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. 2007 Oct 3;100(6):1199–1208. doi: 10.1093/aob/mcm216

Fig. 5.

Fig. 5.

Amino acid alignment of LcVSP1 and other proteins. The lemir from Lycopersicon esculentum (AAC63057), tumour-related protein from Nicotiana tabacum (AAC49969), endopeptidase inhibitor from Arabidopsis thaliana (NP_173228), trypsin inhibitor homologue from Glycine max (S16252), putative 21-kDa trypsin inhibitor from Theobroma microcarpum (AAV41234), miraculin-like protein2 from Citrus jambhiri (BAE79511) and Kunitz trypsin inhibitor 4 from Populus balsamifera subsp. trichocarpa (AAQ84217). Residues that are identical throughout the proteins are shown in black. Residues conserved in > 50 % of the proteins are shown in pink. Similar amino acid residues are shown in blue. Except for LcVSP1, all of the sequences were named conferring to their GenBank accession numbers.