ID A0A024CFD6_9REOV Unreviewed; 835 AA. AC A0A024CFD6; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 11-NOV-2015, entry version 6. DE RecName: Full=Protein VP3 {ECO:0000256|PIRNR:PIRNR004015}; GN Name=VP3 {ECO:0000313|EMBL:AHZ32439.1}; GN ORFNames=L312_46714gpVP3 {ECO:0000313|EMBL:AHZ32439.1}; OS Rotavirus A. OC Viruses; dsRNA viruses; Reoviridae; Sedoreovirinae; Rotavirus. OX NCBI_TaxID=28875 {ECO:0000313|EMBL:AHZ32439.1}; RN [1] {ECO:0000313|EMBL:AHZ32439.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=RVA/Human-wt/ZAF/MRC-DPRU566/2003/G1P[8] RC {ECO:0000313|EMBL:AHZ32439.1}; RA Wentworth D.E., Halpin R.A., Stucker K.M., Akopov A., Fedorova N., RA Tsitrin T., Puri V., Stockwell T., Amedeo P., Bishop B., Gupta N., RA Hoover J., Katzel D., Schobel S., Shrivastava S., Nyaga M.M., RA Magagula N.B., Peenze I., Seheri M.L., Mphahlele J., Steele A.D., RA Mwenda M.J.; RL Submitted (APR-2014) 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; KJ751682; AHZ32439.1; -; 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; 97722 MW; 22DFA71399ABCB64 CRC64; MKVLALRHSV AQVYADTQTY LHDDLKDEYE NAFLISNLTT HNILYLNYSL KTLKILNKSG IAAVEVQSPD ELFALIRCNF TYDYENNIVY LHDYSYYTNN EIRTDQHWIT KTDMIDYLLP GWKLTYVGYN GKNTRGHYNF SFICQNAATD DDIIIEYIYS NELDFQNFLL RKIKERMTTS LPIARLSNRV FRDKLFPSIV NIHKKVINVG PRNESMFTFL NFPTIKQFSN GAYIVKHTIK LKQEKWLGKR VSQFDIGQYK NMLNVVTTIY YYYNLYYSKP IIYMLGSAPS YWIYDIKQYS DFTFETWDPL DTPYSTTHHK ELFFDKDVNK LKDNSVLYID IRTDRGSMDW KEWRKIVEQQ TVSNLNIAYK YLSTGKAKVC CVKLTAMDLE LPITAKLLHH PTTEVRSEFY AILDVWDIIT IKRFIPKGVF YAFINNVTTE NVFIQPPFKL KTSPTDYIVA LYALSNDFNS RQDVINLVNK QKQSLITVRI NNTFKDEPKV NFKNIYDWTF LPTDFELKDS IITSYDGCLG VFGLSISLPS KPTGNNHLFI INGTDKYNKL DQYANHMGIS RRSHQIRFSE SATSYSGYIF RDLSNNNFNL IGTNVENSVS GHVYNALIYY RYNYAFDLKR WIYLHSIGKV AIEGGRYYEH APIELIYACR SAKEFAILQD DLTVLRYANE IEGYINKVYS ITYADDPNYF IGIKFNSIPY EYDVKIPHLT LGVLFISENM INDVITVLKK MKTELFKMEI STSYTYMLSD NTYVANASGV LSTYFKLYNM FYRNHITFGQ SRMFIPHITL SFSNKQTVRI ESTKLKISSI YLRKIKGETV FDMSE //