ID NSP2_ROTH3 Reviewed; 317 AA. AC A4ZCW3; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 29-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 51. 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/Human/Japan/AU-1/1982/G3P3[9]) (RV-A). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A. OX NCBI_TaxID=39013; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=17166908; DOI=10.1128/jvi.01622-06; RA Rahman M., Matthijnssens J., Yang X., Delbeke T., Arijs I., Taniguchi K., RA Iturriza-Gomara M., Iftekharuddin N., Azim T., Van Ranst M.; RT "Evolutionary history and global spread of the emerging G12 human RT rotaviruses."; RL J. Virol. 81:2382-2390(2007). 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; DQ490534; ABF67541.1; -; Genomic_RNA. DR SMR; A4ZCW3; -. DR Proteomes; UP000001454; 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 3: Inferred from homology; 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_0000369535" 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; 36479 MW; C4B9C8B6A6074727 CRC64; MAELACFCYP HLENDSYKFI PFNSLAIKCM LTAKVDKKDL DKFYNSIIYG IAPPPQFKKR YNTNDNSRGM NFETQMFTKV ATLICEALNS LKITQIDVAS VLSRVVSVRH LENLVLRKEN HQDILFHSKD LLIKSVLIAI GQSKEIETTA TAEGGKIVFQ NAAFTMWKLT YLDHQLMPIL DQNFIEYKVT LNEDKPISDG HVKELVAELR WQYNKFAVIT HGKGHYRVVK YSSVANHADR VYATFKNNIK SGIASDFTLL DQRIIWQNWY AFTSSMKQGN TLEVCRKLLF QKMKQEPNPF RGLSTDRKMD EVSQVGI //