ID A0A096XXZ1_9REOV Unreviewed; 317 AA. AC A0A096XXZ1; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 25-APR-2018, entry version 6. DE RecName: Full=Non-structural protein 2 {ECO:0000256|RuleBase:RU364009}; DE EC=3.6.4.- {ECO:0000256|RuleBase:RU364009}; OS Human rotavirus A. OC Viruses; dsRNA viruses; Reoviridae; Sedoreovirinae; Rotavirus; OC 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 RT an 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 CC of virus factories (viroplasms) which are large inclusions in the CC host cytoplasm where replication intermediates are assembled and CC viral RNA replication takes place. Displays ssRNA binding, NTPase, CC RNA triphosphatase (RTPase) and ATP-independent helix-unwinding CC activities. The unwinding activity may prepare and organize plus- CC strand RNAs for packaging and replication by removing interfering CC secondary structures. The RTPase activity plays a role in the CC removal of the gamma-phosphate from the rotavirus RNA minus CC strands of dsRNA genome segments. {ECO:0000256|RuleBase:RU364009}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|RuleBase:RU364009}; CC -!- SUBUNIT: Homooctamer. Interacts with VP1; this interaction is CC weak. Interacts with NSP5; this interaction leads to up-regulation CC of NSP5 phosphorylation and formation of viral factories. CC {ECO:0000256|RuleBase:RU364009}. CC -!- SUBCELLULAR LOCATION: Host cytoplasm CC {ECO:0000256|RuleBase:RU364009}. CC -!- SIMILARITY: Belongs to the rotavirus NSP2 family. CC {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:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0019079; P:viral genome replication; IEA:InterPro. DR Gene3D; 3.30.428.20; -; 1. DR Gene3D; 3.90.1400.10; -; 1. DR InterPro; IPR003668; Rotavirus_NSP2. DR InterPro; IPR024076; Rotavirus_NSP2_C-term. 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 Complete proteome {ECO:0000313|Proteomes:UP000223581}; KW Host cytoplasm {ECO:0000256|RuleBase:RU364009}; KW Hydrolase {ECO:0000256|RuleBase:RU364009}; KW Magnesium {ECO:0000256|RuleBase:RU364009}; KW Metal-binding {ECO:0000256|RuleBase:RU364009}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU364009}; KW RNA-binding {ECO:0000256|RuleBase:RU364009}. 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 //