ID A0A221IRJ8_9REOV Unreviewed; 835 AA. AC A0A221IRJ8; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 20-DEC-2017, entry version 3. DE RecName: Full=Protein VP3 {ECO:0000256|PIRNR:PIRNR004015}; GN Name=VP3 {ECO:0000313|EMBL:ASM56484.1}; OS Rotavirus A. OC Viruses; dsRNA viruses; Reoviridae; Sedoreovirinae; Rotavirus. OX NCBI_TaxID=28875 {ECO:0000313|EMBL:ASM56484.1}; RN [1] {ECO:0000313|EMBL:ASM56484.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RVA/Human-wt/UGA/MUL-13-166/2013/G3P[6] RC {ECO:0000313|EMBL:ASM56484.1}; RX PubMed=28640820; RA Bwogi J., Jere K.C., Karamagi C., Byarugaba D.K., Namuwulya P., RA Baliraine F.N., Desselberger U., Iturriza-Gomara M.; RT "Whole genome analysis of selected human and animal rotaviruses RT identified in Uganda from 2012 to 2014 reveals complex genome RT reassortment events between human, bovine, caprine and porcine RT strains."; RL PLoS ONE 12:E0178855-E0178855(2017). CC -!- FUNCTION: Multifunctional enzyme involved in mRNA capping. CC Catalyzes the formation of the 5' cap structure on the viral plus- CC strand transcripts. Specifically binds to GTP and displays CC guanylyltransferase and methyltransferase activities. CC {ECO:0000256|PIRNR:PIRNR004015}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|PIRNR:PIRNR004015}. CC -!- SIMILARITY: Belongs to the rotavirus VP3 family. CC {ECO:0000256|PIRNR:PIRNR004015}. 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; KX632278; ASM56484.1; -; mRNA. DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-UniRule. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-UniRule. DR InterPro; IPR011181; VP3_Rotav. DR Pfam; PF06929; Rotavirus_VP3; 1. DR PIRSF; PIRSF004015; LigT_rotavirus; 1. DR PROSITE; PS51589; SAM_MT56_VP3; 1. PE 2: Evidence at transcript level; KW GTP-binding {ECO:0000256|PIRNR:PIRNR004015}; KW Methyltransferase {ECO:0000256|PIRNR:PIRNR004015}; KW mRNA capping {ECO:0000256|PIRNR:PIRNR004015}; KW mRNA processing {ECO:0000256|PIRNR:PIRNR004015}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR004015}; KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR004015}; KW RNA-binding {ECO:0000256|PIRNR:PIRNR004015}; KW S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR004015}; KW Transferase {ECO:0000256|PIRNR:PIRNR004015}; KW Virion {ECO:0000256|PIRNR:PIRNR004015}. SQ SEQUENCE 835 AA; 98225 MW; AA5E18234705DD20 CRC64; MKVLALRHSV AQVYADTQMY THDDSKDEYE NAFLISNLTT HNILYFNYNV KTLQILNKSG IAAIEIQEID ELFTLIRCNF TYDYIENVVY LHDYSYYTNN EIRTDQHWIT KTNIEDYLLP GWKLTYVGYN GSDTRGHYNF SFRCQNAATD DDAIIEYIYS DELDFQSFIL KKIKERMTTS LPIARLSNRV FRDKLFETVS VNHDKVVNIG PRNESMFTFL DYPSIKQFSN GPYLVKDTIK LKQERWLGKR LSQFDIGQYK NMLNVLTTLY QYYDIYHEKP IVYMIGSAPS YWIYDVKQYS NLKFETWDPL DTPYSNLHHK ELFYINDVQK LKDNSILYID IRTDRGTVDW KEWRKIVERQ TIDNLHIAYK YLSTGKAKVC CVKMTAMDLE LPISAKLLHH PTTEIRSEFY LVMDIWDSKN IKRFIPKGVL YSYINNIITE NVFIQQPFKL KTLKNEYIIA LYALSNDLNN REDVVKLINN QKKALMTVRI NNTFKDEPKV GFKNIYDWTF LPTDFETNES IITSYDGCLG IFGLSISLAS KPTGNNHLFI LSGTDKYFKL DQFANHMSIS RRSHQIRFSE SATSYSGYIF RDLSNNNFNL IGTNVENSVS GHVYNALIYY RYNYSFDLKR WIYLHSTGKA SIEGGKYYEH APIELIYACR SAREFAKLQD DLTVLRYSNE IENYINKVYS ITYADDPNYF IGVKFKNIPY KYNVKVPHLT FGVLNISEQM LSDVITILKR FKNELFRMEI TTSYTYMLSD EVYVANISGV LSTYFKMYNA FYKEQITFGQ SRMFIPHVTL SFSNEKTVRI DTTKLYIDSI YLRKIKGDTV FDMTG //