DEV01973 Supplementary Material

Files in this Data Supplement:

• Supplemental Figure 1 - Fig.S1. (A) Alignment of Eya domains from chordates, flatworm and fly. Within this protein-protein interaction domain is a catalytic motif essential for phosphatase activity (red) and a metal-binding motif (green), both conserved in common with phosphoserine phosphatase (Li et al., 2003). (B) Alignment of C-terminal region of chordate Pitx protein sequences. The homeodomain (black box) has the lysine (red) at position 50 characteristic of the Pitx class of OAR-containing superfamily of proteins. Though the homeodomain is well conserved between Oikopleura and other chordates, only short motifs (green) are alignable in the C-terminal tail. The OAR domain, conserved in other Pitx proteins, is not recognizable in the larvacean protein; there is, however, a region (blue) rich in serine, leucine and arginine that shares some similarity to the Pitx OAR consensus in short but misordered runs of amino acids. (C) Alignment of Six domains and homeodomains from Six proteins supports the orthology of the cloned Oikopleura genes with Six1/2 and Six3/6, but not Six4/5 paralogy groups. A four amino acid insertion shared among Six3 and Six6 proteins is conserved in Oikopleura and ascidian Six3/6. An asterisk marks an amino acid position that supports the exclusion of these three Oikopleura genes from the Six4/5 subfamily. An amino acid substitution in the two Oikopleura six3/6 genes within a tetrapeptide diagnostic for the Six3 and Six6 paralogy group is shared with the ascidian Halocynthia Six3/6; this similarity, however, could result from convergence rather than common inheritance, as the change from QKTH to QKSH is biochemically conservative and is not shared with Ciona Six3/6. The homeodomain is boxed.