ID   NSP2_ROTP5              Reviewed;         317 AA.
AC   P09366;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 82.
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/Pig/United States/OSU/1977/G5P9[7]) (RV-A)
OS   (Rotavirus A (strain Ohio State University)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=10915;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2829124; DOI=10.1093/nar/16.1.367;
RA   Rushlow K., McNab A., Olson K., Maxwell F., Maxwell I., Stiegler G.;
RT   "Nucleotide sequence of porcine rotavirus (OSU strain) gene segments 7, 8,
RT   and 9.";
RL   Nucleic Acids Res. 16:367-368(1988).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X06722; CAA29902.1; -; mRNA.
DR   PIR; S01747; WMXR5U.
DR   SMR; P09366; -.
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   Gene3D; 3.30.428.20; -; 1.
DR   Gene3D; 3.90.1400.10; -; 1.
DR   HAMAP; MF_04089; ROTA_NSP2; 1.
DR   InterPro; IPR003668; Rotavirus_NSP2.
DR   InterPro; IPR024076; Rotavirus_NSP2_C.
DR   InterPro; IPR024068; Rotavirus_NSP2_N.
DR   Pfam; PF02509; Rota_NS35; 1.
DR   SUPFAM; SSF75347; SSF75347; 1.
DR   SUPFAM; SSF75574; SSF75574; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Host cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide-binding; RNA-binding.
FT   CHAIN           1..317
FT                   /note="Non-structural protein 2"
FT                   /id="PRO_0000149549"
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   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;  36456 MW;  333C3F7D831A7E7C CRC64;
     MAELACFCYP HLEKDSYKFI PFNSLAIKCM LTAKVDKKDQ DKFYNSIVYG IAPPPQFKKR
     YNTNDNSRGM NFETSMFNKV AILICEALNS IKVTQSDVAN VLSRVVSVRH LENLVLRKEN
     HQDVLFHSKE LLLKAVLIAI GQSKEIETTA TAEGGEIVFQ NAAFTMWKLT YLDHKLMPIL
     DQNFIEYKIT LNEDKPISDA CVKELVAELR WQYNRFAVIT HGKGHYRVVK YSSVANHADR
     VFATYKNNAK SGNVTDFNLL DQRIIWQNWY AFTSSMKQGN TLDVCKKLLF QKMKQEKNPF
     KGLSTDRKMD EVSHVGI