ID   A0A221IRJ8_9REOV        Unreviewed;       835 AA.
AC   A0A221IRJ8;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   05-JUN-2019, entry version 5.
DE   RecName: Full=Protein VP3 {ECO:0000256|PIRNR:PIRNR004015};
GN   Name=VP3 {ECO:0000313|EMBL:ASM56484.1};
OS   Rotavirus A.
OC   Viruses; Riboviria; Reoviridae; Sedoreovirinae; Rotavirus.
OX   NCBI_TaxID=28875 {ECO:0000313|EMBL:ASM56484.1, ECO:0000313|Proteomes:UP000225826};
RN   [1] {ECO:0000313|EMBL:ASM56484.1, ECO:0000313|Proteomes:UP000225826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RVA/Human-wt/UGA/MUL-13-166/2013/G3P[6]
RC   {ECO:0000313|EMBL:ASM56484.1, ECO:0000313|Proteomes:UP000225826};
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}.
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DR   EMBL; KX632278; ASM56484.1; -; mRNA.
DR   Proteomes; UP000225826; Genome.
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   Complete proteome {ECO:0000313|Proteomes:UP000225826};
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
//