ID   NSP2_ROTJ1              Reviewed;         297 AA.
AC   Q45UF4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   08-NOV-2023, entry version 51.
DE   RecName: Full=Non-structural protein 2 {ECO:0000255|HAMAP-Rule:MF_04089};
DE            Short=NSP2 {ECO:0000255|HAMAP-Rule:MF_04089};
DE            EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_04089};
DE   AltName: Full=NCVP3 {ECO:0000255|HAMAP-Rule:MF_04089};
DE   AltName: Full=Non-structural RNA-binding protein 35 {ECO:0000255|HAMAP-Rule:MF_04089};
DE            Short=NS35 {ECO:0000255|HAMAP-Rule:MF_04089};
OS   Rotavirus X (strain RVX/Human/China/NADRV-J19/1997/GXP[X]) (RV ADRV-N)
OS   (Rotavirus (isolate novel adult diarrhea rotavirus-J19)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus H.
OX   NCBI_TaxID=335103;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=18796732; DOI=10.1099/vir.0.2008/001933-0;
RA   Jiang S., Ji S., Tang Q., Cui X., Yang H., Kan B., Gao S.;
RT   "Molecular characterization of a novel adult diarrhoea rotavirus strain J19
RT   isolated in China and its significance for the evolution and origin of
RT   group B rotaviruses.";
RL   J. Gen. Virol. 89:2622-2629(2008).
CC   -!- FUNCTION: Participates in replication and packaging of the viral
CC       genome. Plays a crucial role, together with NSP5, in the formation of
CC       virus factories (viroplasms) which are large inclusions in the host
CC       cytoplasm where replication intermediates are assembled and viral RNA
CC       replication takes place. Displays ssRNA binding, NTPase, RNA
CC       triphosphatase (RTPase) and ATP-independent helix-unwinding activities.
CC       The unwinding activity may prepare and organize plus-strand RNAs for
CC       packaging and replication by removing interfering secondary structures.
CC       The RTPase activity plays a role in the removal of the gamma-phosphate
CC       from the rotavirus RNA minus strands of dsRNA genome segments.
CC       {ECO:0000255|HAMAP-Rule:MF_04089}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_04089};
CC   -!- SUBUNIT: Homooctamer. Interacts with VP1; this interaction is weak.
CC       Interacts with NSP5; this interaction leads to up-regulation of NSP5
CC       phosphorylation and formation of viral factories. {ECO:0000255|HAMAP-
CC       Rule:MF_04089}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04089}.
CC       Note=Found in spherical cytoplasmic structures, called viral factories,
CC       that appear early after infection and are the site of viral replication
CC       and packaging. {ECO:0000255|HAMAP-Rule:MF_04089}.
CC   -!- SIMILARITY: Belongs to the rotavirus NSP2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_04089}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ113903; AAZ03491.1; -; Genomic_RNA.
DR   RefSeq; YP_392496.1; NC_007554.1.
DR   GeneID; 5076656; -.
DR   KEGG; vg:5076656; -.
DR   OrthoDB; 14946at10239; -.
DR   Proteomes; UP000007663; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019079; P:viral genome replication; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04089; ROTA_NSP2; 1.
DR   InterPro; IPR003668; Rotavirus_NSP2.
PE   3: Inferred from homology;
KW   ATP-binding; Host cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; RNA-binding.
FT   CHAIN           1..297
FT                   /note="Non-structural protein 2"
FT                   /id="PRO_0000369853"
FT   REGION          212..247
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT   ACT_SITE        231
FT                   /note="For NTPase and RTPase activities"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT   BINDING         119..121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT   BINDING         198
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT   BINDING         227..229
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT   BINDING         233
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
SQ   SEQUENCE   297 AA;  33433 MW;  4F16788D9EA04819 CRC64;
     MVSIKVSLAD FIVKTEEGWI PSDNCPALDR FKTKTEKELL DSIKKEGADR ASIRKQLFLT
     SISNKRLTQL GGVPVRDIRT STTIPSSTRN LITDWLLNIF NDEESGEEVE SAIASKYPDI
     FCSADKISRV AQRLENRRDR VHEDGFRILS ATMLAIDSDI ATEGKCEIVR ATEDAIIAKF
     EPVSEHLCIG NPRGVFYKAF PIKKEQPMVY GVKALLGISN RDFIMNHGHG HLRTVPYSEI
     NNAVRSFAKK NEAEIKRIRS DSLSPNAGEK FINMCDMLLQ KEKIETVIAK IMKSDKN
//