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. 2012 Jul 19;10(7):1545–1565. doi: 10.3390/md10071545

Figure 3.

Figure 3

Alignment of amino acid sequences of protease inhibitors, analgesic polypeptides, Kv channels toxins from sea anemones, and protease inhibitor from bovine pancreas. InhVJ, Jn-IV, APHC1-APHC3, HCGS 2.3, 1.34, 1.26, 1.10, 1.36 from H. crispa [15,21,22,30]; SHPI-1, SHPI-2 from S.helianthus [11,12];SA5 II, AsKC1-AsKC3 from A. sulcata [16,17];SHTX III from Stichodactyla haddoni [20]; APEKTx1 from Anthopleura elegantissima [28]; AXPI-I, AXPI-II, and AXPI-III from Anthopleura aff. xanthogrammica [9,10]; AEAPI, AEPI-I, and AEPI-II from Actiniaequina [14,23]; AFAPI-I, AFAPI-III from Anthopleurafuscoviridis [23]; BPTI from Bos taurus [33]. Р1—amino acid residue of the inhibitor’s reactive center. The asterisks below the sequence of BPTI indicate the contact sites with serine proteases. Identical and conservative residues are indicated by dark and light gray colors.