Evolution of the B-Block Binding Subunit of TFIIIC That Binds to the Internal Promoter for RNA Polymerase III
Figure 5
Comparison of the primary structures of the bacterial B-block binding proteins with the B-block_TFIIIC motif and other HTH motifs. (a) Clustal Omega alignment of the six bacterial proteins provided in Table 2. The relevant region of the alignment is only shown. Amino acid residues conserved in the alignment are indicated by asterisks, colons, and dots. Clustal Omega was performed also using the six bacterial proteins and each cdd sequence of the B-block_TFIIIC (PF04182), MarR (PF01047), MarR_2 (PF12802), and HTH_27 (PF13463) families. The alignments were reviewed by eye, and motif sequences with marks showing amino acid conservation were placed beneath the alignment constructed first from the bacterial proteins only. The cdd sequences were obtained from the CD-search results. Each of the bacterial names is followed by the GI number (or entry name), aa sequence, and aa positions. HTH motifs are also similarly represented. The B-block_TFIIIC regions are colored in blue (see Table 2). (b) -values of the alignments of bacterial B-block binding proteins with MarR, MarR_2, or HTH_27 in CD-search.
