NSP2_ROTJ1
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 03-AUG-2022, entry version 47.
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; Reoviridae; Sedoreovirinae; Rotavirus.
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;
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; DQ113903; AAZ03491.1; -; Genomic_RNA.
DR RefSeq; YP_392496.1; NC_007554.1.
DR PRIDE; Q45UF4; -.
DR GeneID; 5076656; -.
DR KEGG; vg:5076656; -.
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