Figure 2.

Schematic diagrams of the DSX1 structures and its sequence comparison of DM- and oligomerization-domains. (A) Domain structures of DSX1 in Daphnia magna, and identity with D. pulex, D. galeata, C. dubia and M. macrocopa. 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 DSX1 from five cladocerans, respectively. Amino acid sequences were aligned using CLUSTAL-X. Dotted boxes highlight the conserved threonine (T) residue in the DM-domain, and arginine (R) residue substituted for glutamine (Q), which is conserved amino acid residues of DSX. Asterisks indicate the zinc chelating residues [43]. 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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