MCES_YEAST
ID MCES_YEAST Reviewed; 436 AA.
AC P32783; D6VQN2; Q6B2G0;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=mRNA cap guanine-N7 methyltransferase;
DE EC=2.1.1.56 {ECO:0000250|UniProtKB:O43148};
DE AltName: Full=mRNA (guanine-N(7))-methyltransferase;
DE AltName: Full=mRNA cap methyltransferase;
GN Name=ABD1; OrderedLocusNames=YBR236C; ORFNames=YBR1602;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Corrado K., Pringle J.R.;
RT "Molecular analysis of the ABD1 gene of Saccharomyces cerevisiae, a gene
RT that displays mutational synergism with the bud formation gene BEM1.";
RL Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION.
RX PubMed=7623811; DOI=10.1128/mcb.15.8.4167;
RA Mao X., Schwer B., Shuman S.;
RT "Yeast mRNA cap methyltransferase is a 50-kilodalton protein encoded by an
RT essential gene.";
RL Mol. Cell. Biol. 15:4167-4174(1995).
RN [6]
RP MUTAGENESIS OF GLY-174; ASP-178; HIS-253; TYR-254; THR-282; GLU-287;
RP GLU-361 AND TYR-362.
RX PubMed=8552073; DOI=10.1128/mcb.16.2.475;
RA Mao X., Schwer B., Shuman S.;
RT "Mutational analysis of the Saccharomyces cerevisiae ABD1 gene: cap
RT methyltransferase activity is essential for cell growth.";
RL Mol. Cell. Biol. 16:475-480(1996).
RN [7]
RP MUTAGENESIS OF VAL-168; GLU-170; GLY-172; GLY-176; LYS-181; TYR-182;
RP ASP-194; ARG-206; TYR-254; GLY-276; GLY-277; GLU-347; TYR-348; VAL-349;
RP VAL-350; GLY-363; LEU-366; VAL-367 AND PHE-372.
RX PubMed=9169431; DOI=10.1074/jbc.272.23.14683;
RA Wang S.P., Shuman S.;
RT "Structure-function analysis of the mRNA cap methyltransferase of
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 272:14683-14689(1997).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=11018011; DOI=10.1101/gad.836300;
RA Schroeder S.C., Schwer B., Shuman S., Bentley D.;
RT "Dynamic association of capping enzymes with transcribing RNA polymerase
RT II.";
RL Genes Dev. 14:2435-2440(2000).
RN [9]
RP 3D-STRUCTURE MODELING OF 140-424, AND MUTAGENESIS OF GLU-170; ASP-194 AND
RP ARG-206.
RX PubMed=11472630; DOI=10.1186/1471-2105-2-2;
RA Bujnicki J.M., Feder M., Radlinska M., Rychlewski L.;
RT "mRNA:guanine-N7 cap methyltransferases: identification of novel members of
RT the family, evolutionary analysis, homology modeling, and analysis of
RT sequence-structure-function relationships.";
RL BMC Bioinformatics 2:2-2(2001).
CC -!- FUNCTION: Responsible for methylating the 5'-cap structure of mRNAs.
CC {ECO:0000269|PubMed:7623811}.
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;
CC Evidence={ECO:0000250|UniProtKB:O43148, ECO:0000255|PROSITE-
CC ProRule:PRU00895};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11018011}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. mRNA cap 0 methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00895}.
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DR EMBL; L12000; AAA34383.1; -; Genomic_DNA.
DR EMBL; Z36105; CAA85199.1; -; Genomic_DNA.
DR EMBL; AY692770; AAT92789.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07352.1; -; Genomic_DNA.
DR PIR; S41782; S41782.
DR RefSeq; NP_009795.3; NM_001178584.3.
DR AlphaFoldDB; P32783; -.
DR SMR; P32783; -.
DR BioGRID; 32931; 346.
DR DIP; DIP-2503N; -.
DR IntAct; P32783; 10.
DR MINT; P32783; -.
DR STRING; 4932.YBR236C; -.
DR iPTMnet; P32783; -.
DR MaxQB; P32783; -.
DR PaxDb; P32783; -.
DR PRIDE; P32783; -.
DR EnsemblFungi; YBR236C_mRNA; YBR236C; YBR236C.
DR GeneID; 852538; -.
DR KEGG; sce:YBR236C; -.
DR SGD; S000000440; ABD1.
DR VEuPathDB; FungiDB:YBR236C; -.
DR eggNOG; KOG1975; Eukaryota.
DR GeneTree; ENSGT00390000002368; -.
DR HOGENOM; CLU_020346_2_0_1; -.
DR InParanoid; P32783; -.
DR OMA; WDATSIY; -.
DR BioCyc; MetaCyc:G3O-29167-MON; -.
DR BioCyc; YEAST:G3O-29167-MON; -.
DR BRENDA; 2.1.1.56; 984.
DR Reactome; R-SCE-72086; mRNA Capping.
DR Reactome; R-SCE-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR PRO; PR:P32783; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P32783; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005845; C:mRNA cap binding complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; IDA:SGD.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
DR InterPro; IPR016899; mRNA_G-N7_MeTrfase_euk.
DR InterPro; IPR039753; RG7MT1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12189; PTHR12189; 1.
DR Pfam; PF03291; Pox_MCEL; 1.
DR PIRSF; PIRSF028762; ABD1; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51562; RNA_CAP0_MT; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; mRNA capping; mRNA processing; Nucleus;
KW Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..436
FT /note="mRNA cap guanine-N7 methyltransferase"
FT /id="PRO_0000210134"
FT DOMAIN 101..430
FT /note="mRNA cap 0 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 150..151
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="mRNA cap"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 154
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 172
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 194
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT BINDING 223
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT BINDING 249
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT BINDING 254
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:O43148"
FT SITE 175
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 181
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 206
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 253
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 347
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT SITE 416
FT /note="mRNA cap binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00895"
FT MUTAGEN 168
FT /note="V->A: Still viable; normal growth."
FT /evidence="ECO:0000269|PubMed:9169431"
FT MUTAGEN 170
FT /note="E->A: Non-viable; reduced enzyme activity to 8% of
FT wild-type."
FT /evidence="ECO:0000269|PubMed:11472630,
FT ECO:0000269|PubMed:9169431"
FT MUTAGEN 170
FT /note="E->D: Still viable; increase in activity."
FT /evidence="ECO:0000269|PubMed:11472630,
FT ECO:0000269|PubMed:9169431"
FT MUTAGEN 170
FT /note="E->Q: Non-viable; reduced enzyme activity to 8% of
FT wild-type."
FT /evidence="ECO:0000269|PubMed:11472630,
FT ECO:0000269|PubMed:9169431"
FT MUTAGEN 172
FT /note="G->A: Still viable; normal growth."
FT /evidence="ECO:0000269|PubMed:9169431"
FT MUTAGEN 174
FT /note="G->A: Non viable; no growth."
FT /evidence="ECO:0000269|PubMed:8552073"
FT MUTAGEN 176
FT /note="G->A: Still viable; normal growth."
FT /evidence="ECO:0000269|PubMed:9169431"
FT MUTAGEN 178
FT /note="D->A: Microcolony formation."
FT /evidence="ECO:0000269|PubMed:8552073"
FT MUTAGEN 181
FT /note="K->A: Still viable; normal growth."
FT /evidence="ECO:0000269|PubMed:9169431"
FT MUTAGEN 182
FT /note="Y->A: Still viable; normal growth."
FT /evidence="ECO:0000269|PubMed:9169431"
FT MUTAGEN 194
FT /note="D->A: Lethal; no enzyme activity."
FT /evidence="ECO:0000269|PubMed:11472630,
FT ECO:0000269|PubMed:9169431"
FT MUTAGEN 194
FT /note="D->E: Still viable; activity near to wild-type."
FT /evidence="ECO:0000269|PubMed:11472630,
FT ECO:0000269|PubMed:9169431"
FT MUTAGEN 194
FT /note="D->N: Lethal; no enzyme activity."
FT /evidence="ECO:0000269|PubMed:11472630,
FT ECO:0000269|PubMed:9169431"
FT MUTAGEN 206
FT /note="R->A: Lethal."
FT /evidence="ECO:0000269|PubMed:11472630,
FT ECO:0000269|PubMed:9169431"
FT MUTAGEN 206
FT /note="R->K: Still viable; little change in enzyme
FT activity."
FT /evidence="ECO:0000269|PubMed:11472630,
FT ECO:0000269|PubMed:9169431"
FT MUTAGEN 253
FT /note="H->A: Still viable; normal growth."
FT /evidence="ECO:0000269|PubMed:8552073"
FT MUTAGEN 254
FT /note="Y->A: Non viable; no growth."
FT /evidence="ECO:0000269|PubMed:8552073,
FT ECO:0000269|PubMed:9169431"
FT MUTAGEN 254
FT /note="Y->F: Still viable; slow growth; near to wild-type
FT enzyme activity."
FT /evidence="ECO:0000269|PubMed:8552073,
FT ECO:0000269|PubMed:9169431"
FT MUTAGEN 254
FT /note="Y->S: Lethal; Enzyme activity 10% of wild-type."
FT /evidence="ECO:0000269|PubMed:8552073,
FT ECO:0000269|PubMed:9169431"
FT MUTAGEN 276
FT /note="G->A: Still viable; normal growth."
FT /evidence="ECO:0000269|PubMed:9169431"
FT MUTAGEN 277
FT /note="G->A: Still viable; normal growth."
FT /evidence="ECO:0000269|PubMed:9169431"
FT MUTAGEN 282
FT /note="T->A: Still viable; normal growth."
FT /evidence="ECO:0000269|PubMed:8552073"
FT MUTAGEN 287
FT /note="E->A: Still viable; normal growth."
FT /evidence="ECO:0000269|PubMed:8552073"
FT MUTAGEN 347
FT /note="E->A: Still viable; normal growth."
FT /evidence="ECO:0000269|PubMed:9169431"
FT MUTAGEN 348
FT /note="Y->A: Still viable; normal growth."
FT /evidence="ECO:0000269|PubMed:9169431"
FT MUTAGEN 349
FT /note="V->A: Still viable; normal growth."
FT /evidence="ECO:0000269|PubMed:9169431"
FT MUTAGEN 350
FT /note="V->A: Still viable; normal growth."
FT /evidence="ECO:0000269|PubMed:9169431"
FT MUTAGEN 361
FT /note="E->A: Still viable; normal growth."
FT /evidence="ECO:0000269|PubMed:8552073"
FT MUTAGEN 362
FT /note="Y->A: Still viable; normal growth."
FT /evidence="ECO:0000269|PubMed:8552073"
FT MUTAGEN 363
FT /note="G->A: Still viable; normal growth."
FT /evidence="ECO:0000269|PubMed:9169431"
FT MUTAGEN 366
FT /note="L->A: Still viable; normal growth."
FT /evidence="ECO:0000269|PubMed:9169431"
FT MUTAGEN 367
FT /note="V->A: Still viable; normal growth."
FT /evidence="ECO:0000269|PubMed:9169431"
FT MUTAGEN 372
FT /note="F->A: Still viable; normal growth."
FT /evidence="ECO:0000269|PubMed:9169431"
FT CONFLICT 126
FT /note="Y -> C (in Ref. 4; AAT92789)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 436 AA; 50341 MW; EA5A68F0C4A57C4C CRC64;
MSTKPEKPIW MSQEDYDRQY GSITGDESST VSKKDSKVTA NAPGDGNGSL PVLQSSSILT
SKVSDLPIEA ESGFKIQKRR HERYDQEERL RKQRAQKLRE EQLKRHEIEM TANRSINVDQ
IVREHYNERT IIANRAKRNL SPIIKLRNFN NAIKYMLIDK YTKPGDVVLE LGCGKGGDLR
KYGAAGISQF IGIDISNASI QEAHKRYRSM RNLDYQVVLI TGDCFGESLG VAVEPFPDCR
FPCDIVSTQF CLHYAFETEE KARRALLNVA KSLKIGGHFF GTIPDSEFIR YKLNKFPKEV
EKPSWGNSIY KVTFENNSYQ KNDYEFTSPY GQMYTYWLED AIDNVPEYVV PFETLRSLAD
EYGLELVSQM PFNKFFVQEI PKWIERFSPK MREGLQRSDG RYGVEGDEKE AASYFYTMFA
FRKVKQYIEP ESVKPN
