ID   A0A1L3IZK0_9POXV        Unreviewed;       840 AA.
AC   A0A1L3IZK0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   07-APR-2021, entry version 19.
DE   RecName: Full=GTP--RNA guanylyltransferase {ECO:0000256|ARBA:ARBA00018051};
DE            EC=2.1.1.56 {ECO:0000256|ARBA:ARBA00011926};
DE            EC=2.7.7.50 {ECO:0000256|ARBA:ARBA00012475};
DE            EC=3.1.3.33 {ECO:0000256|ARBA:ARBA00013054};
DE   AltName: Full=Polynucleotide 5'-triphosphatase {ECO:0000256|ARBA:ARBA00013957};
DE   AltName: Full=Virus termination factor large subunit {ECO:0000256|ARBA:ARBA00015255};
DE   AltName: Full=mRNA 5'-triphosphatase {ECO:0000256|ARBA:ARBA00018500};
DE   AltName: Full=mRNA guanylyltransferase {ECO:0000256|ARBA:ARBA00016289};
DE   AltName: Full=mRNA-capping enzyme 97 kDa subunit {ECO:0000256|ARBA:ARBA00013716};
DE   AltName: Full=mRNA-capping enzyme catalytic subunit {ECO:0000256|ARBA:ARBA00020120};
DE   AltName: Full=mRNA-capping enzyme large subunit {ECO:0000256|ARBA:ARBA00021441};
GN   ORFNames=BAV00115 {ECO:0000313|EMBL:APG58298.1};
OS   BeAn 58058 virus.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; unclassified Chordopoxvirinae.
OX   NCBI_TaxID=67082 {ECO:0000313|EMBL:APG58298.1, ECO:0000313|Proteomes:UP000202017};
RN   [1] {ECO:0000313|EMBL:APG58298.1, ECO:0000313|Proteomes:UP000202017}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BeAn58058 {ECO:0000313|EMBL:APG58298.1,
RC   ECO:0000313|Proteomes:UP000202017};
RA   Wanzeller A.L.M., Souza A.L.P., Azevedo R.S.S., Junior E.C.S.,
RA   Filho L.C.F., Oliveira R.S., Lemos P.S., Junior J.V., Vasconcelos P.F.C.;
RT   "The Complete Genome Sequence of BeAn58058 Virus Isolated from Oryzomys sp.
RT   Rodents in Amazon Region-Brazll.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end diphospho-(purine-ribonucleoside) in mRNA + GTP +
CC         H(+) = a 5'-end (5'-triphosphoguanosine)-(purine-ribonucleoside) in
CC         mRNA + diphosphate; Xref=Rhea:RHEA:54592, Rhea:RHEA-COMP:13407,
CC         Rhea:RHEA-COMP:13929, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:136896, ChEBI:CHEBI:138276;
CC         EC=2.7.7.50; Evidence={ECO:0000256|ARBA:ARBA00023697};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end triphospho-(purine-ribonucleoside) in mRNA + H2O = a
CC         5'-end diphospho-(purine-ribonucleoside) in mRNA + H(+) + phosphate;
CC         Xref=Rhea:RHEA:11008, Rhea:RHEA-COMP:13929, Rhea:RHEA-COMP:13942,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:138276, ChEBI:CHEBI:138288; EC=3.1.3.33;
CC         Evidence={ECO:0000256|ARBA:ARBA00023738};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: In the N-terminal section; belongs to the dsDNA virus mRNA
CC       guanylyltransferase family. {ECO:0000256|ARBA:ARBA00008556}.
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DR   EMBL; KY094066; APG58298.1; -; Genomic_DNA.
DR   RefSeq; YP_009329713.1; NC_032111.1.
DR   GeneID; 30524354; -.
DR   KEGG; vg:30524354; -.
DR   Proteomes; UP000202017; Genome.
DR   GO; GO:0046872; F:metal ion 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   GO; GO:0004651; F:polynucleotide 5'-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR019602; mRNA_cap_ATPase/GuylTrfase_vir.
DR   InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
DR   InterPro; IPR039753; RG7MT1.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   PANTHER; PTHR12189; PTHR12189; 1.
DR   Pfam; PF10640; Pox_ATPase-GT; 1.
DR   Pfam; PF03291; Pox_MCEL; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51562; RNA_CAP0_MT; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000202017};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          513..840
FT                   /note="MRNA cap 0 methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51562"
SQ   SEQUENCE   840 AA;  98315 MW;  DAB9B1EF3EB70FB5 CRC64;
     MEDNNIFTNS VEGYINELIK IYKGIKPQLP IDDIYDEVEA IIINPPLITL TNVFNISTKV
     ESYILFTVTN KEDGLKLRSR LDMSNVNGLD IKNVQLVDSI ESIIWEKKKL IYEQKIDEFC
     IIRHSTEEKY IFLDFKKFNS SIKIEFVNLV QAKIKNILVD FKIKYFLGSG AQGKSSLLHV
     LNYPKCKPNM TLEFEIIQKD TPIDEKELYN ELITICRNIF MGYPKNIFLK RECGYPIRTH
     MLKKQDINSI SLDDLYITNK TDGIGTFISI LKDGIYCYFS HLNYTIRYDV NKKVDNPIKL
     YGEGLKYDGK WSIYLIKLVT PEFNDRFKEK EFVTNELSNI SNRIQFKTKK YEGPFTTHSE
     LIDKLISYLP NQQEGVVLFY KSNDKAIDYK IKNDNTTDHM INAIYRYMSS EPVIFGEDNT
     FIEYKKFSDE KGFPKEFGNG KLILSDNLKY LNNIYCIEFC NIYNSVGLNN VIVPIKFISE
     FSSNGNFLKP RIDKTAKYIK CDYYGNQHTV VLEHIMDQQL NIADIFDDTK LSNIGQKYSI
     EKNRLNPDIS YFTNKRTRGP LGILSNYIKT LLISLYCSKT FLDNSNKRKV LAVDFGNGAD
     LQKYFYGEIS LLVASDPDQD AINRCLERYN KLNAGIKSKY YKFDYVNDTI RSESYVSNIR
     KVFFFGKFEI VDWQFAIHYS FHKKYYSVVM KNLSELTTSG GKVLITTMDG DKLSEITGIK
     KFIINKNLPE SENYMSVEKI SDETILVYNP SSMSKPMEEY IIKYKDITRI FAEYGFELID
     YVHFNTVIDR SHRFINNVSK MEQRESTKNF FDLNREVLRD NIEDINELLK YYVIYVFSKR
//