ID   A0A024CFD6_9REOV        Unreviewed;       835 AA.
AC   A0A024CFD6;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   18-JAN-2017, entry version 7.
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, ECO:0000313|Proteomes:UP000118715};
RN   [1] {ECO:0000313|EMBL:AHZ32439.1, ECO:0000313|Proteomes:UP000118715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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}.
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DR   EMBL; KJ751682; AHZ32439.1; -; Genomic_RNA.
DR   Proteomes; UP000118715; Segment 3 rna capping protein vp3 (vp3) gene.
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   Complete proteome {ECO:0000313|Proteomes:UP000118715};
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
//