Figure 1.

Multiple sequence alignment of navidefensins, nasonins and related peptides. 1: Amdefensin1(Am); 2: Amdefensin2(Am); 3: Navidefensin1-1(Nv); 4: Navidefensin1-2(Nv); 5: Navidefensin2-1(Nv); 6: Navidefensin2-2(Nv); 7: Navidefensin2-3(Nv); 8: Navidefensin3(Nv); 9: Phormicin(Pt); 10: Sapecin(Sp); 11: Dmdefensin(Dm); 12: Heliomicin(Hv); 13: Nasonin-1(Nv); 14: Nasonin-2(Nv); 15: Nasonin-3(Nv); 16: Nasonin-4(Nv); 17: Nasonin-5(Nv); 18: Nasonin-6(Nv); 19: Nasonin-7(Nv); 20: Nasonin-8(Nv); 21: Nasonin-9(Nv); 22: Nasonin-10(Nv); 23: Nasonin-11(Nv); 24: Nasonin-12(Nv); 25: Nasonin-13(Nv); 26: Nasonin-14(Nv); 27: Cobatoxin-1(Cn); 28: Cll-Defensin1(Cll); 29: Ps-Termicin(Ps); 30: Dr-Termicin(Dr). Am: A. mellifera, Nv: N. vitripennis, Pt: Protophormia terraenovae, Sp: Sarcophaga peregrine, Dm: D. melonagaster, Hv: Heliothis virescens, Cn: Centruroides noxius, Cll: C. limpidus limpidus, Ps: Pseudacanthotermes spiniger, Dr: Drepanotermes rubriceps. Secondary structure elements (α-helix: cylinder; β-strand: arrow) and disulfide bridge connectivity are shown on the bottom of the alignment. Acidic residues in the propeptide are shown in pink and cleavage sites are boxed. Identical amino acids or constitutive replacements are shadowed in yellow and grey, respectively. Consensu/60% (Con.): - (negative), * (Ser/Thr), l (aliphatic), + (positive), t (tiny), a (aromatic), c (charged), s (small), p (polar), b (big), h (hydrophobic). Basic residues (K, R, H) are shown in blue. Residues split by phase 1 or 2 introns are boxed in green or purple. Omitted residues in carboxyl-termini are indicated by +aa.

Tian et al. BMC Genomics 2010 11:187   doi:10.1186/1471-2164-11-187
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