ID   OGT_SULAC               Reviewed;         155 AA.
AC   Q4J9C6;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
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=Saci_1260;
OS   Sulfolobus acidocaldarius.
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=2285;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / IFO 15157 / JCM 8929 / NCIB 11770;
RX   PubMed=15995215; DOI=10.1128/JB.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000077; AAY80605.1; -; Genomic_DNA.
DR   RefSeq; YP_255898.1; -.
DR   GeneID; 3473061; -.
DR   GenomeReviews; CP000077_GR; Saci_1260.
DR   KEGG; sai:Saci_1260; -.
DR   NMPDR; fig|330779.3.peg.2139; -.
DR   HOGENOM; Q4J9C6; -.
DR   OMA; Q4J9C6; TRSYGEL.
DR   BioCyc; SACI330779:SACI_1260-MON; -.
DR   BRENDA; 2.1.1.63; 434.
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; 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   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    155       Methylated-DNA--protein-cysteine
FT                                methyltransferase.
FT                                /FTId=PRO_0000139386.
FT   ACT_SITE    119    119       Nucleophile; methyl group acceptor (By
FT                                similarity).
SQ   SEQUENCE   155 AA;  17556 MW;  2840CF5D08773B1D CRC64;
     MIVYGVYNSP LGTITVAKNE RGIIMLDFCD CAERNLVDNS TFTDLFHKFD NYFQGKPVEF
     NETVDLFVNN FRRRVFNEVR RIGWGKVKTY KEIAETLKTS PRAVGMALSK NPVLLIIPCH
     RIIAESGLGG FSRGIELKKK LLELEGVNIE ALVRG
//