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Entomology and Plant Pathology

Phylogenetic analysis of the catalytic domains of 193 Drosophila SPs and SPHs.

To obtain an overview of this SP-related protein family, sequence alignment and phylogenetic analysis of the catalytic or protease-like domains of 193 Drosophila SPs and SPHs were performed as described in Materials and Methods. To ensure that the same region is compared, 50 amino acid residues upstream of the active site histidine and 50 downstream of the active site serine were included in the alignment. Eighteen sequences (SPHs 73, 162, 180, 181, 190, 194, 198- 204, 205, 208-211) were eliminated because they lack one or more of the three conserved regions (Table 1). A large insertion of 102 residues in SPH175 was deleted for the same reason. Both catalytic domains in SPs 6, 80, 86, 126, and 176 (N and C) were included in this analysis. Construction of a phylogenetic tree was carried out using the ClustalW program based on the multiple sequence alignment. To demonstrate phylogenetic relationships that are statistically significant, complete branches with a bootstrap value larger than 30 (100 trials) at the leftmost node are shown. Nodes marked with I*I have a slightly different order in the distance tree whereas I?I show a significant difference. Vertical bars indicate highly similar sequences whose genes are closely adjacent. Their polytene chromosome band locations are listed at the right of the bar that are closely located on the chromosomes.
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