ID   A0A1L3IZK0_9POXV        Unreviewed;       840 AA.
AC   A0A1L3IZK0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=mRNA-capping enzyme catalytic subunit {ECO:0000256|ARBA:ARBA00020120};
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=Virus termination factor large subunit {ECO:0000256|ARBA:ARBA00033397};
DE   AltName: Full=mRNA-capping enzyme 97 kDa subunit {ECO:0000256|ARBA:ARBA00030246};
DE   AltName: Full=mRNA-capping enzyme large subunit {ECO:0000256|ARBA:ARBA00033175};
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   -!- FUNCTION: Catalytic subunit of the mRNA capping enzyme which catalyzes
CC       three enzymatic reactions: the 5' triphosphate end of the pre-mRNA is
CC       hydrolyzed to a diphosphate by RNA 5' triphosphatase; the diphosphate
CC       RNA end is capped with GMP by RNA guanylyltransferase and the GpppN cap
CC       is methylated by RNA (guanine-N7) methyltransferase. Heterodimeric mRNA
CC       capping enzyme catalyzes the linkage of a N7-methyl-guanosine moiety to
CC       the first transcribed nucleotide (cap 0 structure), whereas the
CC       polymerase associated VP39 is responsible for a second methylation at
CC       the 2'-O position of the ribose (cap 1 structure).
CC       {ECO:0000256|ARBA:ARBA00024926}.
CC   -!- FUNCTION: The heterodimeric enzyme is also involved in early viral gene
CC       transcription termination and intermediate viral gene transcription
CC       initiation. Early gene transcription termination requires the
CC       termination factor VTF, the DNA-dependent ATPase NPH-I and the Rap94
CC       subunit of the viral RNA polymerase, as well as the presence of a
CC       specific termination motif. Binds, together with RAP94, to the
CC       termination motif 5'-UUUUUNU-3' in the nascent early mRNA.
CC       {ECO:0000256|ARBA:ARBA00025126}.
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:0000256|ARBA:ARBA00024268};
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   -!- SUBUNIT: Heterodimer of a catalytic and a regulatory subunit. Intrinsic
CC       methyltransferase activity of the catalytic subunit is weak and needs
CC       to be stimulated 30- to 50-fold by the regulatory subunit, which is
CC       itself catalytically inert. {ECO:0000256|ARBA:ARBA00025807}.
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   Gene3D; 3.40.50.150; -; 1.
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
//