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Protein

DNA-3-methyladenine glycosylase

Gene

MAG1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine or 7-methyladenine from the damaged DNA polymer formed by alkylation lesions.

Catalytic activityi

Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei189 – 1891Determinant for substrate specificity and/or activityBy similarity
Active sitei209 – 2091Proton acceptorBy similarity

GO - Molecular functioni

  1. alkylbase DNA N-glycosylase activity Source: SGD
  2. damaged DNA binding Source: SGD
  3. DNA-3-methyladenine glycosylase activity Source: SGD
  4. DNA-3-methylguanine glycosylase activity Source: UniProtKB-EC
  5. DNA-7-methyladenine glycosylase activity Source: UniProtKB-EC
  6. DNA-7-methylguanine glycosylase activity Source: UniProtKB-EC

GO - Biological processi

  1. base-excision repair, AP site formation Source: SGD
  2. DNA dealkylation involved in DNA repair Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

BioCyciYEAST:G3O-30303-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-3-methyladenine glycosylase (EC:3.2.2.21)
Alternative name(s):
3-methyladenine DNA glycosidase
3MEA DNA glycosylase
Gene namesi
Name:MAG1
Synonyms:MAG
Ordered Locus Names:YER142C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome V

Organism-specific databases

CYGDiYER142c.
SGDiS000000944. MAG1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 296296DNA-3-methyladenine glycosylasePRO_0000194883Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei110 – 1101Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP22134.
PaxDbiP22134.

Expressioni

Inductioni

By DNA damage.

Gene expression databases

GenevestigatoriP22134.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CAN1P048171EBI-10381,EBI-3993

Protein-protein interaction databases

BioGridi36891. 73 interactions.
DIPiDIP-6599N.
MINTiMINT-675790.
STRINGi4932.YER142C.

Structurei

3D structure databases

ProteinModelPortaliP22134.
SMRiP22134. Positions 51-291.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0122.
HOGENOMiHOG000113466.
InParanoidiP22134.
KOiK01247.
OMAiWSAKMFA.
OrthoDBiEOG78SQVJ.

Family and domain databases

Gene3Di1.10.1670.10. 2 hits.
1.10.340.30. 1 hit.
InterProiIPR000035. Alkylbase_DNA_glycsylse_CS.
IPR011257. DNA_glycosylase.
IPR003265. HhH-GPD_domain.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR023170. HTH_base_excis_C.
[Graphical view]
PfamiPF00730. HhH-GPD. 1 hit.
[Graphical view]
SMARTiSM00478. ENDO3c. 1 hit.
SM00278. HhH1. 1 hit.
[Graphical view]
SUPFAMiSSF48150. SSF48150. 2 hits.
PROSITEiPS00516. ALKYLBASE_DNA_GLYCOS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22134-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLKREYDEL IKADAVKEIA KELGSRPLEV ALPEKYIARH EEKFNMACEH
60 70 80 90 100
ILEKDPSLFP ILKNNEFTLY LKETQVPNTL EDYFIRLAST ILSQQISGQA
110 120 130 140 150
AESIKARVVS LYGGAFPDYK ILFEDFKDPA KCAEIAKCGL SKRKMIYLES
160 170 180 190 200
LAVYFTEKYK DIEKLFGQKD NDEEVIESLV TNVKGIGPWS AKMFLISGLK
210 220 230 240 250
RMDVFAPEDL GIARGFSKYL SDKPELEKEL MRERKVVKKS KIKHKKYNWK
260 270 280 290
IYDDDIMEKC SETFSPYRSV FMFILWRLAS TNTDAMMKAE ENFVKS
Length:296
Mass (Da):34,333
Last modified:August 1, 1991 - v1
Checksum:i14CDD51CA6645507
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56662 Genomic DNA. Translation: CAA39989.1.
X57781 Genomic DNA. Translation: CAA40927.1.
U18917 Genomic DNA. Translation: AAB64669.1.
AY692938 Genomic DNA. Translation: AAT92957.1.
BK006939 Genomic DNA. Translation: DAA07803.1.
PIRiS12498.
RefSeqiNP_011069.1. NM_001179032.1.

Genome annotation databases

EnsemblFungiiYER142C; YER142C; YER142C.
GeneIDi856885.
KEGGisce:YER142C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56662 Genomic DNA. Translation: CAA39989.1.
X57781 Genomic DNA. Translation: CAA40927.1.
U18917 Genomic DNA. Translation: AAB64669.1.
AY692938 Genomic DNA. Translation: AAT92957.1.
BK006939 Genomic DNA. Translation: DAA07803.1.
PIRiS12498.
RefSeqiNP_011069.1. NM_001179032.1.

3D structure databases

ProteinModelPortaliP22134.
SMRiP22134. Positions 51-291.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36891. 73 interactions.
DIPiDIP-6599N.
MINTiMINT-675790.
STRINGi4932.YER142C.

Proteomic databases

MaxQBiP22134.
PaxDbiP22134.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER142C; YER142C; YER142C.
GeneIDi856885.
KEGGisce:YER142C.

Organism-specific databases

CYGDiYER142c.
SGDiS000000944. MAG1.

Phylogenomic databases

eggNOGiCOG0122.
HOGENOMiHOG000113466.
InParanoidiP22134.
KOiK01247.
OMAiWSAKMFA.
OrthoDBiEOG78SQVJ.

Enzyme and pathway databases

BioCyciYEAST:G3O-30303-MONOMER.

Miscellaneous databases

NextBioi983278.

Gene expression databases

GenevestigatoriP22134.

Family and domain databases

Gene3Di1.10.1670.10. 2 hits.
1.10.340.30. 1 hit.
InterProiIPR000035. Alkylbase_DNA_glycsylse_CS.
IPR011257. DNA_glycosylase.
IPR003265. HhH-GPD_domain.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR023170. HTH_base_excis_C.
[Graphical view]
PfamiPF00730. HhH-GPD. 1 hit.
[Graphical view]
SMARTiSM00478. ENDO3c. 1 hit.
SM00278. HhH1. 1 hit.
[Graphical view]
SUPFAMiSSF48150. SSF48150. 2 hits.
PROSITEiPS00516. ALKYLBASE_DNA_GLYCOS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-11.
  7. "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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMAG_YEAST
AccessioniPrimary (citable) accession number: P22134
Secondary accession number(s): D3DM49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: March 4, 2015
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.