ID A0A096XXZ1_9REOV Unreviewed; 317 AA. AC A0A096XXZ1; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 15-MAR-2017, entry version 3. 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}; RN [1] {ECO:0000313|EMBL:AIL82720.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RVA/Human-wt/HUN/ERN5611/2012/G1P8 RC {ECO:0000313|EMBL:AIL82720.1}; RX PubMed=25239526; 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. 0:0-0(2014). CC -!- FUNCTION: Involved in genome replication and packaging. Plays a CC crucial role, together with NSP5, in the formation of virus CC factories (viroplasms) which are large inclusions in the cytoplasm CC where replication intermediates are assembled and RNA replication CC takes place. Displays ssRNA binding, NTPase, RNA triphosphatase CC (RTPase) and ATP-independent helix-unwinding activity activities. CC The unwiding activity may prepare and organize plus-strand RNAs CC for packaging and replication by removing interfering secondary CC structures. Unlike typical helicases, NSP2 requires neither a CC divalent cation nor a nucleotide energy source for helix CC destabilization. The RTPase activity may account for the absence CC of the 5'-terminal gamma-phosphate on the minus-strands of dsRNA CC 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 (By similarity). Interacts with VP1; this CC interaction is weak. Interacts with NSP5; this interaction leads CC to up-regulation of NSP5 hyperphosphorylation and formation of CC virus factories. {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 GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. 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 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 //