Fig. 2.

Structure of the ADT-2 protein. (A) Domain organization of ADT-2 protein. Domain organization of mammalian ADAMTS-2 is shown for comparison (predicted by SBASE and SignalP 3.0 Server). (B) Amino acid sequence of ADT-2. Different domains are highlighted. In red is the signal sequence; in violet, the prodomain; in brown, the catalytic domain. Underlined is the Zn binding motif. In green is the conserved methionine residue downstream of the metal binding motif which forms ‘Met-turn’ (Porter et al., 2005). In yellow is the cysteine rich domain. Thrombospondin type I-like repeats are highlighted in blue. The location of the deletion in tm975 and the missense mutation (Gly³⁶⁴ – Ser) in wk156 are indicated by a shaded box and an asterisk, respectively. (C) Zinc binding motif and Met turn of C. elegans ADT-2 are aligned with other mammalian and C. elegans ADAMTS family members. The conserved zinc binding motif and methionine residue downstream of the metal binding site are shaded. Asterisks indicate conserved amino acids. The glycine in red is the conserved residue mutated in adt-2(wk156). (D) Phylogenetic tree showing relationships between C. elegans and human ADAMTS sequences (constructed using BioEdit sequence Alignment Editor and MEGA 4.0.2). The numbers above the nodes indicate the percent bootstrap values in 500 replicates of the data.