patton J.T., Salter-Cid L., Kalbach A.N., Mansell E.A., Kattoura M.D.
      Virology 192:438-446(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "The rotavirus nonstructural protein, NS35, possesses RNA-binding activity in vitro and in vivo."
      Kattoura M.D., Clapp L.L., Patton J.T.
      Virology 191:698-708(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING.
    3. "The rotavirus RNA-binding protein NS35 (NSP2) forms 10S multimers and interacts with the viral RNA polymerase."
      Kattoura M.D., Chen X., Patton J.T.
      Virology 202:803-813(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VP1.
    4. "Multimers formed by the rotavirus nonstructural protein NSP2 bind to RNA and have nucleoside triphosphatase activity."
      Taraporewala Z.F., Chen D., Patton J.T.
      J. Virol. 73:9934-9943(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, RNA-BINDING.
    5. "Rotavirus nonstructural protein NSP2 self-assembles into octamers that undergo ligand-induced conformational changes."
      Schuck P., Taraporewala Z.F., McPhie P., Patton J.T.
      J. Biol. Chem. 276:9679-9687(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, FUNCTION.
    6. "Identification and characterization of the helix-destabilizing activity of rotavirus nonstructural protein NSP2."
      Taraporewala Z.F., Patton J.T.
      J. Virol. 75:4519-4527(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiNSP2_ROTSP
    AccessioniPrimary (citable) accession number: Q03242
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 57 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3