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mRNA cap guanine-N7 methyltransferase (EC 2.1.1.56) (mRNA (guanine-N(7)-)-methyltransferase) (mRNA cap methyltransferase)

 MCES_YEAST              Reviewed;         436 AA.
P32783; D6VQN2; Q6B2G0;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
25-OCT-2017, entry version 149.
RecName: Full=mRNA cap guanine-N7 methyltransferase;
EC=2.1.1.56 {ECO:0000250|UniProtKB:O43148};
AltName: Full=mRNA (guanine-N(7)-)-methyltransferase;
AltName: Full=mRNA cap methyltransferase;
Name=ABD1; OrderedLocusNames=YBR236C; ORFNames=YBR1602;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Corrado K., Pringle J.R.;
"Molecular analysis of the ABD1 gene of Saccharomyces cerevisiae, a
gene that displays mutational synergism with the bud formation gene
BEM1.";
Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418;
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
FUNCTION.
PubMed=7623811; DOI=10.1128/MCB.15.8.4167;
Mao X., Schwer B., Shuman S.;
"Yeast mRNA cap methyltransferase is a 50-kilodalton protein encoded
by an essential gene.";
Mol. Cell. Biol. 15:4167-4174(1995).
[6]
MUTAGENESIS OF GLY-174; ASP-178; HIS-253; TYR-254; THR-282; GLU-287;
GLU-361 AND TYR-362.
PubMed=8552073; DOI=10.1128/MCB.16.2.475;
Mao X., Schwer B., Shuman S.;
"Mutational analysis of the Saccharomyces cerevisiae ABD1 gene: cap
methyltransferase activity is essential for cell growth.";
Mol. Cell. Biol. 16:475-480(1996).
[7]
MUTAGENESIS OF VAL-168; GLU-170; GLY-172; GLY-176; LYS-181; TYR-182;
ASP-194; ARG-206; TYR-254; GLY-276; GLY-277; GLU-347; TYR-348;
VAL-349; VAL-350; GLY-363; LEU-366; VAL-367 AND PHE-372.
PubMed=9169431; DOI=10.1074/jbc.272.23.14683;
Wang S.P., Shuman S.;
"Structure-function analysis of the mRNA cap methyltransferase of
Saccharomyces cerevisiae.";
J. Biol. Chem. 272:14683-14689(1997).
[8]
SUBCELLULAR LOCATION.
PubMed=11018011; DOI=10.1101/gad.836300;
Schroeder S.C., Schwer B., Shuman S., Bentley D.;
"Dynamic association of capping enzymes with transcribing RNA
polymerase II.";
Genes Dev. 14:2435-2440(2000).
[9]
3D-STRUCTURE MODELING OF 140-424, AND MUTAGENESIS OF GLU-170; ASP-194
AND ARG-206.
PubMed=11472630; DOI=10.1186/1471-2105-2-2;
Bujnicki J.M., Feder M., Radlinska M., Rychlewski L.;
"mRNA:guanine-N7 cap methyltransferases: identification of novel
members of the family, evolutionary analysis, homology modeling, and
analysis of sequence-structure-function relationships.";
BMC Bioinformatics 2:2-2(2001).
-!- FUNCTION: Responsible for methylating the 5'-cap structure of
mRNAs. {ECO:0000269|PubMed:7623811}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
{ECO:0000250|UniProtKB:O43148, ECO:0000255|PROSITE-
ProRule:PRU00895}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11018011}.
-!- SIMILARITY: Belongs to the class I-like SAM-binding
methyltransferase superfamily. mRNA cap 0 methyltransferase
family. {ECO:0000255|PROSITE-ProRule:PRU00895}.
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EMBL; L12000; AAA34383.1; -; Genomic_DNA.
EMBL; Z36105; CAA85199.1; -; Genomic_DNA.
EMBL; AY692770; AAT92789.1; -; Genomic_DNA.
EMBL; BK006936; DAA07352.1; -; Genomic_DNA.
PIR; S41782; S41782.
RefSeq; NP_009795.3; NM_001178584.3.
PDB; 1IC3; Model; -; A=140-424.
PDBsum; 1IC3; -.
ProteinModelPortal; P32783; -.
SMR; P32783; -.
BioGrid; 32931; 342.
DIP; DIP-2503N; -.
IntAct; P32783; 10.
MINT; MINT-631955; -.
STRING; 4932.YBR236C; -.
iPTMnet; P32783; -.
MaxQB; P32783; -.
PRIDE; P32783; -.
EnsemblFungi; YBR236C; YBR236C; YBR236C.
GeneID; 852538; -.
KEGG; sce:YBR236C; -.
EuPathDB; FungiDB:YBR236C; -.
SGD; S000000440; ABD1.
GeneTree; ENSGT00390000002368; -.
HOGENOM; HOG000242614; -.
InParanoid; P32783; -.
KO; K00565; -.
OMA; LNLVSCQ; -.
OrthoDB; EOG092C2SMS; -.
BioCyc; MetaCyc:G3O-29167-MONOMER; -.
BioCyc; YEAST:G3O-29167-MONOMER; -.
BRENDA; 2.1.1.56; 984.
Reactome; R-SCE-72086; mRNA Capping.
Reactome; R-SCE-77075; RNA Pol II CTD phosphorylation and interaction with CE.
PRO; PR:P32783; -.
Proteomes; UP000002311; Chromosome II.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0005845; C:mRNA cap binding complex; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; IDA:SGD.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0006370; P:7-methylguanosine mRNA capping; IDA:SGD.
InterPro; IPR016899; mRNA_G-N7_MeTrfase.
InterPro; IPR004971; mRNA_G-N7_MeTrfase_dom.
InterPro; IPR029063; SAM-dependent_MTases.
Pfam; PF03291; Pox_MCEL; 1.
PIRSF; PIRSF028762; ABD1; 1.
SUPFAM; SSF53335; SSF53335; 1.
PROSITE; PS51562; RNA_CAP0_MT; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Methyltransferase; mRNA capping;
mRNA processing; Nucleus; Reference proteome; RNA-binding;
S-adenosyl-L-methionine; Transferase.
CHAIN 1 436 mRNA cap guanine-N7 methyltransferase.
/FTId=PRO_0000210134.
DOMAIN 101 430 mRNA cap 0 methyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00895}.
REGION 150 151 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
BINDING 154 154 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00895}.
BINDING 172 172 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
BINDING 194 194 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00895}.
BINDING 223 223 S-adenosyl-L-methionine; via amide
nitrogen. {ECO:0000250|UniProtKB:O43148}.
BINDING 249 249 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000250|UniProtKB:O43148}.
BINDING 253 253 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
BINDING 254 254 S-adenosyl-L-methionine.
{ECO:0000250|UniProtKB:O43148}.
BINDING 347 347 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
BINDING 416 416 mRNA cap. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
SITE 175 175 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
SITE 181 181 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
SITE 206 206 mRNA cap binding. {ECO:0000255|PROSITE-
ProRule:PRU00895}.
MUTAGEN 168 168 V->A: Still viable; normal growth.
{ECO:0000269|PubMed:9169431}.
MUTAGEN 170 170 E->A: Non-viable; reduced enzyme activity
to 8% of wild-type.
{ECO:0000269|PubMed:11472630,
ECO:0000269|PubMed:9169431}.
MUTAGEN 170 170 E->D: Still viable; increase in activity.
{ECO:0000269|PubMed:11472630,
ECO:0000269|PubMed:9169431}.
MUTAGEN 170 170 E->Q: Non-viable; reduced enzyme activity
to 8% of wild-type.
{ECO:0000269|PubMed:11472630,
ECO:0000269|PubMed:9169431}.
MUTAGEN 172 172 G->A: Still viable; normal growth.
{ECO:0000269|PubMed:9169431}.
MUTAGEN 174 174 G->A: Non viable; no growth.
{ECO:0000269|PubMed:8552073}.
MUTAGEN 176 176 G->A: Still viable; normal growth.
{ECO:0000269|PubMed:9169431}.
MUTAGEN 178 178 D->A: Microcolony formation.
{ECO:0000269|PubMed:8552073}.
MUTAGEN 181 181 K->A: Still viable; normal growth.
{ECO:0000269|PubMed:9169431}.
MUTAGEN 182 182 Y->A: Still viable; normal growth.
{ECO:0000269|PubMed:9169431}.
MUTAGEN 194 194 D->A: Lethal; no enzyme activity.
{ECO:0000269|PubMed:11472630,
ECO:0000269|PubMed:9169431}.
MUTAGEN 194 194 D->E: Still viable; activity near to
wild-type. {ECO:0000269|PubMed:11472630,
ECO:0000269|PubMed:9169431}.
MUTAGEN 194 194 D->N: Lethal; no enzyme activity.
{ECO:0000269|PubMed:11472630,
ECO:0000269|PubMed:9169431}.
MUTAGEN 206 206 R->A: Lethal.
{ECO:0000269|PubMed:11472630,
ECO:0000269|PubMed:9169431}.
MUTAGEN 206 206 R->K: Still viable; little change in
enzyme activity.
{ECO:0000269|PubMed:11472630,
ECO:0000269|PubMed:9169431}.
MUTAGEN 253 253 H->A: Still viable; normal growth.
{ECO:0000269|PubMed:8552073}.
MUTAGEN 254 254 Y->A: Non viable; no growth.
{ECO:0000269|PubMed:8552073,
ECO:0000269|PubMed:9169431}.
MUTAGEN 254 254 Y->F: Still viable; slow growth; near to
wild-type enzyme activity.
{ECO:0000269|PubMed:8552073,
ECO:0000269|PubMed:9169431}.
MUTAGEN 254 254 Y->S: Lethal; Enzyme activity 10% of
wild-type. {ECO:0000269|PubMed:8552073,
ECO:0000269|PubMed:9169431}.
MUTAGEN 276 276 G->A: Still viable; normal growth.
{ECO:0000269|PubMed:9169431}.
MUTAGEN 277 277 G->A: Still viable; normal growth.
{ECO:0000269|PubMed:9169431}.
MUTAGEN 282 282 T->A: Still viable; normal growth.
{ECO:0000269|PubMed:8552073}.
MUTAGEN 287 287 E->A: Still viable; normal growth.
{ECO:0000269|PubMed:8552073}.
MUTAGEN 347 347 E->A: Still viable; normal growth.
{ECO:0000269|PubMed:9169431}.
MUTAGEN 348 348 Y->A: Still viable; normal growth.
{ECO:0000269|PubMed:9169431}.
MUTAGEN 349 349 V->A: Still viable; normal growth.
{ECO:0000269|PubMed:9169431}.
MUTAGEN 350 350 V->A: Still viable; normal growth.
{ECO:0000269|PubMed:9169431}.
MUTAGEN 361 361 E->A: Still viable; normal growth.
{ECO:0000269|PubMed:8552073}.
MUTAGEN 362 362 Y->A: Still viable; normal growth.
{ECO:0000269|PubMed:8552073}.
MUTAGEN 363 363 G->A: Still viable; normal growth.
{ECO:0000269|PubMed:9169431}.
MUTAGEN 366 366 L->A: Still viable; normal growth.
{ECO:0000269|PubMed:9169431}.
MUTAGEN 367 367 V->A: Still viable; normal growth.
{ECO:0000269|PubMed:9169431}.
MUTAGEN 372 372 F->A: Still viable; normal growth.
{ECO:0000269|PubMed:9169431}.
CONFLICT 126 126 Y -> C (in Ref. 4; AAT92789).
{ECO:0000305}.
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


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