ID   NSP2_ROTGA              Reviewed;         279 AA.
AC   Q86197; Q5K038;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-NOV-2023, entry version 57.
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 B (isolate RVB/Human/China/ADRV/1982) (RV-B) (Rotavirus B
OS   (isolate adult diarrhea rotavirus)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus B.
OX   NCBI_TaxID=10942;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=16054865; DOI=10.1016/j.jcv.2005.05.009;
RA   Jiang B., Wang Y., Glass R.I., Fang Z.-Y.;
RT   "The evolution of human group B rotaviruses: correction and an update.";
RL   J. Clin. Virol. 34:158-159(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Mackow E.R., Chen G., Werner R., Fay M.E., Tao H.;
RT   "Primary identification of the eighth RNA segment of the group B rotavirus
RT   ADRV.";
RL   Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAI30287.1; Type=Frameshift;
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DR   EMBL; M91437; AAA47328.1; -; mRNA.
DR   EMBL; AJ867609; CAI30287.1; ALT_FRAME; Genomic_RNA.
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   2: Evidence at transcript level;
KW   ATP-binding; Host cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide-binding; RNA-binding.
FT   CHAIN           1..279
FT                   /note="Non-structural protein 2"
FT                   /id="PRO_0000369851"
FT   REGION          214..249
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT   ACT_SITE        233
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         201
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT   BINDING         229..231
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT   BINDING         235
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT   CONFLICT        60
FT                   /note="C -> S (in Ref. 2; CAI30287)"
FT   CONFLICT        63
FT                   /note="P -> L (in Ref. 2; CAI30287)"
FT   CONFLICT        84
FT                   /note="M -> I (in Ref. 2; CAI30287)"
FT   CONFLICT        105
FT                   /note="N -> S (in Ref. 2; CAI30287)"
FT   CONFLICT        142
FT                   /note="R -> H (in Ref. 2; CAI30287)"
FT   CONFLICT        146
FT                   /note="G -> S (in Ref. 2; CAI30287)"
FT   CONFLICT        175
FT                   /note="S -> T (in Ref. 2; CAI30287)"
SQ   SEQUENCE   279 AA;  32110 MW;  9C48F27D0943BCA2 CRC64;
     MTQSVSLSDF IVKTEDGYMP SDRECIALDR YLSKEQKELR ETFKDGKNDR AALRIKMFLC
     PSPSRRFTQH GVVPMREIKT NTDMPSTLWT LVTDWLLNLL QDEENQEMFE DFISSKFPDV
     LASADKLARF AQRLEDRKDV LRKNFGKAMN AFGACFWAIK PTFATEGKCN VVRASDDSII
     LEFQPVPEYF RCGKSKATFY KLYPLSDEQP VNGMLALKAV AGNQFFMYHG HGHIRTVPYH
     ELLTLSNHSL VKIKKRSKTF LNHHSQLNVV VNFSICSME
//