Skip to main content
. 2017 Jul 26;73(Pt 8):469–475. doi: 10.1107/S2053230X17010007

Figure 1.

Figure 1

Multiple amino-acid sequence alignment of insect-derived Kazal-type proteins. In the upper block AaTI from Aedes aegypti (UniProt entry Q1HRB8) is aligned with other putative Kazal inhibitors from A. albopictus (UniProt entry Q5MIW1), Psorophora albipes (UniProt entry T1D5N9), Culex pipiens pallens (UniProt entry I6XC79), C. quinquefasciatus (UniProt entry B0XEZ9), Ochlerotatus triseriatus (UniProt entry C6ZQX9), Anopheles sinensis (UniProt entry A0A084VPC8), A. gambiae (UniProt entry Q7QG67), A. aquasalis (UniProt entry T1DGP5) and A. darlingi (UniProt entry B6DDZ6). In the lower block, the structurally characterized infestin 1 (PDB entry 2f3c; Campos et al., 2012 ▸) and infestin 4 (PDB entry 2erw; Campos et al., 2012 ▸) from Triatoma infestans and the N-terminal portion of rhodniin (PDB entry 1tbq; van de Locht et al., 1995 ▸) from Rhodnius prolixus are also aligned with the upper sequences. The mature AaTI amino-acid numbering and secondary-structure elements are indicated above the alignment. A green-to-red colour gradient indicates increasing residue conservation. This figure was prepared with ALINE (Bond & Schüttelkopf, 2009 ▸).