MAG_YEAST
ID MAG_YEAST Reviewed; 296 AA.
AC P22134; D3DM49;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=DNA-3-methyladenine glycosylase;
DE EC=3.2.2.21;
DE AltName: Full=3-methyladenine DNA glycosidase;
DE AltName: Full=3MEA DNA glycosylase;
GN Name=MAG1; Synonyms=MAG; OrderedLocusNames=YER142C;
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].
RX PubMed=2265619; DOI=10.1002/j.1460-2075.1990.tb07909.x;
RA Berdal K.G., Bjoeraas M., Bjelland S., Seeberg E.C.;
RT "Cloning and expression in Escherichia coli of a gene for an alkylbase DNA
RT glycosylase from Saccharomyces cerevisiae; a homologue to the bacterial
RT alkA gene.";
RL EMBO J. 9:4563-4568(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2265620; DOI=10.1002/j.1460-2075.1990.tb07910.x;
RA Chen J., Derfler B., Samson L.;
RT "Saccharomyces cerevisiae 3-methyladenine DNA glycosylase has homology to
RT the AlkA glycosylase of E. coli and is induced in response to DNA
RT alkylation damage.";
RL EMBO J. 9:4569-4575(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 1-11.
RX PubMed=7718559; DOI=10.1021/bi00014a010;
RA Bjoras M., Klungland A., Johansen R.F., Seeberg E.;
RT "Purification and properties of the alkylation repair DNA glycosylase
RT encoded the MAG gene from Saccharomyces cerevisiae.";
RL Biochemistry 34:4577-4582(1995).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=11502169; DOI=10.1021/bi010277r;
RA Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S.,
RA Schmitter J.-M.;
RT "Yeast mitochondrial dehydrogenases are associated in a supramolecular
RT complex.";
RL Biochemistry 40:9758-9769(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-
CC methyladenine or 7-methyladenine from the damaged DNA polymer formed by
CC alkylation lesions.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-
CC methylguanine, 7-methylguanine and 7-methyladenine.; EC=3.2.2.21;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11502169}.
CC -!- INDUCTION: By DNA damage.
CC -!- SIMILARITY: Belongs to the alkylbase DNA glycosidase AlkA family.
CC {ECO:0000305}.
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DR EMBL; X56662; CAA39989.1; -; Genomic_DNA.
DR EMBL; X57781; CAA40927.1; -; Genomic_DNA.
DR EMBL; U18917; AAB64669.1; -; Genomic_DNA.
DR EMBL; AY692938; AAT92957.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07803.1; -; Genomic_DNA.
DR PIR; S12498; S12498.
DR RefSeq; NP_011069.1; NM_001179032.1.
DR AlphaFoldDB; P22134; -.
DR SMR; P22134; -.
DR BioGRID; 36891; 122.
DR DIP; DIP-6599N; -.
DR IntAct; P22134; 22.
DR STRING; 4932.YER142C; -.
DR iPTMnet; P22134; -.
DR MaxQB; P22134; -.
DR PaxDb; P22134; -.
DR PRIDE; P22134; -.
DR EnsemblFungi; YER142C_mRNA; YER142C; YER142C.
DR GeneID; 856885; -.
DR KEGG; sce:YER142C; -.
DR SGD; S000000944; MAG1.
DR VEuPathDB; FungiDB:YER142C; -.
DR eggNOG; KOG1918; Eukaryota.
DR GeneTree; ENSGT00640000091554; -.
DR HOGENOM; CLU_000445_72_4_1; -.
DR InParanoid; P22134; -.
DR OMA; FMFILWR; -.
DR BioCyc; YEAST:G3O-30303-MON; -.
DR PRO; PR:P22134; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P22134; protein.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR GO; GO:0032131; F:alkylated DNA binding; IBA:GO_Central.
DR GO; GO:0003905; F:alkylbase DNA N-glycosylase activity; IDA:SGD.
DR GO; GO:0003684; F:damaged DNA binding; IDA:SGD.
DR GO; GO:0008725; F:DNA-3-methyladenine glycosylase activity; IDA:SGD.
DR GO; GO:0052822; F:DNA-3-methylguanine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0052821; F:DNA-7-methyladenine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0043916; F:DNA-7-methylguanine glycosylase activity; IBA:GO_Central.
DR GO; GO:0006285; P:base-excision repair, AP site formation; IMP:SGD.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IMP:SGD.
DR CDD; cd00056; ENDO3c; 1.
DR InterPro; IPR000035; Alkylbase_DNA_glycsylse_CS.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR003265; HhH-GPD_domain.
DR Pfam; PF00730; HhH-GPD; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; SSF48150; 1.
DR PROSITE; PS00516; ALKYLBASE_DNA_GLYCOS; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA damage; DNA repair; Hydrolase; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..296
FT /note="DNA-3-methyladenine glycosylase"
FT /id="PRO_0000194883"
FT ACT_SITE 209
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT SITE 189
FT /note="Determinant for substrate specificity and/or
FT activity"
FT /evidence="ECO:0000250"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 296 AA; 34333 MW; 14CDD51CA6645507 CRC64;
MKLKREYDEL IKADAVKEIA KELGSRPLEV ALPEKYIARH EEKFNMACEH ILEKDPSLFP
ILKNNEFTLY LKETQVPNTL EDYFIRLAST ILSQQISGQA AESIKARVVS LYGGAFPDYK
ILFEDFKDPA KCAEIAKCGL SKRKMIYLES LAVYFTEKYK DIEKLFGQKD NDEEVIESLV
TNVKGIGPWS AKMFLISGLK RMDVFAPEDL GIARGFSKYL SDKPELEKEL MRERKVVKKS
KIKHKKYNWK IYDDDIMEKC SETFSPYRSV FMFILWRLAS TNTDAMMKAE ENFVKS
