(data stored in ACNUC7421 zone)

SWISSPROT: Q47T13_THEFY

ID   Q47T13_THEFY            Unreviewed;       231 AA.
AC   Q47T13;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 91.
DE   RecName: Full=Methylated-DNA--protein-cysteine methyltransferase {ECO:0000256|HAMAP-Rule:MF_00772};
DE            EC=2.1.1.63 {ECO:0000256|HAMAP-Rule:MF_00772};
DE   AltName: Full=6-O-methylguanine-DNA methyltransferase {ECO:0000256|HAMAP-Rule:MF_00772};
DE            Short=MGMT {ECO:0000256|HAMAP-Rule:MF_00772};
DE   AltName: Full=O-6-methylguanine-DNA-alkyltransferase {ECO:0000256|HAMAP-Rule:MF_00772};
GN   OrderedLocusNames=Tfu_0366 {ECO:0000313|EMBL:AAZ54404.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54404.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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:0000256|HAMAP-Rule:MF_00772}.
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-
CC         COMP:10132, Rhea:RHEA-COMP:13555, Rhea:RHEA-COMP:13556,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:82612, ChEBI:CHEBI:137386,
CC         ChEBI:CHEBI:137387; EC=2.1.1.63; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00772};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-
CC         [protein] = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-
CC         [protein]; Xref=Rhea:RHEA:24000, Rhea:RHEA-COMP:10131,
CC         Rhea:RHEA-COMP:10132, Rhea:RHEA-COMP:11367, Rhea:RHEA-
CC         COMP:11368, ChEBI:CHEBI:29950, ChEBI:CHEBI:82612,
CC         ChEBI:CHEBI:85445, ChEBI:CHEBI:85448; EC=2.1.1.63;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00772};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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. {ECO:0000256|HAMAP-Rule:MF_00772}.
CC   -!- SIMILARITY: Belongs to the MGMT family. {ECO:0000256|HAMAP-
CC       Rule:MF_00772}.
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DR   EMBL; CP000088; AAZ54404.1; -; Genomic_DNA.
DR   RefSeq; WP_011290813.1; NC_007333.1.
DR   STRING; 269800.Tfu_0366; -.
DR   EnsemblBacteria; AAZ54404; AAZ54404; Tfu_0366.
DR   KEGG; tfu:Tfu_0366; -.
DR   eggNOG; ENOG4105K85; Bacteria.
DR   eggNOG; COG0350; LUCA.
DR   HOGENOM; HOG000244137; -.
DR   KO; K00567; -.
DR   OMA; NPKSCRA; -.
DR   OrthoDB; 1327994at2; -.
DR   BioCyc; TFUS269800:G1G4Q-368-MONOMER; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IEA:UniProtKB-UniRule.
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; IPR036217; MethylDNA_cys_MeTrfase_DNAb.
DR   InterPro; IPR008332; MethylG_MeTrfase_N.
DR   InterPro; IPR023546; MGMT.
DR   InterPro; IPR036631; MGMT_N_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF01035; DNA_binding_1; 1.
DR   Pfam; PF02870; Methyltransf_1N; 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; Q47T13.
DR   SWISS-2DPAGE; Q47T13.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00772};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00772};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00772};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00772,
KW   ECO:0000313|EMBL:AAZ54404.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00772,
KW   ECO:0000313|EMBL:AAZ54404.1}.
FT   DOMAIN       48    115       Methyltransf_1N. {ECO:0000259|Pfam:
FT                                PF02870}.
FT   DOMAIN      119    198       DNA_binding_1. {ECO:0000259|Pfam:
FT                                PF01035}.
FT   ACT_SITE    170    170       Nucleophile; methyl group acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00772}.
SQ   SEQUENCE   231 AA;  24633 MW;  F972C1CA6120C305 CRC64;
     MRCRAENSLS PPLPHRRTPD TGTSTPAPRT HQGVIVTAEI PARARVHTVV DSPLGPLTLV
     AADGALVGLY QEDQRHRPAP DSFGVPDPAP FTEVIAQLTE YFSGQRTVFD LPLAFTGTPF
     QTTVWRALLE IPYGQTVSYG ELAARIGKPS ASRAVGLANG RNPISIIVPC HRVVGSSGSL
     TGYGGGLARK QWLLALEQRR AHQPPLLDFA DGLDAGEPRS ATLPMGSHHS A
//

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