MCEL_FOWPN
ID MCEL_FOWPN Reviewed; 851 AA.
AC Q9J584;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 89.
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 OrderedLocusNames=FPV146;
OS Fowlpox virus (strain NVSL) (FPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus.
OX NCBI_TaxID=928301;
OH NCBI_TaxID=7742; Vertebrata.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT "The genome of fowlpox virus.";
RL J. Virol. 74:3815-3831(2000).
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; AF198100; AAF44490.1; -; Genomic_DNA.
DR RefSeq; NP_039109.1; NC_002188.1.
DR SMR; Q9J584; -.
DR GeneID; 1486694; -.
DR KEGG; vg:1486694; -.
DR Proteomes; UP000008597; 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..851
FT /note="mRNA-capping enzyme catalytic subunit"
FT /id="PRO_0000210130"
FT DOMAIN 521..851
FT /note="mRNA cap 0 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT REGION 1..544
FT /note="Triphosphatase-guanylyltransferase"
FT /evidence="ECO:0000250"
FT ACT_SITE 266
FT /note="N6-GMP-lysine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 38
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 40
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 199
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 201
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 554..555
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 574..575
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 578
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 603
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 625
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 683..685
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 80
FT /note="Essential for RNA triphosphatase activity"
FT /evidence="ECO:0000250"
FT SITE 110
FT /note="Essential for RNA triphosphatase activity"
FT /evidence="ECO:0000250"
FT SITE 131
FT /note="Essential for RNA triphosphatase activity"
FT /evidence="ECO:0000250"
FT SITE 164
FT /note="Essential for RNA triphosphatase activity"
FT /evidence="ECO:0000250"
FT SITE 166
FT /note="Essential for RNA triphosphatase activity"
FT /evidence="ECO:0000250"
FT SITE 612
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 637
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 687
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 768
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 842
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
SQ SEQUENCE 851 AA; 98888 MW; DC3607ADD634BA7A CRC64;
MDKYISKTPL SCYFEELVDT FISVVNSINK VDESKHHEVE LILFKPPIIT LTNLYNMATT
TESYIEFTML PVDKPNTKFR NRIPLSKIHG LDVKNNQLVE SLDGFIWEEK SLLLKKDISD
NSSAIIKYSI EEKTLFVDYK RRNASIKLEL VSVVRAKLRN IVIDFKMKYF LGSGAQSANS
SSLLCALNHP KNKPSLYIEF EIMMQDKNIS KKKLLEELNM SASALFLSHP KYIRLCPSIN
PILRTHLLKK QDIININTDD LYITSKTDGI FSHVYIEKKS IFCYFSHLGY IKEYTASREI
EETIYLYAEM RKEESILYLT VIKVLKPCME DRLSELAFVK NHLTGIHDRL VFVTKCYDGP
FESSSDLVVS IEEMLKTEQE GIILFYSKGE DSTTDYKVKK DNTIDQCVNV IYRYMSSEPI
VFNDKGSFLE YKRYSNDKGF PKEFSTGKLD LNGSVEYINN IYCIEIKHLN PCTGITNLVL
PIKFIAEFSH NDELIQPRID KTMKYLYESG YYGNQLSVIM DHLNDQKLRI GDVFEEEKLA
DIAAHMKLKD SMRLNPDGNY FLSNRVRGAL GILSNFVKTL LISLYCSKTY LDNHSKRKVL
AIDFGNGADL EKYFYGEIAL MVATDPDDNA IETGKKRYNE RNAGDKSKYY KFNYIKETIR
SETYVSSIRQ VLYFEKFSLV DWQFAIHYSF HPKHYSTIMT NLQELTESGC KVLITTMDGD
YLDTLKEKKK FIIRKLLPET ENYLSIEKID DDKVLVYNPS SMSKPMAEYI VRRDTLIRVF
REYKFKLIDS CNFKTIIDRN ISFINGVSRL ESRGSTKNFF ELNRKALEEC NDTDVLELLS
HYMVYVFSKE V
