ID NSP2_ROTHK Reviewed; 317 AA. AC Q9QNA8; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 67. 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/KU/1995/G1P1A[8]) (RV-A). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A. OX NCBI_TaxID=10952; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Taniguchi K.; RT "Rotavirus."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP FUNCTION, INTERACTION WITH HOST DCP1A, INTERACTION WITH HOST DCP1B, RP INTERACTION WITH HOST DDX6, INTERACTION WITH HOST EDC4, AND INTERACTION RP WITH HOST EIF2S1. RX PubMed=30258011; DOI=10.1128/jvi.01363-18; RA Dhillon P., Rao C.D.; RT "Rotavirus Induces Formation of Remodeled Stress Granules and P Bodies and RT Their Sequestration in Viroplasms To Promote Progeny Virus Production."; RL J. Virol. 92:0-0(2018). 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 (By CC similarity). Participates in the selective exclusion of host proteins CC from stress granules (SG) and P bodies (PB) (PubMed:30258011). CC Participates also in the sequestration of these remodeled organelles in CC viral factories (PubMed:30258011). {ECO:0000255|HAMAP-Rule:MF_04089, CC ECO:0000269|PubMed:30258011}. 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 ECO:0000269|PubMed:30258011}. 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; AB022770; BAA84967.1; -; mRNA. DR SMR; Q9QNA8; -. DR Proteomes; UP000001458; 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 ATP-binding; Host cytoplasm; Host-virus interaction; Hydrolase; Magnesium; KW Metal-binding; Nucleotide-binding; RNA-binding. FT CHAIN 1..317 FT /note="Non-structural protein 2" FT /id="PRO_0000369536" 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; 36719 MW; 444FC34DBD50A9E4 CRC64; MAELACFCYP HLENDSYKFI PFNNLAIKCM LTAKVDKKDQ DKFYNSIIYG IAPPPQFKKR YNTNDNSRGM NYETPMLIKV AILICEALNS IKVTQSDVAN VLSRVVSVRH LENLVLRKEN HQDVLFHSKE LLLKSVLIAI GQSKEIETTA TAEGGEIVFQ NVAFTMWKLT YLDHKLMPIL DQNFIEYKIT MNEDKPISDV HVKELIAELR WQYNRFAVIT HGKGHYRVVK YSSVANHADR VFATYKNNAK SGNVIDFNLL DQRIIWQNWY AFTSSMKQGF TLDVCKKLLF QKMKQERNPF KGLSTDRKMD EVSRIGI //