Reviewed, UniProtKB/Swiss-Prot P22134 (MAG_YEAST)

Names and origin

Protein names

Recommended name:
    DNA-3-methyladenine glycosylase
    EC=3.2.2.21
Alternative name(s):
    3-methyladenine DNA glycosidase
    3MEA DNA glycosylase

Gene names

Name:	MAG1
Synonyms:	MAG
Ordered Locus Names:	YER142C

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

General annotation (Comments)

Function	Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine or 7-methyladenine from the damaged DNA polymer formed by alkylation lesions.
Catalytic activity	Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine.
Subcellular location	Nucleus. Ref.6
Induction	By DNA damage.
Sequence similarities	Belongs to the alkylbase DNA glycosidase alkA family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA dealkylation Ref.2 Inferred from expression pattern. Source: SGD base-excision repair Inferred from electronic annotation. Source: InterPro
Cellular component	nucleus Ref.1 Inferred by curator. Source: SGD
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro alkylbase DNA N-glycosylase activity Ref.1 Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CAN1	P04817	1	EBI-10381,EBI-3993

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 296	296	DNA-3-methyladenine glycosylase		PRO_0000194883
Sites
	Active site	209	1	Proton acceptor By similarity
	Site	189	1	Determinant for substrate specificity and/or activity By similarity
Amino acid modifications
	Modified residue	110	1	Phosphoserine Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P22134-1 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: 14CDD51CA6645507	FASTA	296	34,333
	10 20 30 40 50 60 MKLKREYDEL IKADAVKEIA KELGSRPLEV ALPEKYIARH EEKFNMACEH ILEKDPSLFP 70 80 90 100 110 120 ILKNNEFTLY LKETQVPNTL EDYFIRLAST ILSQQISGQA AESIKARVVS LYGGAFPDYK 130 140 150 160 170 180 ILFEDFKDPA KCAEIAKCGL SKRKMIYLES LAVYFTEKYK DIEKLFGQKD NDEEVIESLV 190 200 210 220 230 240 TNVKGIGPWS AKMFLISGLK RMDVFAPEDL GIARGFSKYL SDKPELEKEL MRERKVVKKS 250 260 270 280 290 KIKHKKYNWK IYDDDIMEKC SETFSPYRSV FMFILWRLAS TNTDAMMKAE ENFVKS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression in Escherichia coli of a gene for an alkylbase DNA glycosylase from Saccharomyces cerevisiae; a homologue to the bacterial alkA gene." Berdal K.G., Bjoeraas M., Bjelland S., Seeberg E.C. EMBO J. 9:4563-4568(1990) [PubMed: 2265619] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Saccharomyces cerevisiae 3-methyladenine DNA glycosylase has homology to the AlkA glycosylase of E. coli and is induced in response to DNA alkylation damage." Chen J., Derfler B., Samson L. EMBO J. 9:4569-4575(1990) [PubMed: 2265620] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W. Nature 387:78-81(1997) [PubMed: 9169868] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"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.
[5]	"Purification and properties of the alkylation repair DNA glycosylase encoded the MAG gene from Saccharomyces cerevisiae." Bjoras M., Klungland A., Johansen R.F., Seeberg E. Biochemistry 34:4577-4582(1995) [PubMed: 7718559] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-11.
[6]	"Yeast mitochondrial dehydrogenases are associated in a supramolecular complex." Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M. Biochemistry 40:9758-9769(2001) [PubMed: 11502169] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X56662 Genomic DNA. Translation: CAA39989.1. X57781 Genomic DNA. Translation: CAA40927.1. U18917 Genomic DNA. Translation: AAB64669.1. AY692938 Genomic DNA. Translation: AAT92957.1.
PIR	S12498.
RefSeq	NP_011069.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:6599N.
IntAct	P22134. 19 interactions.
STRING	P22134.
Genome annotation databases
Ensembl	YER142C; YER142C; YER142C; Saccharomyces cerevisiae. [Genome view]
GeneID	856885.
GenomeReviews	Gene locus YER142C in contig U00092_GR.
KEGG	sce:YER142C.
NMPDR	fig|4932.3.peg.2148.
Organism-specific databases
CYGD	YER142c.
SGD	S000000944. MAG1.
Phylogenomic databases
HOGENOM	P22134.
OMA	WSAKMFA.
Enzyme and pathway databases
BRENDA	3.2.2.21. 250.
Gene expression databases
ArrayExpress	P22134.
Genevestigator	P22134.
GermOnline	YER142C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000035. Alkylbase_DNA_glycsylse_CS. IPR003265. HhH-GPD_domain. IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif. [Graphical view]
Pfam	PF00730. HhH-GPD. 1 hit. [Graphical view]
SMART	SM00478. ENDO3c. 1 hit. SM00278. HhH1. 1 hit. [Graphical view]
PROSITE	PS00516. ALKYLBASE_DNA_GLYCOS. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	983278.

Entry information

Entry name

MAG_YEAST

Accession

Primary (citable) accession number: P22134

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	November 3, 2009
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)