Fig. 7. Sequence similarity between SEU, SEUSS-LIKE proteins and Ldb proteins. (A) Diagramatic representation of the open reading frames of SEU, SEUSS-LIKE proteins from Oleracea sativa (AAF34437) and A. thaliana (CAA18174), representative Ldb family members from Danio rerio (AF031377), and Mus musculus (AF024524) and a putative Ldb family member from Saccharomyces pombe (AL031262). Numbers indicate amino acid residues. The shaded portion represents the putative dimerization domain for each protein. Percentages shown within the putative dimerization domain indicate amino acid sequence identity between SEU and the respective protein. Percentages shown to the right are percentage identity to SEU over the entire open reading frame. Glutamine-rich regions are shown as hatched boxes. LID: LIM interaction domain. (B) Sequence alignment of SEU with representative SEUSS-LIKE proteins, and Ldb family proteins in the putative dimerization domain. Identical residues are shaded black. Similar residues are shaded gray. The predicted alpha-helical portion of SEU is indicated with a two-headed arrow. Four hydrophobic or non-polar amino acids (•) in SEU are spaced seven residues apart in this region. Six hydrophobic or non-polar amino acids (•) in the M. musculus Ldb1 protein are also spaced seven residues apart, suggesting a hydrophobic zipper structure (Jurata and Gill, 1997).
