ID   NSP2_ROTA1              Reviewed;         315 AA.
AC   Q03244;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 80.
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/Turkey/Ireland/Ty-1/1978/G7P[17]) (RV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=12584;
OH   NCBI_TaxID=8782; Aves.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8380660; DOI=10.1006/viro.1993.1059;
RA   Patton J.T., Salter-Cid L., Kalbach A.N., Mansell E.A., Kattoura M.D.;
RT   "Nucleotide and amino acid sequence analysis of the rotavirus nonstructural
RT   RNA-binding protein NS35.";
RL   Virology 192:438-446(1993).
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       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. {ECO:0000255|HAMAP-
CC       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. Interacts with host
CC       DCP1A, DCP1B, DDX6, EDC4 and EIF2S1/eIF2-alpha; these interactions are
CC       probably part of the sequestration of some host SGs and PBs proteins in
CC       viral factories. {ECO:0000255|HAMAP-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; L04533; AAA47300.1; -; Genomic_RNA.
DR   SMR; Q03244; -.
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   3: Inferred from homology;
KW   ATP-binding; Host cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide-binding; RNA-binding.
FT   CHAIN           1..315
FT                   /note="Non-structural protein 2"
FT                   /id="PRO_0000149553"
FT   REGION          204..240
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT   ACT_SITE        224
FT                   /note="For NTPase and RTPase activities"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT   BINDING         106..108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT   BINDING         187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT   BINDING         220..222
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
FT   BINDING         226
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04089"
SQ   SEQUENCE   315 AA;  35930 MW;  B4FB84AB69EA65C6 CRC64;
     MAELACFCYP CDREGASVAR YSRSAIKCML SAKIDKSHSS QPYDTQVYGL APPPVYKKRF
     NDGNNSRGMN FDTDMYDKVA DLLVQILNGI KIGKDKAAEI MAVPISVRHL ENLIYRIENK
     DDILSADPNL ITKSVLIAMG LIKDCELTTT AEGGDIVFQN QGFTMWRLDY KSHVLMPITD
     PNFVEYKITL NHTNPIDDKI VKELVAELRW QYNKFAVITH GKGHYRVVRY STVANHADRV
     YSTFKSIQKR NPSYKFNELD TRVIWTNWAA FVKSMLNGMK LDDSKRLLFT KMKPNESSFK
     GVTTERKLDE VSLLG
//