ID NSP2_ROTSH Reviewed; 317 AA. AC A2T3P0; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 1. DT 27-MAR-2024, entry version 62. 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 (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A) OS (Simian Agent 11 (isolate SI/South Africa/H96/58)). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A. OX NCBI_TaxID=450149; OH NCBI_TaxID=60710; Chlorocebus pygerythrus (Vervet monkey) (Cercopithecus pygerythrus). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=17059839; DOI=10.1016/j.virol.2006.09.024; RA Small C., Barro M., Brown T.L., Patton J.T.; RT "Genome heterogeneity of SA11 rotavirus due to reassortment with 'O' RT agent."; RL Virology 359:415-424(2007). RN [2] RP FUNCTION, AND MUTAGENESIS OF HIS-110; GLU-153; TYR-171; LYS-188; HIS-221; RP LYS-223; HIS-225 AND ARG-227. RX PubMed=14699117; DOI=10.1074/jbc.m311563200; RA Carpio R.V., Gonzalez-Nilo F.D., Jayaram H., Spencer E., Prasad B.V.V., RA Patton J.T., Taraporewala Z.F.; RT "Role of the histidine triad-like motif in nucleotide hydrolysis by the RT rotavirus RNA-packaging protein NSP2."; RL J. Biol. Chem. 279:10624-10633(2004). RN [3] RP INTERACTION WITH NSP5. 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 INTERACTION WITH VP1. RX PubMed=17182692; DOI=10.1128/jvi.01494-06; RA Arnoldi F., Campagna M., Eichwald C., Desselberger U., Burrone O.R.; RT "Interaction of rotavirus polymerase VP1 with nonstructural protein NSP5 is RT stronger than that with NSP2."; RL J. Virol. 81:2128-2137(2007). RN [5] RP STRUCTURE BY ELECTRON MICROSCOPY (9.0 ANGSTROMS) IN COMPLEX WITH NSP5 OR RP RNA. RX PubMed=16928740; DOI=10.1128/jvi.01347-06; RA Jiang X., Jayaram H., Kumar M., Ludtke S.J., Estes M.K., Prasad B.V.V.; RT "Cryoelectron microscopy structures of rotavirus NSP2-NSP5 and NSP2-RNA RT complexes: implications for genome replication."; RL J. Virol. 80:10829-10835(2006). 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 (PubMed:14699117). Participates in the selective exclusion of host CC proteins from stress granules (SG) and P bodies (PB). Participates also CC in the sequestration of these remodeled organelles in viral factories CC (By similarity). {ECO:0000255|HAMAP-Rule:MF_04089, CC ECO:0000269|PubMed:14699117}. 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 (PubMed:17182692). 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:17182692}. 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; DQ838615; ABG75789.1; -; Genomic_RNA. DR RefSeq; YP_002302221.1; NC_011502.2. DR PDB; 6AUK; X-ray; 2.60 A; A=1-317. DR PDB; 6CY9; X-ray; 2.62 A; A=1-317. DR PDB; 6CYA; X-ray; 2.60 A; A=1-317. DR PDB; 7PKO; EM; 3.90 A; A/B/C/D/E/F/G/U=1-313. DR PDB; 7PKP; EM; 3.10 A; A/B/C/D/E/F/G/U=1-313. DR PDBsum; 6AUK; -. DR PDBsum; 6CY9; -. DR PDBsum; 6CYA; -. DR PDBsum; 7PKO; -. DR PDBsum; 7PKP; -. DR EMDB; EMD-13474; -. DR EMDB; EMD-13476; -. DR SMR; A2T3P0; -. DR GeneID; 7011357; -. DR KEGG; vg:7011357; -. DR Proteomes; UP000001119; 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 3D-structure; ATP-binding; Host cytoplasm; Host-virus interaction; KW Hydrolase; Magnesium; Metal-binding; Nucleotide-binding; KW Reference proteome; RNA-binding. FT CHAIN 1..317 FT /note="Non-structural protein 2" FT /id="PRO_0000367818" 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" FT MUTAGEN 110 FT /note="H->A: 35% loss of NTPase activity." FT /evidence="ECO:0000269|PubMed:14699117" FT MUTAGEN 153 FT /note="E->A: Almost complete loss of NTPase activity. FT Unable to induce NSP5 phosphorylation." FT /evidence="ECO:0000269|PubMed:14699117" FT MUTAGEN 171 FT /note="Y->A: Almost complete loss of NTPase activity." FT /evidence="ECO:0000269|PubMed:14699117" FT MUTAGEN 188 FT /note="K->A: Almost complete loss of NTPase activity. FT Unable to induce NSP5 phosphorylation." FT /evidence="ECO:0000269|PubMed:14699117" FT MUTAGEN 221 FT /note="H->A: Almost complete loss of NTPase activity." FT /evidence="ECO:0000269|PubMed:14699117" FT MUTAGEN 223 FT /note="K->A: 75% loss of NTPase activity." FT /evidence="ECO:0000269|PubMed:14699117" FT MUTAGEN 225 FT /note="H->A: Almost complete loss of NTPase activity. FT Unable to induce NSP5 phosphorylation." FT /evidence="ECO:0000269|PubMed:14699117" FT MUTAGEN 227 FT /note="R->A: Almost complete loss of NTPase activity." FT /evidence="ECO:0000269|PubMed:14699117" FT HELIX 4..6 FT /evidence="ECO:0007829|PDB:6CYA" FT STRAND 8..13 FT /evidence="ECO:0007829|PDB:6CYA" FT STRAND 16..21 FT /evidence="ECO:0007829|PDB:6CYA" FT HELIX 24..31 FT /evidence="ECO:0007829|PDB:6CYA" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:6CYA" FT STRAND 44..46 FT /evidence="ECO:0007829|PDB:6CYA" FT TURN 47..49 FT /evidence="ECO:0007829|PDB:6CYA" FT STRAND 50..52 FT /evidence="ECO:0007829|PDB:6CYA" FT HELIX 55..60 FT /evidence="ECO:0007829|PDB:6CYA" FT STRAND 66..70 FT /evidence="ECO:0007829|PDB:6CYA" FT HELIX 75..90 FT /evidence="ECO:0007829|PDB:6CYA" FT HELIX 95..97 FT /evidence="ECO:0007829|PDB:6CYA" FT HELIX 98..103 FT /evidence="ECO:0007829|PDB:6CYA" FT HELIX 108..118 FT /evidence="ECO:0007829|PDB:6CYA" FT HELIX 124..127 FT /evidence="ECO:0007829|PDB:6CYA" FT HELIX 129..139 FT /evidence="ECO:0007829|PDB:6CYA" FT HELIX 149..151 FT /evidence="ECO:0007829|PDB:7PKP" FT STRAND 156..160 FT /evidence="ECO:0007829|PDB:6CYA" FT STRAND 162..168 FT /evidence="ECO:0007829|PDB:6CYA" FT HELIX 171..173 FT /evidence="ECO:0007829|PDB:6CYA" FT STRAND 175..177 FT /evidence="ECO:0007829|PDB:6CYA" FT STRAND 186..195 FT /evidence="ECO:0007829|PDB:6CYA" FT HELIX 199..212 FT /evidence="ECO:0007829|PDB:6CYA" FT TURN 213..215 FT /evidence="ECO:0007829|PDB:6AUK" FT STRAND 216..219 FT /evidence="ECO:0007829|PDB:6CYA" FT STRAND 222..230 FT /evidence="ECO:0007829|PDB:6CYA" FT HELIX 231..233 FT /evidence="ECO:0007829|PDB:6CYA" FT HELIX 234..251 FT /evidence="ECO:0007829|PDB:6CYA" FT TURN 262..264 FT /evidence="ECO:0007829|PDB:6CYA" FT HELIX 267..277 FT /evidence="ECO:0007829|PDB:6CYA" FT HELIX 282..290 FT /evidence="ECO:0007829|PDB:6CYA" FT STRAND 300..302 FT /evidence="ECO:0007829|PDB:6CY9" FT HELIX 303..312 FT /evidence="ECO:0007829|PDB:6CYA" SQ SEQUENCE 317 AA; 36569 MW; 3D7BEA9514934E62 CRC64; MAELACFCYP HLENDSYKFI PFNNLAIKAM LTAKVDKKDM DKFYDSIIYG IAPPPQFKKR YNTNDNSRGM NFETIMFTKV AMLICEALNS LKVTQANVSN VLSRVVSIRH LENLVIRKEN PQDILFHSKD LLLKSTLIAI GQSKEIETTI TAEGGEIVFQ NAAFTMWKLT YLEHQLMPIL DQNFIEYKVT LNEDKPISDV HVKELVAELR WQYNKFAVIT HGKGHYRIVK YSSVANHADR VYATFKSNVK TGVNNDFNLL DQRIIWQNWY AFTSSMKQGN TLDVCKRLLF QKMKPEKNPF KGLSTDRKMD EVSQVGV //