ID NSP2_ROTHC Reviewed; 312 AA. AC Q9PY93; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 86. 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 C (isolate RVC/Human/United Kingdom/Bristol/1989) (RV-C). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Sedoreoviridae; Rotavirus; Rotavirus C. OX NCBI_TaxID=31567; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=10567650; DOI=10.1099/0022-1317-80-12-3181; RA James V.L., Lambden P.R., Deng Y., Caul E.O., Clarke I.N.; RT "Molecular characterization of human group C rotavirus genes 6, 7 and 9."; RL J. Gen. Virol. 80:3181-3187(1999). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND MUTAGENESIS OF LYS-185 AND RP HIS-222. RX PubMed=16873255; DOI=10.1128/jvi.00172-06; RA Taraporewala Z.F., Jiang X., Vasquez-Del Carpio R., Jayaram H., RA Prasad B.V.V., Patton J.T.; RT "Structure-function analysis of rotavirus NSP2 octamer by using a novel RT complementation system."; RL J. Virol. 80:7984-7994(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 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}. 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; AJ132205; CAB52753.1; -; Genomic_RNA. DR RefSeq; YP_392488.1; NC_007545.1. DR PDB; 2GU0; X-ray; 2.80 A; A/B=1-312. DR PDBsum; 2GU0; -. DR SMR; Q9PY93; -. DR GeneID; 3773135; -. DR KEGG; vg:3773135; -. DR EvolutionaryTrace; Q9PY93; -. DR Proteomes; UP000007664; 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; Hydrolase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome; RNA-binding. FT CHAIN 1..312 FT /note="Non-structural protein 2" FT /id="PRO_0000367815" FT REGION 202..238 FT /note="RNA-binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04089" FT ACT_SITE 222 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 185 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04089" FT BINDING 218..220 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04089" FT BINDING 224 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04089" FT MUTAGEN 185 FT /note="K->A: Loss of NTPase activity and dsRNA synthesis. FT No effect on octamerization." FT /evidence="ECO:0000269|PubMed:16873255" FT MUTAGEN 222 FT /note="H->A: Loss of NTPase activity and dsRNA synthesis. FT No effect on octamerization." FT /evidence="ECO:0000269|PubMed:16873255" FT HELIX 4..6 FT /evidence="ECO:0007829|PDB:2GU0" FT STRAND 8..11 FT /evidence="ECO:0007829|PDB:2GU0" FT STRAND 13..16 FT /evidence="ECO:0007829|PDB:2GU0" FT STRAND 18..21 FT /evidence="ECO:0007829|PDB:2GU0" FT HELIX 24..32 FT /evidence="ECO:0007829|PDB:2GU0" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:2GU0" FT STRAND 47..49 FT /evidence="ECO:0007829|PDB:2GU0" FT HELIX 55..60 FT /evidence="ECO:0007829|PDB:2GU0" FT HELIX 74..90 FT /evidence="ECO:0007829|PDB:2GU0" FT HELIX 94..96 FT /evidence="ECO:0007829|PDB:2GU0" FT HELIX 99..103 FT /evidence="ECO:0007829|PDB:2GU0" FT HELIX 108..119 FT /evidence="ECO:0007829|PDB:2GU0" FT HELIX 124..126 FT /evidence="ECO:0007829|PDB:2GU0" FT HELIX 129..139 FT /evidence="ECO:0007829|PDB:2GU0" FT HELIX 149..151 FT /evidence="ECO:0007829|PDB:2GU0" FT STRAND 157..160 FT /evidence="ECO:0007829|PDB:2GU0" FT STRAND 162..170 FT /evidence="ECO:0007829|PDB:2GU0" FT STRAND 175..177 FT /evidence="ECO:0007829|PDB:2GU0" FT STRAND 182..192 FT /evidence="ECO:0007829|PDB:2GU0" FT HELIX 196..209 FT /evidence="ECO:0007829|PDB:2GU0" FT STRAND 213..216 FT /evidence="ECO:0007829|PDB:2GU0" FT STRAND 218..227 FT /evidence="ECO:0007829|PDB:2GU0" FT HELIX 228..230 FT /evidence="ECO:0007829|PDB:2GU0" FT HELIX 231..243 FT /evidence="ECO:0007829|PDB:2GU0" FT HELIX 264..275 FT /evidence="ECO:0007829|PDB:2GU0" FT HELIX 279..282 FT /evidence="ECO:0007829|PDB:2GU0" FT HELIX 285..288 FT /evidence="ECO:0007829|PDB:2GU0" FT HELIX 293..307 FT /evidence="ECO:0007829|PDB:2GU0" SQ SEQUENCE 312 AA; 35915 MW; D2E6C11B6582637F CRC64; MAELACFVSF SLTEDKVVWY PINKKAVQTM LCAKVEKDQR SNYYDTILYG VAPPPEFRNR FKTNERYGLD YESDQYTELV NLLADTLNMV SMPTEKFQFD IVKTVVQVRH LENLLCRIKD VNDILNANVK LRVKAVMIAC NLVNETETTP LTESNDIVYQ DSYFTITKLD YSNHKLLPLM ADEYKITINT KTDIPDRNQT AFAAYIRYNF NKFAAISHGK RHWRLVLHSQ LMSHAERLDR KIKSDKKHGR QFSYDDGDMA FVHPGWKTCI GQLCGGTTFE VAKTSLYSIK PSKTVRTATN KIESDLISMV GN //