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MULTISPECIES: bifunctional transcriptional activator/DNA repair


LOCUS       WP_004151500             352 aa            linear   BCT 19-FEB-2025
            enzyme AdaA [Klebsiella].
ACCESSION   WP_004151500
VERSION     WP_004151500.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Aravind,L., Anantharaman,V., Balaji,S., Babu,M.M. and Iyer,L.M.
  TITLE     The many faces of the helix-turn-helix domain: transcription
            regulation and beyond
  JOURNAL   FEMS Microbiol Rev 29 (2), 231-262 (2005)
   PUBMED   15808743
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Rosinski,J.A. and Atchley,W.R.
  TITLE     Molecular evolution of helix-turn-helix proteins
  JOURNAL   J Mol Evol 49 (3), 301-309 (1999)
   PUBMED   10473770
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Wintjens,R. and Rooman,M.
  TITLE     Structural classification of HTH DNA-binding domains and
            protein-DNA interaction modes
  JOURNAL   J Mol Biol 262 (2), 294-313 (1996)
   PUBMED   8831795
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Morohoshi,F., Hayashi,K. and Munakata,N.
  TITLE     Molecular analysis of Bacillus subtilis ada mutants deficient in
            the adaptive response to simple alkylating agents
  JOURNAL   J Bacteriol 173 (24), 7834-7840 (1991)
   PUBMED   1744039
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Morohoshi,F., Hayashi,K. and Munakata,N.
  TITLE     Bacillus subtilis ada operon encodes two DNA alkyltransferases
  JOURNAL   Nucleic Acids Res 18 (18), 5473-5480 (1990)
   PUBMED   2120677
REFERENCE   6  (residues 1 to 352)
  AUTHORS   Brennan,R.G. and Matthews,B.W.
  TITLE     The helix-turn-helix DNA binding motif
  JOURNAL   J Biol Chem 264 (4), 1903-1906 (1989)
   PUBMED   2644244
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 11450612
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..352
                     /product="bifunctional transcriptional activator/DNA
                     repair enzyme AdaA"
                     /EC_number="2.1.1.-"
                     /GO_function="GO:0003677 - DNA binding [Evidence IEA]"
                     /GO_function="GO:0003700 - DNA-binding transcription
                     factor activity [Evidence IEA]"
                     /GO_function="GO:0008168 - methyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006281 - DNA repair [Evidence IEA]"
                     /GO_process="GO:0032259 - methylation [Evidence IEA]"
                     /calculated_mol_wt=39695
     Region          3..351
                     /region_name="AdaA"
                     /note="Methylphosphotriester-DNA--protein-cysteine
                     methyltransferase (N-terminal fragment of Ada), contains
                     Zn-binding and two AraC-type DNA-binding domains
                     [Replication, recombination and repair]; COG2169"
                     /db_xref="CDD:441772"
ORIGIN      
        1 mkitdsmqcd iwyqallera veftgvffvg vkttgvfcis vcrarkprre nvefyndfks
       61 aldagfrpck vcrptenart apafveqalr llreapkvrl sdselrqhdi spervrrwfl
      121 qnhgitfqaf qrmqrlnmal qelkagrstt dvafdsgyes lsgfgytckk ltgfapsaqr
      181 qvvlihrftt plgpmfvcat qrgicllefv drralesefs dlqrrfnasi iagenahtrq
      241 aqqeiteyfa gqrqsfeval dtpgsefqra vwrrlqhvsf getthyqsia meigkptatr
      301 avaaanganr vaiiipchri igkdgsmtgy gggiarkiwl inheatirek rg