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Database: UniProt
Entry: A0A1T4T2U3_9ACTN
LinkDB: A0A1T4T2U3_9ACTN
Original site: A0A1T4T2U3_9ACTN 
ID   A0A1T4T2U3_9ACTN        Unreviewed;       226 AA.
AC   A0A1T4T2U3;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Methylated-DNA-[protein]-cysteine S-methyltransferase {ECO:0000313|EMBL:SKA34795.1};
GN   ORFNames=SAMN02745673_04394 {ECO:0000313|EMBL:SKA34795.1};
OS   Marinactinospora thermotolerans DSM 45154.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Marinactinospora.
OX   NCBI_TaxID=1122192 {ECO:0000313|EMBL:SKA34795.1, ECO:0000313|Proteomes:UP000190637};
RN   [1] {ECO:0000313|EMBL:SKA34795.1, ECO:0000313|Proteomes:UP000190637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45154 {ECO:0000313|EMBL:SKA34795.1,
RC   ECO:0000313|Proteomes:UP000190637};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001286};
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:0000256|ARBA:ARBA00001596};
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DR   EMBL; FUWS01000013; SKA34795.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4T2U3; -.
DR   STRING; 1122192.SAMN02745673_04394; -.
DR   OrthoDB; 9802228at2; -.
DR   Proteomes; UP000190637; Unassembled WGS sequence.
DR   GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006304; P:DNA modification; IEA:UniProt.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd06445; ATase; 1.
DR   Gene3D; 3.30.160.70; Methylated DNA-protein cysteine methyltransferase domain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; IPR036631; MGMT_N_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   NCBIfam; TIGR00589; ogt; 1.
DR   PANTHER; PTHR10815; METHYLATED-DNA--PROTEIN-CYSTEINE METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10815:SF13; METHYLATED-DNA--PROTEIN-CYSTEINE METHYLTRANSFERASE; 1.
DR   Pfam; PF01035; DNA_binding_1; 1.
DR   Pfam; PF02870; Methyltransf_1N; 1.
DR   SUPFAM; SSF53155; Methylated DNA-protein cysteine methyltransferase domain; 1.
DR   SUPFAM; SSF46767; Methylated DNA-protein cysteine methyltransferase, C-terminal domain; 1.
DR   PROSITE; PS00374; MGMT; 1.
PE   4: Predicted;
KW   DNA damage {ECO:0000256|ARBA:ARBA00023204};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:SKA34795.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190637};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SKA34795.1}.
FT   DOMAIN          53..124
FT                   /note="Methylguanine DNA methyltransferase ribonuclease-
FT                   like"
FT                   /evidence="ECO:0000259|Pfam:PF02870"
FT   DOMAIN          130..187
FT                   /note="Methylated-DNA-[protein]-cysteine S-
FT                   methyltransferase DNA binding"
FT                   /evidence="ECO:0000259|Pfam:PF01035"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          207..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   226 AA;  24299 MW;  CC77C2A59FAA4CA2 CRC64;
     MTKTWSEERP GDPDLGGDLD ALIRATSSCP PPPPAPPRRS ALPREALDVV TGTVETPIGV
     LSLALTRRGL VSCSFDAEET VLPRLARAVS PRIGAHEAGL DPVRRELDAY FDGRLTSFTI
     PLDLRLTSDF GRLVLRSLLD VEHGTTTTHG RLAARIGRGR AIRAVASSLA TNPVCVLLPC
     HRVVPEDYPE DTGPYAGAPR PNASCWGWRR SPRPAPIRGR GGAGHR
//
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