Reviewed, UniProtKB/Swiss-Prot P32783 (MCES_YEAST)

Names and origin

Protein names

Recommended name:
    mRNA cap guanine-N7 methyltransferase
    EC=2.1.1.56
Alternative name(s):
    mRNA (guanine-N(7)-)-methyltransferase
    mRNA cap methyltransferase

Gene names

Name:	ABD1
Ordered Locus Names:	YBR236C
ORF Names:	YBR1602

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	436 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Responsible for methylating the 5'-cap structure of mRNAs. Ref.4
Catalytic activity	S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.
Subcellular location	Nucleus.
Sequence similarities	Belongs to the methyltransferase superfamily. mRNA cap methyltransferase family.

Ontologies

Keywords
Biological process	mRNA capping mRNA processing
Cellular component	Nucleus
Ligand	RNA-binding S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	mRNA capping Ref.4 Inferred from direct assay. Source: SGD
Cellular component	DNA-directed RNA polymerase II, holoenzyme Ref.7 Inferred from physical interaction. Source: SGD
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW mRNA (guanine-N7-)-methyltransferase activity Ref.4 Inferred from direct assay. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 436

436

mRNA cap guanine-N7 methyltransferase

PRO_0000210134

Regions

Region

150 – 151

2

mRNA cap binding By similarity

Sites

Binding site

154

1

S-adenosyl-L-methionine By similarity

Binding site

172

1

S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Binding site

175

1

mRNA cap By similarity

Binding site

181

1

mRNA cap By similarity

Binding site

194

1

S-adenosyl-L-methionine By similarity

Binding site

206

1

mRNA cap By similarity

Binding site

223

1

S-adenosyl-L-methionine

Binding site

249

1

S-adenosyl-L-methionine; via carbonyl oxygen

Binding site

253

1

mRNA cap By similarity

Binding site

347

1

mRNA cap By similarity

Binding site

416

1

mRNA cap By similarity

Experimental info

Mutagenesis

168

1

V → A: Still viable; normal growth. Ref.6

Mutagenesis

170

1

E → A: Non-viable; reduced enzyme activity to 8% of wild-type. Ref.6 Ref.8

Mutagenesis

170

1

E → D: Still viable; increase in activity. Ref.6 Ref.8

Mutagenesis

170

1

E → Q: Non-viable; reduced enzyme activity to 8% of wild-type. Ref.6 Ref.8

Mutagenesis

172

1

G → A: Still viable; normal growth. Ref.6

Mutagenesis

174

1

G → A: Non viable; no growth. Ref.5

Mutagenesis

176

1

G → A: Still viable; normal growth. Ref.6

Mutagenesis

178

1

D → A: Microcolony formation. Ref.5

Mutagenesis

181

1

K → A: Still viable; normal growth. Ref.6

Mutagenesis

182

1

Y → A: Still viable; normal growth. Ref.6

Mutagenesis

194

1

D → A: Lethal; no enzyme activity. Ref.6 Ref.8

Mutagenesis

194

1

D → E: Still viable; activity near to wild-type. Ref.6 Ref.8

Mutagenesis

194

1

D → N: Lethal; no enzyme activity. Ref.6 Ref.8

Mutagenesis

206

1

R → A: Lethal. Ref.6 Ref.8

Mutagenesis

206

1

R → K: Still viable; little change in enzyme activity. Ref.6 Ref.8

Mutagenesis

253

1

H → A: Still viable; normal growth. Ref.5

Mutagenesis

254

1

Y → A: Non viable; no growth. Ref.6 Ref.5

Mutagenesis

254

1

Y → F: Still viable; slow growth; near to wild-type enzyme activity. Ref.6 Ref.5

Mutagenesis

254

1

Y → S: Lethal; Enzyme activity 10% of wild-type. Ref.6 Ref.5

Mutagenesis

276

1

G → A: Still viable; normal growth. Ref.6

Mutagenesis

277

1

G → A: Still viable; normal growth. Ref.6

Mutagenesis

282

1

T → A: Still viable; normal growth. Ref.5

Mutagenesis

287

1

E → A: Still viable; normal growth. Ref.5

Mutagenesis

347

1

E → A: Still viable; normal growth. Ref.6

Mutagenesis

348

1

Y → A: Still viable; normal growth. Ref.6

Mutagenesis

349

1

V → A: Still viable; normal growth. Ref.6

Mutagenesis

350

1

V → A: Still viable; normal growth. Ref.6

Mutagenesis

361

1

E → A: Still viable; normal growth. Ref.5

Mutagenesis

362

1

Y → A: Still viable; normal growth. Ref.5

Mutagenesis

363

1

G → A: Still viable; normal growth. Ref.6

Mutagenesis

366

1

L → A: Still viable; normal growth. Ref.6

Mutagenesis

367

1

V → A: Still viable; normal growth. Ref.6

Mutagenesis

372

1

F → A: Still viable; normal growth. Ref.6

Sequence conflict

126

1

Y → C in AAT92789. Ref.3

Secondary structure

1

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436

Helix Strand Turn

Details...

Helix

151 – 161

11

Beta strand

168 – 171

4

Helix

177 – 185

9

Beta strand

190 – 195

6

Helix

197 – 210

14

Beta strand

217 – 221

5

Helix

224 – 226

3

Helix

227 – 231

5

Turn

232 – 239

8

Beta strand

244 – 248

5

Helix

253 – 255

3

Helix

261 – 271

11

Beta strand

278 – 284

7

Helix

286 – 292

7

Turn

304 – 306

3

Beta strand

312 – 320

9

Turn

322 – 324

3

Beta strand

327 – 339

13

Helix

352 – 359

8

Beta strand

366 – 374

9

Beta strand

415 – 421

7

Sequences

	Sequence		Length	Mass (Da)
	P32783-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: EA5A68F0C4A57C4C	FASTA	436	50,341
	10 20 30 40 50 60 MSTKPEKPIW MSQEDYDRQY GSITGDESST VSKKDSKVTA NAPGDGNGSL PVLQSSSILT 70 80 90 100 110 120 SKVSDLPIEA ESGFKIQKRR HERYDQEERL RKQRAQKLRE EQLKRHEIEM TANRSINVDQ 130 140 150 160 170 180 IVREHYNERT IIANRAKRNL SPIIKLRNFN NAIKYMLIDK YTKPGDVVLE LGCGKGGDLR 190 200 210 220 230 240 KYGAAGISQF IGIDISNASI QEAHKRYRSM RNLDYQVVLI TGDCFGESLG VAVEPFPDCR 250 260 270 280 290 300 FPCDIVSTQF CLHYAFETEE KARRALLNVA KSLKIGGHFF GTIPDSEFIR YKLNKFPKEV 310 320 330 340 350 360 EKPSWGNSIY KVTFENNSYQ KNDYEFTSPY GQMYTYWLED AIDNVPEYVV PFETLRSLAD 370 380 390 400 410 420 EYGLELVSQM PFNKFFVQEI PKWIERFSPK MREGLQRSDG RYGVEGDEKE AASYFYTMFA 430 FRKVKQYIEP ESVKPN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular analysis of the ABD1 gene of Saccharomyces cerevisiae, a gene that displays mutational synergism with the bud formation gene BEM1." Corrado K., Pringle J.R. Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete DNA sequence of yeast chromosome II." 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. EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." 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. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Yeast mRNA cap methyltransferase is a 50-kilodalton protein encoded by an essential gene." Mao X., Schwer B., Shuman S. Mol. Cell. Biol. 15:4167-4174(1995) [PubMed: 7623811] [Abstract] Cited for: FUNCTION.
[5]	"Mutational analysis of the Saccharomyces cerevisiae ABD1 gene: cap methyltransferase activity is essential for cell growth." Mao X., Schwer B., Shuman S. Mol. Cell. Biol. 16:475-480(1996) [PubMed: 8552073] [Abstract] Cited for: MUTAGENESIS OF GLY-174; ASP-178; HIS-253; TYR-254; THR-282; GLU-287; GLU-361 AND TYR-362.
[6]	"Structure-function analysis of the mRNA cap methyltransferase of Saccharomyces cerevisiae." Wang S.P., Shuman S. J. Biol. Chem. 272:14683-14689(1997) [PubMed: 9169431] [Abstract] Cited for: 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.
[7]	"Dynamic association of capping enzymes with transcribing RNA polymerase II." Schroeder S.C., Schwer B., Shuman S., Bentley D. Genes Dev. 14:2435-2440(2000) [PubMed: 11018011] [Abstract] Cited for: SUBCELLULAR LOCATION.
[8]	"mRNA:guanine-N7 cap methyltransferases: identification of novel members of the family, evolutionary analysis, homology modeling, and analysis of sequence-structure-function relationships." Bujnicki J.M., Feder M., Radlinska M., Rychlewski L. BMC Bioinformatics 2:2-2(2001) [PubMed: 11472630] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 140-424, MUTAGENESIS OF GLU-170; ASP-194 AND ARG-206.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L12000 Genomic DNA. Translation: AAA34383.1.
Z36105 Genomic DNA. Translation: CAA85199.1.
AY692770 Genomic DNA. Translation: AAT92789.1.

PIR

S41782.

RefSeq

NP_009795.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IC3	model	-	A	140-424	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:2503N.

IntAct

P32783. 13 interactions.

STRING

P32783.

Proteomic databases

PeptideAtlas

P32783.

Genome annotation databases

Ensembl

YBR236C; YBR236C; YBR236C; Saccharomyces cerevisiae. [Genome view]

GeneID

852538.

KEGG

sce:YBR236C.

NMPDR

fig|4932.3.peg.510.

Organism-specific databases

CYGD

YBR236c.

SGD

S000000440. ABD1.

Phylogenomic databases

HOGENOM

P32783.

OMA

WLEDAID

OrthoDB

EOG9GMWD7

Enzyme and pathway databases

BRENDA

2.1.1.56. 250.

Gene expression databases

ArrayExpress

P32783.

Genevestigator

P32783.

GermOnline

YBR236C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR016899. mRNA_G-N7_MeTrfase.
IPR004971. Pox_MCEL.
[Graphical view]

Pfam

PF03291. Pox_MCEL. 1 hit.
[Graphical view]

PIRSF

PIRSF028762. ABD1. 1 hit.

ProtoNet

Search...

Other Resources

NextBio

971601.

Entry information

Entry name

MCES_YEAST

Accession

Primary (citable) accession number: P32783
Secondary accession number(s): Q6B2G0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	November 24, 2009
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)