MCE_ASFB7
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 03-AUG-2022, entry version 97.
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=3.1.3.33;
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.
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-(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: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 +
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; 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}.
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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 PDBsum; 7D8U; -.
DR SMR; P32094; -.
DR GeneID; 22220330; -.
DR KEGG; vg:22220330; -.
DR UniPathway; UPA00922; -.
DR Proteomes; UP000000624; Genome.
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 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; IPR033469; CYTH-like_dom_sf.
DR InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
DR InterPro; IPR039753; RG7MT1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12189; PTHR12189; 1.
DR Pfam; PF03291; Pox_MCEL; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF55154; SSF55154; 1.
DR PROSITE; PS51562; RNA_CAP0_MT; 1.
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 545..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 597..612
FT /evidence="ECO:0007829|PDB:7D8U"
FT TURN 613..616
FT /evidence="ECO:0007829|PDB:7D8U"
FT STRAND 618..624
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
