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Q9PY93

- NSP2_ROTHC

UniProt

Q9PY93 - NSP2_ROTHC

Protein

Non-structural protein 2

Gene
N/A
Organism
Rotavirus C (isolate Human/United Kingdom/Bristol/1989) (RV-C)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 57 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      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 sitei222 – 2221For 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 C (isolate Human/United Kingdom/Bristol/1989) (RV-C)
    Taxonomic identifieri31567 [NCBI]
    Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000007664: 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
    Mutagenesisi185 – 1851K → A: Loss of NTPase activity and dsRNA synthesis. No effect on octamerization. 1 Publication
    Mutagenesisi222 – 2221H → A: Loss of NTPase activity and dsRNA synthesis. No effect on octamerization. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 312312Non-structural protein 2PRO_0000367815Add
    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 similarity

    Structurei

    Secondary structure

    1
    312
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 63
    Beta strandi8 – 114
    Beta strandi13 – 164
    Beta strandi18 – 214
    Helixi24 – 329
    Helixi37 – 393
    Beta strandi47 – 493
    Helixi55 – 606
    Helixi74 – 9017
    Helixi94 – 963
    Helixi99 – 1035
    Helixi108 – 11912
    Helixi124 – 1263
    Helixi129 – 13911
    Helixi149 – 1513
    Beta strandi157 – 1604
    Beta strandi162 – 1709
    Beta strandi175 – 1773
    Beta strandi182 – 19211
    Helixi196 – 20914
    Beta strandi213 – 2164
    Beta strandi218 – 22710
    Helixi228 – 2303
    Helixi231 – 24313
    Helixi264 – 27512
    Helixi279 – 2824
    Helixi285 – 2884
    Helixi293 – 30715

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GU0X-ray2.80A/B1-312[»]
    ProteinModelPortaliQ9PY93.
    SMRiQ9PY93. Positions 2-309.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9PY93.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni202 – 23837RNA-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.

    Q9PY93-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAELACFVSF SLTEDKVVWY PINKKAVQTM LCAKVEKDQR SNYYDTILYG    50
    VAPPPEFRNR FKTNERYGLD YESDQYTELV NLLADTLNMV SMPTEKFQFD 100
    IVKTVVQVRH LENLLCRIKD VNDILNANVK LRVKAVMIAC NLVNETETTP 150
    LTESNDIVYQ DSYFTITKLD YSNHKLLPLM ADEYKITINT KTDIPDRNQT 200
    AFAAYIRYNF NKFAAISHGK RHWRLVLHSQ LMSHAERLDR KIKSDKKHGR 250
    QFSYDDGDMA FVHPGWKTCI GQLCGGTTFE VAKTSLYSIK PSKTVRTATN 300
    KIESDLISMV GN 312
    Length:312
    Mass (Da):35,915
    Last modified:May 1, 2000 - v1
    Checksum:iD2E6C11B6582637F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ132205 Genomic RNA. Translation: CAB52753.1.
    RefSeqiYP_392488.1. NC_007545.1.

    Genome annotation databases

    GeneIDi3773135.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ132205 Genomic RNA. Translation: CAB52753.1 .
    RefSeqi YP_392488.1. NC_007545.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GU0 X-ray 2.80 A/B 1-312 [» ]
    ProteinModelPortali Q9PY93.
    SMRi Q9PY93. Positions 2-309.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 3773135.

    Miscellaneous databases

    EvolutionaryTracei Q9PY93.

    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. "Molecular characterization of human group C rotavirus genes 6, 7 and 9."
      James V.L., Lambden P.R., Deng Y., Caul E.O., Clarke I.N.
      J. Gen. Virol. 80:3181-3187(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    2. "Structure-function analysis of rotavirus NSP2 octamer by using a novel complementation system."
      Taraporewala Z.F., Jiang X., Vasquez-Del Carpio R., Jayaram H., Prasad B.V.V., Patton J.T.
      J. Virol. 80:7984-7994(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), MUTAGENESIS OF LYS-185 AND HIS-222.

    Entry informationi

    Entry nameiNSP2_ROTHC
    AccessioniPrimary (citable) accession number: Q9PY93
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: May 1, 2000
    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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    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