>Functions associated to the different protein domains
>5|P06134|ADA regulatory protein (Regulatory protein of adaptative response) [Contains: Methylated-DNA--protein-cysteine methyltransferase (EC 2.1.1.63) (O-6-methylguanine-DNA alkyltransferase)]|Escherichia coli|AraC
The N-terminal domain of Ada carries the determinants for specific DNA-binding.
The determinants for RNA-polymerase binding reside in the C-terminal domain of the Ada protein. The activating region of the Ada protein at ada and aidB promoters is probably a positively-charged patch at the Ada C-terminal domain.
The methylated-DNA-protein-cysteine methyltransferase activity is located between residues 170 and 354.
>15|P03021|Arabinose operon regulatory protein|Escherichia coli O157:H7|AraC
The C-terminal domain contain the DNA-binding region and the N-terminal domain is responsible for dimerization and L-arabinose binding.
>100|P23217|HTH-type transcriptional regulator qacR|Staphylococcus aureus subsp. aureus Mu50|TetR
The crystal structure showed that QacR is comprised of nine alpha helices. The first three helices of QacR form a three-helix bundle DNA binding domain and contain the helix-turn-helix motif (alpha-helix2 and alpha-helix3). Helices 4 through 9 form the drug binding/dimerization domain. The drug-binding pocket is composed of residues from all helices of the inducer-binding domain except alpha 9, as well as residues from 8'.
>110|P09377|L-rhamnose operon regulatory protein rhaS|Escherichia coli|AraC
In RhaS, the C-terminal domain is responsible for DNA binding, and it is probable that the N-terminal domain functions in L-rhamnose binding and dimerization of the protein.
>126|P04483|Tetracycline repressor protein class B from transposon Tn10|Escherichia coli|TetR
TetR(B) utilizes the conserved HTH structural motif in binding to tet operator.
>128|P09164|Tetracycline repressor protein class D|Escherichia coli|TetR
The crystal structure of the class TetR(D) shows that this protein forms stable homodimers. The polypeptide chain of each mononer is folded into 10 alpha-helices with connecting turns and loops: (1) The N-terminal three-helix alpha-helices (1, 2 and 3) form the DNA-binding domain including HTH motif. (2) The core of the protein is formed by helices alpha 5 to 10. It is responsible for dimerization (helices alpha 8 and 10 represent the dimerization motif) and constains a binding tunnel that accommodates tetracycline in presence of a divalent cation. (3) The alpha-helix 4 connect the DNA-binding domain to the rigid TetR core.
>416|Q60011|Virginiae butanolide receptor|Streptomyces virginiae|TetR
The C-terminal domain of the BarA protein is essential for binding and effect of the virginiae butanolides (VBs).