ID   OGT_METBF               Reviewed;         158 AA.
AC   Q46EW4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=O-6-methylguanine-DNA-alkyltransferase;
GN   Name=ogt; OrderedLocusNames=Mbar_A0598;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980466; DOI=10.1128/JB.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P.,
RA   Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R.,
RA   Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
CC   -!- FUNCTION: Involved in the cellular defense against the biological
CC       effects of O6-methylguanine (O6-MeG) in DNA. Repairs alkylated
CC       guanine in DNA by stoichiometrically transferring the alkyl group
CC       at the O-6 position to a cysteine residue in the enzyme. This is a
CC       suicide reaction: the enzyme is irreversibly inactivated (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: DNA (containing 6-O-methylguanine) + protein
CC       L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-
CC       cysteine.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the MGMT family.
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DR   EMBL; CP000099; AAZ69578.1; -; Genomic_DNA.
DR   RefSeq; YP_304158.1; -.
DR   GeneID; 3627658; -.
DR   GenomeReviews; CP000099_GR; Mbar_A0598.
DR   KEGG; mba:Mbar_A0598; -.
DR   NMPDR; fig|269797.3.peg.781; -.
DR   HOGENOM; Q46EW4; -.
DR   OMA; Q46EW4; GAMRGNP.
DR   BioCyc; MBAR269797:MBAR_A0598-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methylt...; IEA:HAMAP.
DR   GO; GO:0006307; P:DNA dealkylation; IEA:HAMAP.
DR   HAMAP; MF_00772; -; 1.
DR   InterPro; IPR001497; MethylDNA_cys_MeTrfase_AS.
DR   InterPro; IPR014048; MethylDNA_cys_MeTrfase_DNA_bd.
DR   InterPro; IPR008332; MethylG_MeTrfase.
DR   InterPro; IPR011991; Wing_hlx_DNA_bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   PANTHER; PTHR10815; MethylDNA_cys_mtrans_DNA_bd; 1.
DR   Pfam; PF01035; DNA_binding_1; 1.
DR   Pfam; PF02870; Methyltransf_1N; 1.
DR   TIGRFAMs; TIGR00589; ogt; 1.
DR   PROSITE; PS00374; MGMT; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; DNA damage; DNA repair;
KW   Methyltransferase; Transferase.
FT   CHAIN         1    158       Methylated-DNA--protein-cysteine
FT                                methyltransferase.
FT                                /FTId=PRO_1000017350.
FT   ACT_SITE    126    126       Nucleophile; methyl group acceptor (By
FT                                similarity).
SQ   SEQUENCE   158 AA;  17887 MW;  9512FB5BCCECD850 CRC64;
     MYYDIIESPI GPILLAGNEK GLKHLDFLKG KKRIEIPADW IENKKFFREA ARQLEAYFSG
     KLESFDLKLA PEGTDFQKSV WKALCEIPYG ETRTYKEIAV SIGKPRAYRA VGLANNRNPI
     AIIIPCHRVI GSDGKLTGYA SGLDIKEFLL KLEENNLR
//