ID   MCE_ASFB7               Reviewed;         868 AA.
AC   P32094;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   02-SEP-2026, entry version 110.
DE   RecName: Full=mRNA-capping enzyme {ECO:0000303|PubMed:23041356, ECO:0000303|PubMed:32725217};
DE   AltName: Full=VTF/CE {ECO:0000303|PubMed:32725217};
DE   Includes:
DE     RecName: Full=Polynucleotide 5'-triphosphatase;
DE              EC=3.6.1.74;
DE     AltName: Full=mRNA 5'-triphosphatase;
DE              Short=TPase;
DE   Includes:
DE     RecName: Full=mRNA guanylyltransferase;
DE              EC=2.7.7.50;
DE     AltName: Full=GTP--RNA guanylyltransferase;
DE              Short=GTase;
DE   Includes:
DE     RecName: Full=mRNA (guanine-N(7))-methyltransferase;
DE              EC=2.1.1.56;
GN   OrderedLocusNames=Ba71V-101; ORFNames=NP868R;
OS   African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS   (ASFV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Asfuvirales; Asfarviridae; Asfivirus; Asfivirus haemorrhagiae;
OC   African swine fever virus.
OX   NCBI_TaxID=10498;
OH   NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=8382399; DOI=10.1006/viro.1993.1128;
RA   Pena L., Yanez R.J., Revilla Y., Vinuela E., Salas M.L.;
RT   "African swine fever virus guanylyltransferase.";
RL   Virology 193:319-328(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA   Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA   Rodriguez J.F., Vinuela E.;
RT   "Analysis of the complete nucleotide sequence of African swine fever
RT   virus.";
RL   Virology 208:249-278(1995).
RN   [3]
RP   REVIEW.
RX   PubMed=23041356; DOI=10.1016/j.virusres.2012.09.014;
RA   Rodriguez J.M., Salas M.L.;
RT   "African swine fever virus transcription.";
RL   Virus Res. 173:15-28(2013).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=30185597; DOI=10.1128/jvi.01293-18;
RA   Alejo A., Matamoros T., Guerra M., Andres G.;
RT   "A Proteomic Atlas of the African Swine Fever Virus Particle.";
RL   J. Virol. 92:0-0(2018).
RN   [5]
RP   REVIEW.
RX   PubMed=32725217; DOI=10.1042/bst20191108;
RA   Cackett G., Sykora M., Werner F.;
RT   "Transcriptome view of a killer: African swine fever virus.";
RL   Biochem. Soc. Trans. 48:1569-1581(2020).
RN   [6]
RP   INDUCTION.
RX   PubMed=32075923; DOI=10.1128/jvi.00119-20;
RA   Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J.,
RA   Dixon L., Werner F.;
RT   "The African Swine Fever Virus Transcriptome.";
RL   J. Virol. 94:0-0(2020).
CC   -!- FUNCTION: Probably catalyzes the second reaction in the mRNA cap
CC       formation pathway (Probable). Forms a covalent complex with GTP
CC       (PubMed:8382399). {ECO:0000269|PubMed:8382399,
CC       ECO:0000305|PubMed:8382399}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end
CC         diphospho-ribonucleoside in mRNA + phosphate + H(+);
CC         Xref=Rhea:RHEA:67004, Rhea:RHEA-COMP:17164, Rhea:RHEA-COMP:17165,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:167616, ChEBI:CHEBI:167618; EC=3.6.1.74;
CC         Evidence={ECO:0000250|UniProtKB:P04298};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67005;
CC         Evidence={ECO:0000250|UniProtKB:P04298};
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:8382399};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-
CC         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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU00895};
CC   -!- PATHWAY: mRNA processing; mRNA capping.
CC   -!- SUBUNIT: Part of the viral DNA-directed RNA polymerase that consists of
CC       8 polII-like subunits (RPB1, RPB2, RPB3, RPB5, RPB6, RPB7, RPB9,
CC       RPB10), a capping enzyme and a termination factor.
CC       {ECO:0000303|PubMed:32725217}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:30185597}. Note=Found
CC       in association with viral nucleoid. {ECO:0000269|PubMed:30185597}.
CC   -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC       {ECO:0000269|PubMed:32075923}.
CC   -!- DOMAIN: The N-terminus contains the mRNA 5'-triphosphatase domain, the
CC       central part contains the mRNA guanylyltransferase, and C-terminus
CC       contains the methyltransferase domain. {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the dsDNA virus mRNA
CC       guanylyltransferase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the class I-like SAM-
CC       binding methyltransferase superfamily. mRNA cap 0 methyltransferase
CC       family. {ECO:0000255|PROSITE-ProRule:PRU00895}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L07263; AAA42692.1; -; Genomic_DNA.
DR   EMBL; U18466; AAA65330.1; -; Genomic_DNA.
DR   PIR; A45391; A45391.
DR   RefSeq; NP_042794.1; NC_001659.2.
DR   PDB; 7D8U; X-ray; 2.70 A; A/B=586-868.
DR   AlphaFoldDB; P32094; -.
DR   SMR; P32094; -.
DR   GeneID; 22220330; -.
DR   KEGG; vg:22220330; -.
DR   UniPathway; UPA00922; -.
DR   Proteomes; UP000000624; Segment.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0140818; F:mRNA 5'-triphosphate monophosphatase activity; ISS:UniProtKB.
DR   GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR033469; CYTH-like_dom_sf.
DR   InterPro; IPR001339; mRNA_cap_enzyme_adenylation.
DR   InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
DR   InterPro; IPR039753; RG7MT1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR12189:SF2; MRNA CAP GUANINE-N7 METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR12189; MRNA GUANINE-7- METHYLTRANSFERASE; 1.
DR   Pfam; PF01331; mRNA_cap_enzyme; 1.
DR   Pfam; PF03291; mRNA_G-N7_MeTrfase; 1.
DR   SUPFAM; SSF55154; CYTH-like phosphatases; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51562; RNA_CAP0_MT; 1.
DR   PDBsum; 7D8U; -.
PE   1: Evidence at protein level;
KW   3D-structure; Early protein; GTP-binding; Hydrolase; Methyltransferase;
KW   mRNA capping; mRNA processing; Nucleotide-binding; Nucleotidyltransferase;
KW   Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase;
KW   Virion.
FT   CHAIN           1..868
FT                   /note="mRNA-capping enzyme"
FT                   /id="PRO_0000210132"
FT   DOMAIN          594..868
FT                   /note="mRNA cap 0 methyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT   ACT_SITE        282
FT                   /note="N6-GMP-lysine intermediate"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:8382399"
FT   BINDING         607
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT   BINDING         624
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT   BINDING         646
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT   BINDING         710..712
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT   SITE            627
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT   SITE            658
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT   SITE            713
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT   SITE            806
FT                   /note="mRNA cap binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT   STRAND          586..588
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   HELIX           589..591
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   HELIX           597..612
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   TURN            613..616
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   STRAND          618..623
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   HELIX           631..636
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   STRAND          640..647
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   HELIX           649..660
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   STRAND          673..678
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   HELIX           685..693
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   STRAND          703..710
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   HELIX           712..715
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   HELIX           719..732
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   STRAND          733..744
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   HELIX           746..755
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   STRAND          763..765
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   STRAND          775..778
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   STRAND          791..795
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   STRAND          799..801
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   STRAND          803..807
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   HELIX           811..820
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   STRAND          823..830
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   HELIX           831..834
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   HELIX           835..838
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   HELIX           843..848
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   HELIX           851..857
FT                   /evidence="ECO:0007829|PDB:7D8U"
FT   STRAND          860..867
FT                   /evidence="ECO:0007829|PDB:7D8U"
SQ   SEQUENCE   868 AA;  99969 MW;  7068ED099D38ADA2 CRC64;
     MASLDNLVAR YQRCFNDQSL KNSTIELEIR FQQINFLLFK TVYEALVAQE IPSTISHSIR
     CIKKVHHENH CREKILPSEN LYFKKQPLMF FKFSEPASLG CKVSLAIEQP IRKFILDSSV
     LVRLKNRTTF RVSELWKIEL TIVKQLMGSE VSAKLAAFKT LLFDTPEQQT TKNMMTLINP
     DDEYLYEIEI EYTGKPESLT AADVIKIKNT VLTLISPNHL MLTAYHQAIE FIASHILSSE
     ILLARIKSGK WGLKRLLPQV KSMTKADYMK FYPPVGYYVT DKADGIRGIA VIQDTQIYVV
     ADQLYSLGTT GIEPLKPTIL DGEFMPEKKE FYGFDVIMYE GNLLTQQGFE TRIESLSKGI
     KVLQAFNIKA EMKPFISLTS ADPNVLLKNF ESIFKKKTRP YSIDGIILVE PGNSYLNTNT
     FKWKPTWDNT LDFLVRKCPE SLNVPEYAPK KGFSLHLLFV GISGELFKKL ALNWCPGYTK
     LFPVTQRNQN YFPVQFQPSD FPLAFLYYHP DTSSFSNIDG KVLEMRCLKR EINYVRWEIV
     KIREDRQQDL KTGGYFGNDF KTAELTWLNY MDPFSFEELA KGPSGMYFAG AKTGIYRAQT
     ALISFIKQEI IQKISHQSWV IDLGIGKGQD LGRYLDAGVR HLVGIDKDQT ALAELVYRKF
     SHATTRQHKH ATNIYVLHQD LAEPAKEISE KVHQIYGFPK EGASSIVSNL FIHYLMKNTQ
     QVENLAVLCH KLLQPGGMVW FTTMLGEQVL ELLHENRIEL NEVWEARENE VVKFAIKRLF
     KEDILQETGQ EIGVLLPFSN GDFYNEYLVN TAFLIKIFKH HGFSLVQKQS FKDWIPEFQN
     FSKSLYKILT EADKTWTSLF GFICLRKN
//