Figure 2

Multiple alignment of FH2 and DAD domains of Dictyostelium formins. Amino acid sequences were aligned with ClustalX and the output file was subsequently edited manually. The sequence of the human Diaphanous-related formin 3 has been included for reference. Dashes indicate gaps introduced for optimal alignment. In some places extensive repetitive stretches have been removed and replaced by a figure indicating the number of residues omitted. Residues identical or similar in at least 40% of the sequences are boxed in black or gray, respectively. Secondary structure elements as determined for mouse Dia1 core FH2 domain [12] are indicated on top of the aligned sequences. Color coding denotes the N-terminal knob subdomain (red), three-helix-bundle (blue) and FH2 motif post-containg region (green). Regions involved in the formation of the lasso/post dimer interface, as determined for Bni1p [13] are also indicated, as well as the highly conserved GNY/FMN motif (boxed). Conserved residues discussed in the text are indicated by circles and are numbered consecutively. Below the DAD region triangles indicate conserved residues discussed in the text.