ID A0A0Q4FRS0_9SPHN Unreviewed; 351 AA.
AC A0A0Q4FRS0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=6-O-methylguanine DNA methyltransferase {ECO:0000313|EMBL:KQM63430.1};
GN ORFNames=ASE75_13390 {ECO:0000313|EMBL:KQM63430.1};
OS Sphingomonas sp. Leaf17.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1735683 {ECO:0000313|EMBL:KQM63430.1, ECO:0000313|Proteomes:UP000051777};
RN [1] {ECO:0000313|EMBL:KQM63430.1, ECO:0000313|Proteomes:UP000051777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf17 {ECO:0000313|EMBL:KQM63430.1,
RC ECO:0000313|Proteomes:UP000051777};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM63430.1, ECO:0000313|Proteomes:UP000051777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf17 {ECO:0000313|EMBL:KQM63430.1,
RC ECO:0000313|Proteomes:UP000051777};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR000409-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000409-3};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQM63430.1}.
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DR EMBL; LMKL01000008; KQM63430.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q4FRS0; -.
DR STRING; 1735683.ASE75_13390; -.
DR OrthoDB; 9802228at2; -.
DR Proteomes; UP000051777; Unassembled WGS sequence.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; 3.40.10.10; DNA Methylphosphotriester Repair Domain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 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; IPR035451; Ada-like_dom_sf.
DR InterPro; IPR004026; Ada_DNA_repair_Zn-bd.
DR InterPro; IPR016221; Bifunct_regulatory_prot_Ada.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR001497; MethylDNA_cys_MeTrfase_AS.
DR InterPro; IPR014048; MethylDNA_cys_MeTrfase_DNA-bd.
DR InterPro; IPR036217; MethylDNA_cys_MeTrfase_DNAb.
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:SF5; METHYLATED-DNA--PROTEIN-CYSTEINE METHYLTRANSFERASE; 1.
DR Pfam; PF02805; Ada_Zn_binding; 1.
DR Pfam; PF01035; DNA_binding_1; 1.
DR Pfam; PF12833; HTH_18; 1.
DR PIRSF; PIRSF000409; Ada; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SUPFAM; SSF57884; Ada DNA repair protein, N-terminal domain (N-Ada 10); 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; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS00374; MGMT; 1.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW DNA damage {ECO:0000256|ARBA:ARBA00023204};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000409-3};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KQM63430.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051777};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KQM63430.1};
KW Zinc {ECO:0000256|PIRSR:PIRSR000409-3}.
FT DOMAIN 81..181
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT ACT_SITE 37
FT /note="Nucleophile; methyl group acceptor from
FT methylphosphotriester"
FT /evidence="ECO:0000256|PIRSR:PIRSR000409-1"
FT ACT_SITE 319
FT /note="Nucleophile; methyl group acceptor from either O6-
FT methylguanine or O4-methylthymine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000409-1"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000409-3"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000409-3"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000409-3"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000409-3"
SQ SEQUENCE 351 AA; 37993 MW; 135280CB2584C415 CRC64;
MTTTLPADDI LYAALLARDP AYDGHAFVGV TTTGIFCRLS CPARKPLFEN TRYFDSVAAC
YTAGFRPCLR CRPVAQVGAR EPVVAMLMAR LDAEPDRVWS EEDLIALDLD PSTVRRAFRR
HIGTTFLDLA RLRRAGRGVD RIAGGASVID AQIEAGYDSG SGFRDAVIRL IGDAPAALRG
TPLLTADWIE TPLGAMLAIA DATHLHLLEF FDRKALPEGL ARLRQRTGAA IVFGRTPPID
RIAAELSTYF DGTDARFTGP IAAHAAADFT ASVWTALQTI PPGETRSYSA LATTIGRPSA
VRALARANGA NQLAIVIPCH RVIGADGTLT GYAGGLWRKR WLIEHERRHF A
//
