ID G9L887_9REOV Unreviewed; 835 AA. AC G9L887; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 11-NOV-2015, entry version 9. DE RecName: Full=Protein VP3 {ECO:0000256|PIRNR:PIRNR004015}; OS Lamb rotavirus. OC Viruses; dsRNA viruses; Reoviridae; Sedoreovirinae; Rotavirus; OC Rotavirus A. OX NCBI_TaxID=28326 {ECO:0000313|EMBL:AEV53328.1}; RN [1] {ECO:0000313|EMBL:AEV53328.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=LLR {ECO:0000313|EMBL:AEV53328.1}; RA Zhao Y., Feng D., Liu C., Wei R., Gao X., Zhu L.; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. 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; JQ013504; AEV53328.1; -; Genomic_RNA. DR GO; GO:0019013; C:viral nucleocapsid; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. 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-KW. DR GO; GO:0016032; P:viral process; IEA:InterPro. 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 3: Inferred from homology; 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; 98068 MW; B428F0DA3427C779 CRC64; MKVLALRHSV ARVYADTQVY THDDSKDDYE NAFLISNLTT HNILYLNYSI KTLQILNKSG IAAIEIQKMD ELFTLIRCNF TYDYIDDIVY LHDYSYYTNN EIRTDQHWVT KTNIEDYLLP GWKLTYVGYN GSGTRGHYNF SFKCQNAATD DDAIIEYIYS DELDFQNFIL KKIKERMTTS LPIARLSNRV FRDKLFKILL VNHNKVINVG PRNESMFTFL DYPSIKQFSN GPYLVKDTIK LKQERWLGKR LSQFDIGQYK NMLNVLTTLY QYYDMYHDKP IIYMVGSAPS YWIYDVKQYS NLKFETWDPL DTPYSDLHHK ELFYINDVLK LKDNSILYVD IRTDRENMNW KEWRKVVEEQ TISNLNIAYK YLSTGKAKIC CVKMTAMDLE LPISAKLLHH PTTEIRSEFY LIMDIWDSRN IKRFIPKGVL YSYVNNIITE NVFIQQPFKL KTLKNEYIVA LYALSNDFNN RENVIKLINN QKKALITVRI NNTFKDEPKV GFKNIYDWTF LPTDFETNES IVTSYDGCLG VFGLSISLAS KPTGNNHLFI LSGTDKYFKL DQFANHMSIS RRSHQIRFSE SATSYSGYIF RDLSNNNFNL IGTNVENSVS GHVYNALIYY RYNYSFDLKR WIYLHSTGKA SIEGGRYYEH APIELMYACR SAREFAKLQD DLTVLRYSNE IEDYINKVYS ITYADDPNYF IGIKFKSIPY KYDVKVPHLT FGVLNVSEPI LPDVIAILKK FKNELFKMDI TTSYTYMLSD EVYVANVSGV LSTYFKIYNA FYKEQIAFGQ SRMFIPHITL SFNNEKTVRI DTTKLNIDSI YLRKIKGDTV FDMTE //