MCE_ASFM2
ID MCE_ASFM2 Reviewed; 868 AA.
AC Q65216;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=mRNA-capping enzyme {ECO:0000250|UniProtKB:P32094};
DE AltName: Full=VTF/CE {ECO:0000250|UniProtKB:P32094};
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=Mal-109; ORFNames=g4R;
OS African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10500;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8021596; DOI=10.1099/0022-1317-75-7-1655;
RA Dixon L.K., Twigg S.R.F., Baylis S.A., Vydelingum S., Bristow C.,
RA Hammond J.M., Smith G.L.;
RT "Nucleotide sequence of a 55 kbp region from the right end of the genome of
RT a pathogenic African swine fever virus isolate (Malawi LIL20/1).";
RL J. Gen. Virol. 75:1655-1684(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kutish G.F., Rock D.L.;
RT "African swine fever virus genomes.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably catalyzes the second reaction in the mRNA cap
CC formation pathway (By similarity). Forms a covalent complex with GTP
CC (By similarity). {ECO:0000250|UniProtKB:P32094}.
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:P32094};
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:0000250|UniProtKB:P32094};
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:0000250|UniProtKB:P32094}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P32094}. Note=Found
CC in association with viral nucleoid. {ECO:0000250|UniProtKB:P32094}.
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC {ECO:0000305}.
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:0000250|UniProtKB:P32094}.
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; X71982; CAA50806.1; -; Genomic_DNA.
DR EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR UniPathway; UPA00922; -.
DR Proteomes; UP000000860; 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 3: Inferred from homology;
KW GTP-binding; Hydrolase; Methyltransferase; mRNA capping; mRNA processing;
KW Nucleotide-binding; Nucleotidyltransferase; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; Virion.
FT CHAIN 1..868
FT /note="mRNA-capping enzyme"
FT /id="PRO_0000373092"
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"
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"
SQ SEQUENCE 868 AA; 99937 MW; 4657BBD07E25DC62 CRC64;
MASLENLVAR YQRCFNDQSL KNSTIELEIR FQHINFLLFK TVYEALVAQE IPSTISHSIR
CIKKVHHENH CREKILPSEN LYFKKQPLMF FKFSEPASLG CKVSLAIEQP IRKFILDSSV
LVRLKNRTTF QISDLWKIEL TIVKQLMGSE VSAKLTAFKT LLFDTPEQQT AKNMMTLINP
DDEYLYEIEI EYTGKPESLT AADVIKIKNT VLTLISPNHL MLTAYHQAIE FIASHILSSE
ILLARIKSGK WGLKRLLPQV KSMTKADYMK FYPPVGYYVT DKADGIRGIA VIQDTQIYVV
ADQLYSLGTT GIEPLKPTIL DGEFMPEKKE FYGFDVIMYE GNLLTQQGFE IRIESLNKGI
KVLQAFNIKA EMKPFISLTS ADPNVLLKNF ESVFKKKTRP YAIDGLILVE PGNSYLNTNT
FKWKPTWDNT LDFLVRKCPE SLNVPEYAPK KGFSLYLLFV GISGELFKKL ALNWCPGYTK
LFPVTQRNQN YFPVQFQPSD FPLAFLYYHP DTSSFSDIDG KVLEMRCLKR EVNHVSWEIV
KIREDRQQDL KTGGYFGNDF KTAELTWLNY MDPFSFEELA KGPSGMYFAG AKTGIYRAQT
ALISFIKQEI IQKISHQSWV IDLGIGKGQD LGRYLDAGIR HLVGIDKDQT ALAELIYRKF
SHATTRQHKH ATNIYVLHQD LAEPAKEISE KVHQIYGFPK EGASSIVSNL FIHYLMKNSQ
QVENLAVLCH KLLQPGGMVW FTTMLGERVL ELLHENRIEL NEVWEARENE VVKFAIKRLF
KEDILQETGQ EIGVLLPFSN GDFYNEYLVN TAFLIKIFKH HGFSLVQMQS FKDWIPEFQT
FSKTLYKILT EADKTWTSLF GFICLRKN
