ID A0A1X9YAR1_9SPHN Unreviewed; 358 AA.
AC A0A1X9YAR1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Transcriptional regulator Ada / DNA-O6-methylguanine--protein-cysteine S-methyltransferase {ECO:0000313|EMBL:ARS25864.1};
GN ORFNames=KC8_00955 {ECO:0000313|EMBL:ARS25864.1};
OS Sphingomonas sp. KC8.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1030157 {ECO:0000313|EMBL:ARS25864.1, ECO:0000313|Proteomes:UP000194475};
RN [1] {ECO:0000313|EMBL:ARS25864.1, ECO:0000313|Proteomes:UP000194475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KC8 {ECO:0000313|EMBL:ARS25864.1};
RA Chen Y.-L., Yu C.-P., Hu A., Lee T.-H., Yang F.-C., Ismail W., Wang P.-H.,
RA Wang C.-H., Goh K.-S., Shih C.-J., Chiang Y.-R.;
RT "Bacteria use an extradiol dioxygenase-mediated pathway to degrade natural
RT estrogens in aquatic ecosystems.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; CP016306; ARS25864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X9YAR1; -.
DR STRING; 1030157.GCA_000214335_02279; -.
DR KEGG; spkc:KC8_00955; -.
DR eggNOG; COG0350; Bacteria.
DR eggNOG; COG2169; Bacteria.
DR Proteomes; UP000194475; Chromosome.
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:InterPro.
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:InterPro.
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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
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:SF14; BIFUNCTIONAL TRANSCRIPTIONAL ACTIVATOR_DNA REPAIR ENZYME ADA; 1.
DR PANTHER; PTHR10815; 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 Pfam; PF02870; Methyltransf_1N; 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; SSF46689; Homeodomain-like; 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.
PE 4: Predicted;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000409-3};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ARS25864.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000194475};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000313|EMBL:ARS25864.1};
KW Zinc {ECO:0000256|PIRSR:PIRSR000409-3}.
FT DOMAIN 98..194
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT ACT_SITE 51
FT /note="Nucleophile; methyl group acceptor from
FT methylphosphotriester"
FT /evidence="ECO:0000256|PIRSR:PIRSR000409-1"
FT ACT_SITE 328
FT /note="Nucleophile; methyl group acceptor from either O6-
FT methylguanine or O4-methylthymine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000409-1"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000409-3"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000409-3"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000409-3"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR000409-3"
SQ SEQUENCE 358 AA; 38315 MW; F50C8BB45022AB37 CRC64;
MPLPHIRRMS QIESYPEAAI DAEAAWAAVL RRDREQDGRF VTGVMTTGIY CRPSCAARHP
RRENVRFFRD GTTARAAGLR ACRRCLPDDV ARDEAGITRA LAFMAAAEDP PSLDAVAAAA
GYAPHHFLRL FRRATGLTPA AYVRALRARR VGAILQESDT VTEALYDAGY GAPARFYADA
PARLGMTPSA WRNGGRGVTI RWAIAPTSLG QMLVAATERG ICRLSFGEDE TVLAERFPHA
DIAPGEAGLT ELVARTIAAV ESPQRPHDLP LDVQGTAFQE AVWRELSRIP AGETLSYAAL
AARVGKPGAA RAAGSACGAN NVAILIPCHR AKRGDGTLGG YAYGLAIKTE LLARESKG
//
