Fig. 4

MUSCLE alignment of the DDE domain in MULE transposases and the impact of mutations. a MUSCLE alignment of the DDE domain in Muta1, MuDR, TED, atMu1, Os3378, Jittery, and Hop. Shaded residues have related physical or chemical properties with darker shading denoting more conservation. Asterisks denote residues conserved in all sequences. b Schematic of the 504 amino acid Muta1 transposase with positions of the putative FLYWCH type zinc finger DNA binding domain (24–92 aa), and DDE triad (residues D214, D283, E419). Designated amino acids were mutated to alanine (A) or to both alanine and phenylalanine (F) resulting in the excision frequencies shown below. See text for details