GenomeNet

Database: UniProt
Entry: B2T7R1_PARPJ
LinkDB: B2T7R1_PARPJ
Original site: B2T7R1_PARPJ 
ID   B2T7R1_PARPJ            Unreviewed;       391 AA.
AC   B2T7R1;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   24-JAN-2024, entry version 109.
DE   SubName: Full=Transcriptional regulator, AraC family {ECO:0000313|EMBL:ACD18342.1};
DE            EC=2.1.1.63 {ECO:0000313|EMBL:ACD18342.1};
GN   OrderedLocusNames=Bphyt_3955 {ECO:0000313|EMBL:ACD18342.1};
OS   Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS   (Burkholderia phytofirmans).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=398527 {ECO:0000313|EMBL:ACD18342.1, ECO:0000313|Proteomes:UP000001739};
RN   [1] {ECO:0000313|EMBL:ACD18342.1, ECO:0000313|Proteomes:UP000001739}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17436 / LMG 22146 / PsJN
RC   {ECO:0000313|Proteomes:UP000001739};
RX   PubMed=21551308; DOI=10.1128/JB.05055-11;
RA   Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.;
RT   "Complete genome sequence of the plant growth-promoting endophyte
RT   Burkholderia phytofirmans strain PsJN.";
RL   J. Bacteriol. 193:3383-3384(2011).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001052; ACD18342.1; -; Genomic_DNA.
DR   RefSeq; WP_012434857.1; NC_010681.1.
DR   AlphaFoldDB; B2T7R1; -.
DR   STRING; 398527.Bphyt_3955; -.
DR   KEGG; bpy:Bphyt_3955; -.
DR   eggNOG; COG0350; Bacteria.
DR   eggNOG; COG2169; Bacteria.
DR   HOGENOM; CLU_000445_52_0_4; -.
DR   OMA; ALTGYHW; -.
DR   OrthoDB; 9802228at2; -.
DR   Proteomes; UP000001739; Chromosome 1.
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: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; 3.40.10.10; 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; 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: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.
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:ACD18342.1};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACD18342.1};
KW   Zinc {ECO:0000256|PIRSR:PIRSR000409-3}.
FT   DOMAIN          93..190
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   REGION          360..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..391
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        46
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         46
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000409-3"
FT   BINDING         50
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000409-3"
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000409-3"
FT   BINDING         80
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000409-3"
SQ   SEQUENCE   391 AA;  42141 MW;  3F3633F7C2EB95DC CRC64;
     MNRKSTDTAA AASWTCDDAR WEAVTHRESQ ADGAFFYAVK TTGVFCRPSC ASRLPRRENV
     AFFTDAAAAR AAGFRDCKRC QPGGLPRELE IVNRACAALD ADPQERLTLA QLSDAVHVSP
     FHLQRLFKRV VGVSPRQYQA AQRGAALRDA LQSGSDVTRA TLDAGFGSPS RMYDSASAEL
     GMAPSAYRRK GAGLIVRYAS APTSLGHVLV AATEKGICKI GFGDDKAMLA DDLRGEFANA
     DVLEDPEHMA PFIAQIDAYL RGTRQDFDLP LDIASTAFRQ RVWDALRRIP YGETRSYSQI
     AETVGAPRAV RAVASACATN PVALAIPCHR VVAKGGALAG YRWGLPRKAA LLDNEAQHAG
     DFSGGQAERN RRADADSDLD IKTTTKLDHA A
//
DBGET integrated database retrieval system