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MGMT_LODEL
ID   MGMT_LODEL              Reviewed;         201 AA.
AC   A5E7M8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Methylated-DNA--protein-cysteine methyltransferase;
DE            EC=2.1.1.63;
DE   AltName: Full=6-O-methylguanine-DNA methyltransferase;
DE            Short=MGMT;
DE   AltName: Full=DNA repair MTase;
DE   AltName: Full=O-6-methylguanine-DNA-alkyltransferase;
GN   Name=MGT1; ORFNames=LELG_05617;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- FUNCTION: Involved in the cellular defense against the biological
CC       effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in
CC       DNA. Repairs the methylated nucleobase in DNA by stoichiometrically
CC       transferring the methyl group to a cysteine residue in the enzyme. This
CC       is a suicide reaction: the enzyme is irreversibly inactivated.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein]
CC         = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-[protein];
CC         Xref=Rhea:RHEA:24000, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132,
CC         Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:11368, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:82612, ChEBI:CHEBI:85445, ChEBI:CHEBI:85448; EC=2.1.1.63;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10017};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a
CC         thymidine in DNA + S-methyl-L-cysteinyl-[protein];
CC         Xref=Rhea:RHEA:53428, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132,
CC         Rhea:RHEA-COMP:13555, Rhea:RHEA-COMP:13556, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:82612, ChEBI:CHEBI:137386, ChEBI:CHEBI:137387;
CC         EC=2.1.1.63; Evidence={ECO:0000255|PROSITE-ProRule:PRU10017};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- MISCELLANEOUS: This enzyme catalyzes only one turnover and therefore is
CC       not strictly catalytic. According to one definition, an enzyme is a
CC       biocatalyst that acts repeatedly and over many reaction cycles.
CC   -!- SIMILARITY: Belongs to the MGMT family. {ECO:0000305}.
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DR   EMBL; CH981534; EDK47436.1; -; Genomic_DNA.
DR   RefSeq; XP_001523071.1; XM_001523021.1.
DR   AlphaFoldDB; A5E7M8; -.
DR   SMR; A5E7M8; -.
DR   STRING; 379508.A5E7M8; -.
DR   EnsemblFungi; EDK47436; EDK47436; LELG_05617.
DR   GeneID; 5230165; -.
DR   KEGG; lel:LELG_05617; -.
DR   VEuPathDB; FungiDB:LELG_05617; -.
DR   eggNOG; KOG4062; Eukaryota.
DR   HOGENOM; CLU_000445_52_2_1; -.
DR   InParanoid; A5E7M8; -.
DR   OMA; TFIETEV; -.
DR   OrthoDB; 1573162at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IEA:UniProt.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd06445; ATase; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR001497; MethylDNA_cys_MeTrfase_AS.
DR   InterPro; IPR014048; MethylDNA_cys_MeTrfase_DNA-bd.
DR   InterPro; IPR036217; MethylDNA_cys_MeTrfase_DNAb.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF01035; DNA_binding_1; 1.
DR   SUPFAM; SSF46767; SSF46767; 1.
DR   TIGRFAMs; TIGR00589; ogt; 1.
DR   PROSITE; PS00374; MGMT; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; DNA-binding; Methyltransferase; Nucleus;
KW   Reference proteome; Transferase.
FT   CHAIN           1..201
FT                   /note="Methylated-DNA--protein-cysteine methyltransferase"
FT                   /id="PRO_0000333686"
FT   ACT_SITE        163
FT                   /note="Nucleophile; methyl group acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10017"
FT   BINDING         131
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         146
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   201 AA;  22686 MW;  87415A5DA7D4894F CRC64;
     MLVKTLYYRL VEGTFAKAML VLDEKGTLYY ASLGEDSNAL RETLVTDFAS KQRQFQLKPM
     VTLSNHERAD YTALCFLKLM EEEEDWKNEG EESLQQKGAK RIPIEFIFGT ELQRKVWQQL
     LEIPVGEVRY YGNIVEALGL PKSASRAVGN ACGANKIALV VPCHRVIAQT GKLTGYRWGL
     ATKKQILKME LGDAYTTLVS E
 
 
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