Figure 1

Comparison of Vps25 amino acid sequences. A multiple alignment of 119 Vps25 homologs was generated using ClustalX. Only the amino-terminal region (top) and carboxy-terminal region (bottom) of an abridged number of species is presented here. A full alignment of all known Vps25 homologs can be found in Additional File 18. Amino acid numbering is to the left of aligned sequences. Consensus amino acid sequences (obtained from the alignment of Vps25 from all species) are found below the alignment, where an uppercase letter represent the only completely conserved amino acid in the regions aligned [see Additional File 18]. Shading was done using Boxshade, where regions of greater than 50% conservation in the total alignment [Additional File 18] are shaded (identical amino acids are in black boxes and similar amino acids in gray boxes). Protein accession numbers are found in Additional File 1. Gaps that were required for optimal alignment of the full length Vps25 homologs are indicated by dashes. Standard single letter amino acid abbreviations are used. The secondary structure elements of yeast Vps25p are provided beneath the alignment. The two 3/10 helices (η1 and η2) prior to the first winged helix (WH domain) and the first alpha helix (α1) of WH-1 are in the aligned amino-terminal region, while helix (H2) and the final two beta strands (B2 and B3) of WH-2 are in the aligned carboxy-terminal region. An asterisk indicates the position of a highly conserved lysine residue close to the carboxy-terminus.