(data stored in ACNUC7421 zone)

SWISSPROT: OGT_SULIK

ID   OGT_SULIK               Reviewed;         151 AA.
AC   C4KKV8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   30-AUG-2017, entry version 49.
DE   RecName: Full=Methylated-DNA--protein-cysteine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00772};
DE            EC=2.1.1.63 {ECO:0000255|HAMAP-Rule:MF_00772};
DE   AltName: Full=6-O-methylguanine-DNA methyltransferase {ECO:0000255|HAMAP-Rule:MF_00772};
DE            Short=MGMT {ECO:0000255|HAMAP-Rule:MF_00772};
DE   AltName: Full=O-6-methylguanine-DNA-alkyltransferase {ECO:0000255|HAMAP-Rule:MF_00772};
GN   Name=ogt {ECO:0000255|HAMAP-Rule:MF_00772};
GN   OrderedLocusNames=M164_0289;
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- FUNCTION: Involved in the cellular defense against the biological
CC       effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT)
CC       in DNA. Repairs the methylated nucleobase in DNA by
CC       stoichiometrically transferring the methyl group to a cysteine
CC       residue in the enzyme. This is a suicide reaction: the enzyme is
CC       irreversibly inactivated. {ECO:0000255|HAMAP-Rule:MF_00772}.
CC   -!- CATALYTIC ACTIVITY: DNA (containing 6-O-methylguanine) + protein
CC       L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-
CC       cysteine. {ECO:0000255|HAMAP-Rule:MF_00772}.
CC   -!- CATALYTIC ACTIVITY: DNA (containing 4-O-methylthymine) + protein
CC       L-cysteine = DNA (without 4-O-methylthymine) + protein S-methyl-L-
CC       cysteine. {ECO:0000255|HAMAP-Rule:MF_00772}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00772}.
CC   -!- MISCELLANEOUS: This enzyme catalyzes only one turnover and
CC       therefore is not strictly catalytic. According to one definition,
CC       an enzyme is a biocatalyst that acts repeatedly and over many
CC       reaction cycles.
CC   -!- SIMILARITY: Belongs to the MGMT family. {ECO:0000255|HAMAP-
CC       Rule:MF_00772}.
DR   EMBL; CP001402; ACR40923.1; -; Genomic_DNA.
DR   RefSeq; WP_010923891.1; NC_012726.1.
DR   ProteinModelPortal; C4KKV8; -.
DR   SMR; C4KKV8; -.
DR   EnsemblBacteria; ACR40923; ACR40923; M164_0289.
DR   GeneID; 8760125; -.
DR   KEGG; sid:M164_0289; -.
DR   HOGENOM; HOG000244137; -.
DR   KO; K00567; -.
DR   OMA; YGESRSY; -.
DR   OrthoDB; POG093Z0E1E; -.
DR   BioCyc; SISL426118:GI01-291-MONOMER; -.
DR   Proteomes; UP000001479; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   CDD; cd06445; ATase; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   HAMAP; MF_00772; OGT; 1.
DR   InterPro; IPR001497; MethylDNA_cys_MeTrfase_AS.
DR   InterPro; IPR014048; MethylDNA_cys_MeTrfase_DNA-bd.
DR   InterPro; IPR008332; MethylG_MeTrfase_N.
DR   InterPro; IPR023546; MGMT.
DR   InterPro; IPR011991; WHTH_DNA-bd_dom.
DR   Pfam; PF01035; DNA_binding_1; 1.
DR   SUPFAM; SSF46767; SSF46767; 1.
DR   SUPFAM; SSF53155; SSF53155; 1.
DR   TIGRFAMs; TIGR00589; ogt; 1.
DR   PROSITE; PS00374; MGMT; 1.
PE   3: Inferred from homology;
DR   PRODOM; C4KKV8.
DR   SWISS-2DPAGE; C4KKV8.
KW   Complete proteome; Cytoplasm; DNA damage; DNA repair;
KW   Methyltransferase; Transferase.
FT   CHAIN         1    151       Methylated-DNA--protein-cysteine
FT                                methyltransferase.
FT                                /FTId=PRO_1000212902.
FT   ACT_SITE    119    119       Nucleophile; methyl group acceptor.
FT                                {ECO:0000255|HAMAP-Rule:MF_00772}.
SQ   SEQUENCE   151 AA;  17037 MW;  8457864CD5BC8F99 CRC64;
     MLVYGLYKSP LGYITVAKDD KGFIMLDFCD CVEGNSRDDS SFTEFFHKLD LYFEGKPINL
     REPINLKTYP FRLSVFKEVM KIPWGKVMTY KQIADSLGTS PRAVGMALSK NPILLIIPCH
     RVIAENGIGG YSRGVKLKRA LLELEGVKIP E
//

If you have problems or comments...

PBIL Back to PBIL home page