Figure 3

(A) Multiple sequence alignments of the α-helical region of an ultraspiracle ligand binding domain from Drosophila (ULBD), α-helix of a conserved hypothetical protein from C. tepidum (CHPfCT), and the eh1 motifs of human FoxB1, murine FoxB2 and amphioxus FoxE4 proteins, which have a high likelihood of α-helix formation. (B) Sequence alignment for the α-helical region of the Hepatitis C Virus RNA Polymerase Genotype 2a (HCVRPG) and the eh1 motif of the cnidarian Fox1 protein. The defined α-helices are represented as red solid boxes and predicted α-helices are shown as red dotted boxes. Amino acid similarities are shown in yellow. hum, Human; mus, Mouse; amp, amphioxus; nem, Sea Anemone. Wheel models of the eh1-like motifs of Xenopus FoxB1 (C) and amphioxus FoxE4 (D) form an amphipathic α-helical structure. Hydrophobic residues on the wheel are shown in the red, hydrophilic residues are shown in the blue, and non-charged residues are shown in the gray.