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Q03243

- NSP2_ROTSR

UniProt

Q03243 - NSP2_ROTSR

Protein

Non-structural protein 2

Gene
N/A
Organism
Rotavirus A (strain SA11-Ramig G3-Px[x]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-Ex-Hx) (RV-A) (Simian Agent 11 (strain Ramig))
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 71 (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) 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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi153 – 1531MagnesiumSequence Analysis
    Metal bindingi171 – 1711MagnesiumSequence Analysis
    Active sitei225 – 2251For NTPase/RTPase activity1 Publication

    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-Ramig G3-Px[x]-Ix-Rx-Cx-Mx-Ax-Nx-Tx-Ex-Hx) (RV-A) (Simian Agent 11 (strain Ramig))
    Taxonomic identifieri36435 [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_0000149552Add
    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

    Secondary structure

    1
    317
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 63
    Beta strandi8 – 136
    Beta strandi16 – 216
    Helixi24 – 318
    Helixi37 – 393
    Beta strandi47 – 493
    Helixi55 – 606
    Beta strandi68 – 703
    Helixi75 – 8915
    Turni90 – 923
    Turni95 – 973
    Helixi98 – 1036
    Helixi108 – 11811
    Helixi124 – 1274
    Helixi129 – 13911
    Helixi149 – 1513
    Beta strandi156 – 1605
    Beta strandi162 – 1687
    Helixi171 – 1733
    Beta strandi175 – 1773
    Beta strandi186 – 1916
    Helixi199 – 21214
    Turni213 – 2153
    Beta strandi216 – 2194
    Beta strandi222 – 2309
    Helixi231 – 2333
    Helixi234 – 25118
    Turni262 – 2643
    Helixi267 – 27711
    Helixi282 – 2898
    Beta strandi295 – 2973
    Turni299 – 3024
    Helixi303 – 31210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1L9VX-ray2.60A1-317[»]
    2R7CX-ray2.70A1-317[»]
    2R7JX-ray2.60A1-317[»]
    2R7PX-ray2.80A1-317[»]
    2R8FX-ray2.80A1-317[»]
    4G0AX-ray2.10A/B/C/D1-317[»]
    4G0JX-ray3.40A/B/C/D/E/F/G/H/I/J1-294[»]
    ProteinModelPortaliQ03243.
    SMRiQ03243. Positions 1-313.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ03243.

    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.

    Q03243-1 [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 AFTSSMKQGN TLDVCKRLLF QKMKPEKNPF 300
    KGLSTDRKMD EVSQVGV 317
    Length:317
    Mass (Da):36,569
    Last modified:June 1, 1994 - v1
    Checksum:i3D7BEA9514934E62
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04532 Genomic RNA. Translation: AAA47299.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04532 Genomic RNA. Translation: AAA47299.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1L9V X-ray 2.60 A 1-317 [» ]
    2R7C X-ray 2.70 A 1-317 [» ]
    2R7J X-ray 2.60 A 1-317 [» ]
    2R7P X-ray 2.80 A 1-317 [» ]
    2R8F X-ray 2.80 A 1-317 [» ]
    4G0A X-ray 2.10 A/B/C/D 1-317 [» ]
    4G0J X-ray 3.40 A/B/C/D/E/F/G/H/I/J 1-294 [» ]
    ProteinModelPortali Q03243.
    SMRi Q03243. Positions 1-313.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q03243.

    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. "Rotavirus protein involved in genome replication and packaging exhibits a HIT-like fold."
      Jayaram H., Taraporewala Z.F., Patton J.T., Prasad B.V.V.
      Nature 417:311-315(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
    3. "Crystallographic and biochemical analysis of rotavirus NSP2 with nucleotides reveals a nucleoside diphosphate kinase-like activity."
      Kumar M., Jayaram H., Vasquez-Del Carpio R., Jiang X., Taraporewala Z.F., Jacobson R.H., Patton J.T., Prasad B.V.V.
      J. Virol. 81:12272-12284(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), ACTIVE SITE.

    Entry informationi

    Entry nameiNSP2_ROTSR
    AccessioniPrimary (citable) accession number: Q03243
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 71 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

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3