ID   NSP2_ROTB2              Reviewed;         297 AA.
AC   Q0H8C2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 49.
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 (isolate RVX/Human/Bangladesh/NADRV-B219/2002/GXP[X]) (RV
OS   ADRV-N) (Rotavirus (isolate novel adult diarrhea rotavirus-B219)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; unclassified Rotavirus.
OX   NCBI_TaxID=348136;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=16900303; DOI=10.1007/s00705-006-0831-y;
RA   Alam M.M., Kobayashi N., Ishino M., Ahmed M.S., Ahmed M.U., Paul S.K.,
RA   Muzumdar B.K., Hussain Z., Wang Y.H., Naik T.N.;
RT   "Genetic analysis of an ADRV-N-like novel rotavirus strain B219 detected in
RT   a sporadic case of adult diarrhea in Bangladesh.";
RL   Arch. Virol. 152:199-208(2007).
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;
CC         Evidence={ECO:0000255|HAMAP-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}.
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DR   EMBL; DQ168035; ABA60395.1; -; Genomic_RNA.
DR   PRIDE; Q0H8C2; -.
DR   Proteomes; UP000174021; 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_0000369852"
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;  33554 MW;  C3090C54595FCC06 CRC64;
     MVSIKVSLAD FIVKTDEGWI PSDNCPALDR FKTKTEKELL DSIKREGADR ASIRKQLFLT
     PISNKRLTQI GGVPVRDIRT STTIPSSTRN LITDWLLNIF NDEESGEEVE NAIASKYPDI
     FCSADKISRV AQRLENRRDR VHEDGFRILS ATMLAIDSDI ATEGKCEIVR ATEDAIIAKF
     EPVSEHLCIG NPRGVFYKAF PIKKEQPMVY GIKALLGISN RDFIMNHGHG HLRTVPYSEI
     NNAIRSFAKK NEAEIKRIRS DSLSPNAGEK FINMCDMLLQ KEKIETIIAK IMKNDKN