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UniProtKB/Swiss-Prot entry P26188


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MGMT_YEAST
Primary accession number P26188
Secondary accession numbers None
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on May 20, 2008 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 77)
Name and origin of the protein
Protein name Methylated-DNA--protein-cysteine methyltransferase
Synonyms EC 2.1.1.63
6-O-methylguanine-DNA methyltransferase
MGMT
DNA repair MTase
O-6-methylguanine-DNA-alkyltransferase
Gene name
Name: MGT1
OrderedLocusNames: YDL200C
ORFNames: D1204
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=2065659 [NCBI, ExPASy, EBI, Israel, Japan]
Xiao W., Derfler B., Chen J., Samson L.;
"Primary sequence and biological functions of a Saccharomyces cerevisiae O6-methylguanine/O4-methylthymine DNA repair methyltransferase gene.";
EMBO J. 10:2179-2186(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
STRAIN=ATCC 44774 / DBY747;
DOI=10.1093/nar/20.14.3599; PubMed=1641326 [NCBI, ExPASy, EBI, Israel, Japan]
Xiao W., Samson L.;
"The Saccharomyces cerevisiae MGT1 DNA repair methyltransferase gene: its promoter and entire coding sequence, regulation and in vivo biological functions.";
Nucleic Acids Res. 20:3599-3606(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
DOI=10.1002/(SICI)1097-0061(199702)13:2<163::AID-YEA54>3.3.CO;2-W; PubMed=9046097 [NCBI, ExPASy, EBI, Israel, Japan]
Bahr A., Moeller-Rieker S., Hankeln T., Kraemer C., Protin U., Schmidt E.R.;
"The nucleotide sequence of a 39 kb segment of yeast chromosome IV: 12 new open reading frames, nine known genes and one gene for Gly-tRNA.";
Yeast 13:163-169(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169867 [NCBI, ExPASy, EBI, Israel, Japan]
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
STRAIN=ATCC 96604 / S288c / FY1679;
DOI=10.1002/(SICI)1097-0061(199609)12:10B<1065::AID-YEA995>3.3.CO;2-6; PubMed=8896272 [NCBI, ExPASy, EBI, Israel, Japan]
Verhasselt P., Voet M., Mathys J., Volckaert G.;
"The sequence of 23 kb surrounding the SNF3 locus on the left arm of yeast chromosome IV reveals the location of five known genes and characterizes at least six new open reading frames including putative genes for ribosomal protein L35 and a sugar transport protein.";
Yeast 12:1065-1070(1996).
[6]
FUNCTION, CHARACTERIZATION, AND LEVEL OF PROTEIN EXPRESSION.
PubMed=2403555 [NCBI, ExPASy, EBI, Israel, Japan]
Sassanfar M., Samson L.;
"Identification and preliminary characterization of an O6-methylguanine DNA repair methyltransferase in the yeast Saccharomyces cerevisiae.";
J. Biol. Chem. 265:20-25(1990).
[7]
FUNCTION.
PubMed=1993655 [NCBI, ExPASy, EBI, Israel, Japan]
Sassanfar M., Dosanjh M.K., Essigmann J.M., Samson L.;
"Relative efficiencies of the bacterial, yeast, and human DNA methyltransferases for the repair of O6-methylguanine and O4-methylthymine.";
J. Biol. Chem. 266:2767-2771(1991).
[8]
INDUCTION.
PubMed=7549791 [NCBI, ExPASy, EBI, Israel, Japan]
Joo J.H., Rho J.K., Kim J.H., Kim W.J., Choe S.Y., Park S.D.;
"Expression of yeast O6-methylguanine-DNA methyltransferase (MGMT) gene.";
Cell. Mol. Biol. 41:545-553(1995).
[9]
IDENTIFICATION OF PROBABLE INITIATION SITE.
DOI=10.1038/nature01644; PubMed=12748633 [NCBI, ExPASy, EBI, Israel, Japan]
Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
"Sequencing and comparison of yeast species to identify genes and regulatory elements.";
Nature 423:241-254(2003).
[10]
IDENTIFICATION OF PROBABLE INITIATION SITE.
DOI=10.1126/science.1084337; PubMed=12775844 [NCBI, ExPASy, EBI, Israel, Japan]
Cliften P.F., Sudarsanam P., Desikan A., Fulton L., Fulton B., Majors J., Waterston R., Cohen B.A., Johnston M.;
"Finding functional features in Saccharomyces genomes by phylogenetic footprinting.";
Science 301:71-76(2003).
Comments
  • FUNCTION: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) in DNA. Repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated. Also repairs O-4-methylthymine. Prefers double-stranded DNA over single-stranded DNA as subtsrate.
  • CATALYTIC ACTIVITY: DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-cysteine.
  • SUBCELLULAR LOCATION: Nucleus.
  • INDUCTION: In contrast to some bacterial and mammalian enzymes, MGT1 is not induced by alkylating agents.
  • MISCELLANEOUS: Present with 150 molecules/cell in log phase YPD medium, but not detectable in stationary phase cells.
  • SIMILARITY: Belongs to the MGMT family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X60368; CAA42920.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M94227; AAA34780.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X99000; CAA67469.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z74248; CAA98778.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z74247; CAA98777.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X83276; CAA58247.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S29370; XUBYMC.
RefSeq NP_010081.2; -.
3D structure databases
HSSP P16455; 1QNT. [HSSP ENTRY / PDB]
ModBase P26188.
Protein-protein interaction databases
DIP DIP:7461N; -.
Organism-specific databases
CYGD YDL200c; -.
SGD S000002359; MGT1.
Yeast-GFP YDL200C.
Gene expression databases
GermOnline YDL200C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003908; Molecular function: methylated-DNA-[protein]-cysteine S-methyltransferase activity (inferred from electronic annotation from InterPro).
GO:0006307; Biological process: DNA dealkylation (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR001497; MethylDNA_cys_MeTrfase_AS.
IPR014048; MethylDNA_cys_MeTrfase_DNA_bd.
IPR008332; MethylG_MeTrfase.
IPR011991; Wing_hlx_DNA_bd.
Graphical view of domain structure.
Gene3D G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
PANTHER PTHR10815; MethylDNA_cys_mtrans_DNA_bd; 1.
Pfam PF01035; DNA_binding_1; 1.
PF02870; Methyltransf_1N; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00589; ogt; 1.
PROSITE PS00374; MGMT; 1.
BLOCKS P26188.
ProtoNet P26188.
Proteomic databases
PeptideAtlas P26188; -.
Genome annotation databases
Ensembl YDL200C; Saccharomyces cerevisiae. [Contig view]
GeneID 851327; -.
GenomeReviews Z71256_GR; YDL200C.
KEGG sce:YDL200C; -.
NMPDR fig|4932.3.peg.814; -.
Phylogenomic databases
HOGENOM P26188; -.
Other
LinkHub P26188; -.
NextBio 968381; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; DNA damage; DNA repair; DNA-binding; Methyltransferase; Nucleus; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   188  188     Methylated-DNA--protein-cysteine methyltransferase. PRO_0000139362
ACT_SITE   151   151        Nucleophile; methyl group acceptor (By similarity). 
BINDING   120   120        DNA (By similarity). 
BINDING   121   121        DNA; via amide nitrogen (By similarity). 
BINDING   134   134        DNA (By similarity). 
BINDING   157   157        DNA; via amide nitrogen (By similarity). 
Sequence information
Length: 188 AA [This is the length of the unprocessed precursor] Molecular weight: 21499 Da [This is the MW of the unprocessed precursor] CRC64: 956E71B47016E47D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKELLYYTFI ETEVTGAFLV FREKTQNLVF ASLGNDKLFL LGKVEGFLKK HEKQDTMYDL 

        70         80         90        100        110        120 
QELKEAETYK KSIENYTICL ENKMPLPSGA IPFEFLFGTD FQRKVWNELL NVEHGHVVTY 

       130        140        150        160        170        180 
GDIAKRIGKP TAARSVGRAC GSNNLALLVP CHRIVGSNRK LTGYKWSCKL KEQLLNNEKE 


NSLSLSRL 

P26188 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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