VP3_BAVJK
ID VP3_BAVJK Reviewed; 720 AA.
AC Q9INI4;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Viral guanylyltransferase VP3;
DE AltName: Full=Virion protein 3;
DE Short=VP3;
DE Includes:
DE RecName: Full=mRNA guanylyltransferase;
DE EC=2.7.7.50 {ECO:0000269|PubMed:15784908};
DE Includes:
DE RecName: Full=mRNA (guanine-N(7))-methyltransferase;
DE EC=2.1.1.56 {ECO:0000305|PubMed:15784908};
GN Name=Segment-3; Synonyms=S3;
OS Banna virus (strain Indonesia/JKT-6423/1980) (BAV).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Seadornavirus.
OX NCBI_TaxID=649604;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=182211; Culex annulus.
OH NCBI_TaxID=7178; Culex tritaeniorhynchus (Mosquito).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10811934; DOI=10.1099/0022-1317-81-6-1507;
RA Attoui H., Billoir F., Biagini P., de Micco P., de Lamballerie X.;
RT "Complete sequence determination and genetic analysis of Banna virus and
RT Kadipiro virus: proposal for assignment to a new genus (Seadornavirus)
RT within the family Reoviridae.";
RL J. Gen. Virol. 81:1507-1515(2000).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15784908; DOI=10.1099/vir.0.80579-0;
RA Mohd Jaafar F., Attoui H., Mertens P.P., de Micco P., de Lamballerie X.;
RT "Identification and functional analysis of VP3, the guanylyltransferase of
RT Banna virus (genus Seadornavirus, family Reoviridae).";
RL J. Gen. Virol. 86:1141-1146(2005).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=15784909; DOI=10.1099/vir.0.80578-0;
RA Mohd Jaafar F., Attoui H., Mertens P.P., de Micco P., de Lamballerie X.;
RT "Structural organization of an encephalitic human isolate of Banna virus
RT (genus Seadornavirus, family Reoviridae).";
RL J. Gen. Virol. 86:1147-1157(2005).
CC -!- FUNCTION: Outer capsid protein involved in mRNA capping. Catalyzes the
CC last 3 enzymatic activities for formation of the 5' cap structure on
CC the viral plus-strand transcripts, namely the RNA guanylyltransferase,
CC RNA-7N- and RNA-2'O-methyltransferase activities.
CC {ECO:0000269|PubMed:15784908}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-
CC end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate;
CC Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50;
CC Evidence={ECO:0000269|PubMed:15784908};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA +
CC S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-
CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-
CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461,
CC ChEBI:CHEBI:167617; EC=2.1.1.56;
CC Evidence={ECO:0000305|PubMed:15784908};
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:15784909}.
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DR EMBL; AF134515; AAF78856.1; -; Genomic_RNA.
DR RefSeq; NP_694476.1; NC_004218.1.
DR PRIDE; Q9INI4; -.
DR GeneID; 995349; -.
DR KEGG; vg:995349; -.
DR BRENDA; 2.7.7.50; 8007.
DR Proteomes; UP000000832; Genome.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:UniProtKB-EC.
DR InterPro; IPR026379; Seadorna_VP3.
DR TIGRFAMs; TIGR04232; seadorna_VP3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Capsid protein; GTP-binding; Methyltransferase; mRNA capping;
KW mRNA processing; Multifunctional enzyme; Nucleotide-binding;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Virion.
FT CHAIN 1..720
FT /note="Viral guanylyltransferase VP3"
FT /id="PRO_0000404239"
SQ SEQUENCE 720 AA; 82120 MW; 3584EEEA74EDCD66 CRC64;
MELFSDSGSI VENFKERINK LVFDYSLNHG GFRKTYKIQR DRVYYMLGDA HHANLSGKCL
MLYNSEKDIF EGLGFKVKGS RINVSKTQIL RNYEINFETI IGVEPNGLKT ISTAKDVKKL
YDIYSYKSSL HPFDDFMAHC INRWGMSIPA SLERIIKSEI IKVRSGVLNR NSELYNYIPT
VDASFSEMSR GPANVILTDG KLVPDGTCFG PILSKSVEDP RLKNEFRSKG LIMVHDYFIL
IGESPGPHYK KYTKMTKDNT IFWDPRRTDH KFNNVVSYFK KENIRDVVEY TTDALNRGLK
PLVLIDIRKD KPKNLNTPEG AIEWERMVHD DNNLIIDMVN ALDKRVTVCA KLRPAFMQVG
SMRKLLRPVR ILPLPYLRRS TAEFNMFVPN EALMNGNEIY DVTYDDLVRM SSEVFVLKNI
IGGLYNMYLK DMHLNLGVVN KSVSLSDGSS AIWSLSNINN ERISNFNFNN FLYAAPYSDF
ATSSVKRHFK GRNYSDWCLN ILDEVNLKDG VYLVPLYAIV GGGQITSHDF VNAIITDQEQ
LIDFTQSERA LSTQVVKLVS FILKDSFTAK GLNWTEIDNE IRNRRLSSLS GVGFTVTKML
DGKVLVDGKV VTVSGHMLYI LLGSILGLPY GIKKYLKEIE LNILKPGSSY ERGVGGRVWH
GLISHYLAVD CVIDVIDEYM VCTYEDRSKL NVVLRYVKSK LLELGSKYDV YLSVDERLVL