ID   NSP2_ROTS1              Reviewed;         317 AA.
AC   P03537;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 101.
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 A (strain RVA/SA11-Both/G3P5B[2]) (RV-A) (Simian Agent 11 (strain
OS   Both)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=37137;
OH   NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6296764; DOI=10.1093/nar/10.22.7075;
RA   Both G.W., Bellamy A.R., Street J.E., Siegman L.J.;
RT   "A general strategy for cloning double-stranded RNA: nucleotide sequence of
RT   the Simian-11 rotavirus gene 8.";
RL   Nucleic Acids Res. 10:7075-7088(1982).
RN   [2]
RP   COFACTOR, AND FUNCTION.
RX   PubMed=10559306; DOI=10.1128/jvi.73.12.9934-9943.1999;
RA   Taraporewala Z.F., Chen D., Patton J.T.;
RT   "Multimers formed by the rotavirus nonstructural protein NSP2 bind to RNA
RT   and have nucleoside triphosphatase activity.";
RL   J. Virol. 73:9934-9943(1999).
RN   [3]
RP   FUNCTION, INTERACTION WITH NSP5, AND SUBCELLULAR LOCATION.
RX   PubMed=14993647; DOI=10.1099/vir.0.19611-0;
RA   Eichwald C., Rodriguez J.F., Burrone O.R.;
RT   "Characterization of rotavirus NSP2/NSP5 interactions and the dynamics of
RT   viroplasm formation.";
RL   J. Gen. Virol. 85:625-634(2004).
RN   [4]
RP   FUNCTION, SUBUNIT, AND CATALYTIC ACTIVITY.
RX   PubMed=22811529; DOI=10.1128/jvi.01201-12;
RA   Hu L., Chow D.C., Patton J.T., Palzkill T., Estes M.K., Prasad B.V.;
RT   "Crystallographic Analysis of Rotavirus NSP2-RNA Complex Reveals Specific
RT   Recognition of 5' GG Sequence for RTPase Activity.";
RL   J. Virol. 86:10547-10557(2012).
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 (PubMed:14993647). Displays ssRNA binding,
CC       NTPase, RNA triphosphatase (RTPase) and ATP-independent helix-unwinding
CC       activities (PubMed:22811529). The unwinding activity may prepare and
CC       organize plus-strand RNAs for packaging and replication by removing
CC       interfering secondary structures (PubMed:22811529). The RTPase activity
CC       plays a role in the removal of the gamma-phosphate from the rotavirus
CC       RNA minus strands of dsRNA genome segments (PubMed:22811529).
CC       Participates in the selective exclusion of host proteins from stress
CC       granules (SG) and P bodies (PB). Participates also in the sequestration
CC       of these remodeled organelles in viral factories (By similarity).
CC       {ECO:0000255|HAMAP-Rule:MF_04089, ECO:0000269|PubMed:14993647,
CC       ECO:0000269|PubMed:22811529}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_04089};
CC   -!- SUBUNIT: Homooctamer (PubMed:22811529). Interacts with VP1; this
CC       interaction is weak. Interacts with NSP5; this interaction leads to up-
CC       regulation of NSP5 phosphorylation and formation of viral factories
CC       (PubMed:14993647). Interacts with host DCP1A, DCP1B, DDX6, EDC4 and
CC       EIF2S1/eIF2-alpha; these interactions are probably part of the
CC       sequestration of some host SGs and PBs proteins in viral factories (By
CC       similarity). {ECO:0000255|HAMAP-Rule:MF_04089,
CC       ECO:0000269|PubMed:14993647, ECO:0000269|PubMed:22811529}.
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; J02353; AAA47293.1; -; Genomic_RNA.
DR   PIR; A04144; WMXR3S.
DR   SMR; P03537; -.
DR   Proteomes; UP000007180; 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:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:InterPro.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019079; P:viral genome replication; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.428.20; Rotavirus NSP2 fragment, C-terminal domain; 1.
DR   Gene3D; 3.90.1400.10; Rotavirus NSP2 fragment, N-terminal domain; 1.
DR   HAMAP; MF_04089; ROTA_NSP2; 1.
DR   InterPro; IPR048306; Rota_NS35_C.
DR   InterPro; IPR048573; Rota_NS35_N.
DR   InterPro; IPR003668; Rotavirus_NSP2.
DR   InterPro; IPR024076; Rotavirus_NSP2_C.
DR   InterPro; IPR024068; Rotavirus_NSP2_N.
DR   Pfam; PF02509; Rota_NS35_C; 1.
DR   Pfam; PF21067; Rota_NS35_N; 1.
DR   SUPFAM; SSF75347; Rotavirus NSP2 fragment, C-terminal domain; 1.
DR   SUPFAM; SSF75574; Rotavirus NSP2 fragment, N-terminal domain; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Host cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; RNA-binding.
FT   CHAIN           1..317
FT                   /note="Non-structural protein 2"
FT                   /id="PRO_0000149550"
FT   REGION          205..241
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT   ACT_SITE        225
FT                   /note="For NTPase and RTPase activities"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089,
FT                   ECO:0000269|PubMed:22811529"
FT   BINDING         107..109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT   BINDING         188
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT   BINDING         221..223
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT   BINDING         227
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
SQ   SEQUENCE   317 AA;  36628 MW;  25670C29E6607474 CRC64;
     MAELACFCYP HLENDSYRFI PFNSLAIKCM LTAKVDKKDQ DKFYNSIIYG IAPPPQFKKR
     YNTSDNSRGM NYETSMFNKV AALICEALNS IKVTQSDVAS VLSKIVSVRH LENLVLRREN
     HQDVLFHSKE LLLKSVLIAI GHSKEIETTA TAEGGEIVFQ NAAFTMWKLT YLEHKLMPIL
     DQNFIEYKIT LNEDKPISES HVKELIAELR WQYNKFAVIT HGKGHYRVVK YSSVANHADR
     VYATFKSNNK NGNMIEFNLL DQRIIWQNWY AFTSSMKQGN TLEICKKLLF QKMKRESNPF
     KGLSTDRKMD EVSQIGI
//