MCEL_RFVKA
ID MCEL_RFVKA Reviewed; 836 AA.
AC P25950; Q77PC1;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=mRNA-capping enzyme catalytic subunit;
DE AltName: Full=Virus termination factor large subunit;
DE Short=VTF large subunit;
DE AltName: Full=mRNA-capping enzyme 97 kDa subunit;
DE AltName: Full=mRNA-capping enzyme large subunit;
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;
DE AltName: Full=mRNA cap methyltransferase;
GN ORFNames=D3R, s076R;
OS Rabbit fibroma virus (strain Kasza) (RFV) (Shope fibroma virus (strain
OS Kasza)).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Leporipoxvirus.
OX NCBI_TaxID=10272;
OH NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1649507; DOI=10.1016/0042-6822(91)91009-6;
RA Upton C., Stuart D., McFadden G.;
RT "Identification and DNA sequence of the large subunit of the capping enzyme
RT from Shope fibroma virus.";
RL Virology 183:773-777(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1660196; DOI=10.1016/0042-6822(91)90529-k;
RA Strayer D.S., Jerng H.H., O'Connor K.;
RT "Sequence and analysis of a portion of the genomes of Shope fibroma virus
RT and malignant rabbit fibroma virus that is important for viral replication
RT in lymphocytes.";
RL Virology 185:585-595(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10562495; DOI=10.1006/viro.1999.0002;
RA Willer D.O., McFadden G., Evans D.H.;
RT "The complete genome sequence of shope (Rabbit) fibroma virus.";
RL Virology 264:319-343(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-97.
RX PubMed=2161144; DOI=10.1016/0042-6822(90)90013-h;
RA Upton C., Opgenorth A., Traktman P., McFadden G.;
RT "Identification and DNA sequence of the Shope fibroma virus DNA
RT topoisomerase gene.";
RL Virology 176:439-447(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-836.
RX PubMed=1329373; DOI=10.1016/0168-1702(92)90104-h;
RA Strayer D.S., Jerng H.H.;
RT "Sequence and analysis of the BamHI 'D' fragment of Shope fibroma virus:
RT comparison with similar regions of related poxviruses.";
RL Virus Res. 25:117-132(1992).
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) (By similarity).
CC {ECO:0000250}.
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 (By
CC similarity). {ECO:0000250}.
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 -!- 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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P04298};
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=All the enzymes and
CC other proteins required to synthesize early mRNAs are packaged within
CC the virion core along with the DNA genome.
CC -!- DOMAIN: The N-terminus contains the triphosphatase and
CC guanylyltransferase domains, whereas the C-terminus contains the
CC methyltransferase domain. The N-terminus is involved in binding to the
CC termination motif 5'-UUUUUNU-3' in the nascent mRNA (By similarity).
CC {ECO:0000250}.
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; M63902; AAA47224.1; -; Genomic_DNA.
DR EMBL; AF170722; AAF17958.1; -; Genomic_DNA.
DR PIR; A40478; QQVZRA.
DR RefSeq; NP_051965.1; NC_001266.1.
DR SMR; P25950; -.
DR PRIDE; P25950; -.
DR GeneID; 1486919; -.
DR KEGG; vg:1486919; -.
DR Proteomes; UP000000868; 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_sf.
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; Magnesium; Metal-binding; Methyltransferase; mRNA capping;
KW mRNA processing; Multifunctional enzyme; Nucleotidyltransferase;
KW Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase;
KW Virion.
FT CHAIN 1..836
FT /note="mRNA-capping enzyme catalytic subunit"
FT /id="PRO_0000210131"
FT DOMAIN 509..836
FT /note="mRNA cap 0 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT REGION 1..532
FT /note="Triphosphatase-guanylyltransferase"
FT /evidence="ECO:0000250"
FT ACT_SITE 256
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for RNA triphosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:P04298"
FT BINDING 37
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for RNA triphosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:P04298"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for RNA triphosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:P04298"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for RNA triphosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:P04298"
FT BINDING 541..542
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 561..562
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 565
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 590
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 612
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 670..672
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 74
FT /note="Essential for RNA triphosphatase activity"
FT /evidence="ECO:0000250"
FT SITE 104
FT /note="Essential for RNA triphosphatase activity"
FT /evidence="ECO:0000250"
FT SITE 123
FT /note="Essential for RNA triphosphatase activity"
FT /evidence="ECO:0000250"
FT SITE 156
FT /note="Essential for RNA triphosphatase activity"
FT /evidence="ECO:0000250"
FT SITE 158
FT /note="Essential for RNA triphosphatase activity"
FT /evidence="ECO:0000250"
FT SITE 599
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 624
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 674
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 755
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 828
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
SQ SEQUENCE 836 AA; 97018 MW; 7375FDA548AE1730 CRC64;
MDDSKKKRGT DYIEELILLY EDVPNPVQTD DMNHEVELTF IQPPVITLST LLPFATSQES
YILFTVTNKG VKIRNRINLS KIHGLDLKNI QLVDSIDNII WEKKTLVKEH KIDSVALVKY
STEEKYIFLD YKKYLSAIKL ELVNVVQVKV KHVTVDFKFK YFLGSGAQAK SSLLHVLNHP
KSKPNPSLEF EIITTDEKID SASLRKELIA LFKLVFMASP SNIILDVVFK NPVQTILLKK
NELPGIDLTN LYVTTKTDGV GVLITVTNKG IYCFFTHLQY TIRYDTTFES NESVTLYGEA
VKQNNVWQIY LIKLITPKVS DRFKEKEYVE ERLQNICDRM TFKVKKYEGP FESHSEIIDL
LTTYLPSQPE GVVLFYSDQR NQPDYKIKLD NTTDHMINII YRYMSSEPVI FGENSTFLEY
KKFSDDKGFP KDYGTGKLML TDNVRYLNNI YCIAFTNVYE DVGIKNVVVP IKFISEFSAT
GELIKPRIDK TFKYLYKEYY GNQYQIVVAH IRDQNIKIGD VLDEDKLSDV GQHYANDKYR
LNPDVSYFTN KRTRGPLGIL SNYVKTLLIS LYCSKTFLDN SNKRKVLAID FGNGADLEKY
FYGEISSLVA TDPDKEAIGR CIERYNSLNS GIKSKYYKFD YIQETIRSVT YVSSVREVFF
FGKFDLVDWQ FAIHYSFHPK HYATVMNNLT ELTASGGKVL ITTMDGDLLS QLTDKKTFVI
HKNLPSSENY MSVEKIHEDQ ILVYNPSSMS RPMQEYIVKR VNLTKIFSEY GFELIDCVHF
DTIIERSKRF INSVSKMEER KSTKNFFELN REALKHEGTD IDDLLRYYIV YVFSKR
