NSP2_ROTGA
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 03-AUG-2022, entry version 54.
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; Reoviridae; Sedoreovirinae; Rotavirus.
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;
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}.
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 PRIDE; Q86197; -.
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
