[3] Originally discovered in bacteria, the helix-turn-helix motif is commonly found in repressor proteins and is about 20 amino acids long.
[7] In transcription factors these domains are often found in arrays (usually separated by short linker sequences) and adjacent fingers are spaced at 3 basepair intervals when bound to DNA.
The basic leucine zipper (bZIP) domain is found mainly in eukaryotes and to a limited extent in bacteria.
Consisting of about 110 amino acids, the winged helix (WH) domain has four helices and a two-strand beta-sheet.
The basic helix-loop-helix (bHLH) domain is found in some transcription factors and is characterized by two alpha helices (α-helixes) connected by a loop.
HMG-box domains are found in high mobility group proteins which are involved in a variety of DNA-dependent processes like replication and transcription.
[12] The immunoglobulin domain (InterPro: IPR013783) consists of a beta-sheet structure with large connecting loops, which serve to recognize either DNA major grooves or antigens.
The B3 DBD (InterPro: IPR003340, SCOP 117343) is found exclusively in transcription factors from higher plants and restriction endonucleases EcoRII and BfiI and typically consists of 100-120 residues.
It includes seven beta sheets and two alpha helices, which form a DNA-binding pseudobarrel protein fold.
[17] Related proteins are found in bacterial plant pathogen Ralstonia solanacearum,[18] the fungal endosymbiont Burkholderia rhizoxinica[19] and two as-yet unidentified marine-microorganisms.
[20] The DNA binding code and the structure of the repeat array is conserved between these groups, referred to collectively as the TALE-likes.