ID A0A096XXZ1_9REOV Unreviewed; 317 AA. AC A0A096XXZ1; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 29-SEP-2021, entry version 14. DE RecName: Full=Non-structural protein 2 {ECO:0000256|HAMAP-Rule:MF_04089}; DE Short=NSP2 {ECO:0000256|HAMAP-Rule:MF_04089}; DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_04089}; DE AltName: Full=NCVP3 {ECO:0000256|HAMAP-Rule:MF_04089}; DE AltName: Full=Non-structural RNA-binding protein 35 {ECO:0000256|HAMAP-Rule:MF_04089}; DE Short=NS35 {ECO:0000256|HAMAP-Rule:MF_04089}; OS Human rotavirus A. OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A. OX NCBI_TaxID=10941 {ECO:0000313|EMBL:AIL82720.1, ECO:0000313|Proteomes:UP000223581}; RN [1] {ECO:0000313|EMBL:AIL82720.1, ECO:0000313|Proteomes:UP000223581} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RVA/Human-wt/HUN/ERN5611/2012/G1P8 RC {ECO:0000313|EMBL:AIL82720.1, ECO:0000313|Proteomes:UP000223581}; RX PubMed=25239526; DOI=10.1016/j.meegid.2014.09.016; RA Doro R., Mihalov-Kovacs E., Marton S., Laszlo B., Deak J., Jakab F., RA Juhasz A., Kisfali P., Martella V., Melegh B., Molnar P., Santha I., RA Schneider F., Banyai K.; RT "Large-scale whole genome sequencing identifies country-wide spread of an RT emerging G9P[8] rotavirus strain in Hungary, 2012."; RL Infect. Genet. Evol. 28:495-512(2014). 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:0000256|HAMAP-Rule:MF_04089, ECO:0000256|RuleBase:RU364009}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_04089, CC ECO:0000256|RuleBase:RU364009}; 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:0000256|HAMAP- CC Rule:MF_04089, ECO:0000256|RuleBase:RU364009}. CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_04089}. CC -!- SIMILARITY: Belongs to the rotavirus NSP2 family. {ECO:0000256|HAMAP- CC Rule:MF_04089, ECO:0000256|RuleBase:RU364009}. 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; KJ918968; AIL82720.1; -; Genomic_RNA. DR Proteomes; UP000223581; 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: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 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_04089}; KW Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04089, KW ECO:0000256|RuleBase:RU364009}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04089, ECO:0000256|RuleBase:RU364009}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_04089, ECO:0000256|RuleBase:RU364009}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_04089, KW ECO:0000256|RuleBase:RU364009}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04089, KW ECO:0000256|RuleBase:RU364009}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_04089, KW ECO:0000256|RuleBase:RU364009}. FT NP_BIND 107..109 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04089" FT NP_BIND 221..223 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04089" FT REGION 205..241 FT /note="RNA-binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04089" FT ACT_SITE 225 FT /note="For NTPase and RTPase activities" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04089" FT BINDING 188 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04089" FT BINDING 227 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04089" SQ SEQUENCE 317 AA; 36601 MW; A809051751AB0BB2 CRC64; MAELACFCYP HLENDSYKFI PFNNLAIKCM LTAKVEKKDQ DKFYNSIIYG IAPPPQFKKR YNTNDNSRGM NYETAMFNKV AVLICEALNS IKVTQSDVAS VLSRVVSVRH LENLVLRREN HQDVLFHSKE LLLKSVLIAI GYSKEIETTA TAEGGEIVFQ NVAFTMWKLT YLEHKLMPIL DQNFIEYKIT VNEDKPISES HVKELIAELR WQYNKFAVIT HGKGHYRVVK YSSVANHADR VYATFKSNNK NGGPLEFNLL DQRIIWQNWY AFTSSMKQGN TLDVCKKLLF QKMKRESNPF KGLSTDRKMD EVSQVGI //