Figure 3.

Schematic diagrams of the DSX2 structures and its sequence comparison of DM- and oligomerization-domains. (A) Domain structures of the DSX2 of Daphnia magna, and identity with D. pulex, D. galeata and C. dubia. DM- and oligomerization-domains are indicated by black and gray boxes, respectively. (B, C) Alignment of predicted amino acid sequences of DM- and oligomerization-domains of DSX2 from four daphniids, respectively. Amino acid sequences were aligned using CLUSTAL-X. Dotted boxes highlight the conserved threonine (T) and glutamine (Q) residues in DSX2. Asterisks indicate the zinc chelating residues. Position of non-polar amino acids important in formation of the hydrophobic interface between oligomerization-domains in Drosophila DSX are indicated with solid triangles [31,41].

Toyota et al. BMC Genomics 2013 14:239   doi:10.1186/1471-2164-14-239
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