Figure 3

Sequence alignments of ω and κ -hexatoxins. (A) Sequence alignment of ω-HXTX-Hv1a paralogs from each species: Hadronyche modesta (Hmo1a–Hmo1d), Atrax robustus (Ar1a–Ar1g), Hadronyche infensa (Hi1a–Hi1g), and Hadronyche venenata (Hvn1a and Hvn1b). The level of residue conservation is graded from black (fully conserved across all paralogs) to dark grey (conserved in most toxins) to light grey (conserved in a majority of orthologs). The lines below the sequence alignment indicate the disulfide-bond connectivity of ω-HXTX-Hv1a. (B) Alignment of κ-HXTX-Hv1a paralogs from Hadronyche versuta and one ortholog from Hadronyche modesta. The level of residue conservation is graded as in panel (A) and the signal peptide, propeptide, and mature toxin regions are highlighted. The lines below the sequence alignment indicate the disulfide-bond connectivity of κ-HXTX-Hv1c, with the vicinal disulfide bond highlighted in red. Note that ω-HXTX-Ar1a (UniProt PF06357), ω-HXTX-Hi1a (UniProt P0C2L5), ω-HXTX-Hi1b (UniProt P0C2L6), ω-HXTX-Hi1c (UniProt P0C2L7), and κ-HXTX-Hv1c (UniProt P82228) have been previously isolated directly from venom.