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. 2016 Apr 25;113(19):5305–5310. doi: 10.1073/pnas.1521239113

Fig. S1.

Fig. S1.

Protein alignment of BgGRN with pro-GRNs of S. mansoni, S. hematobium, and S. japonicum. Comparison of the amino acid conservation between the pro-BgGRN and pro-GRN proteins of three schistosomes highlights the conservation of the 12-cysteine motif that defines members of the GRN family. Granulin domains are highlighted in green and highlight the high amino acid conservation of the GRN domains between the three schistosomes. The four GRN domains of BgGRN share a 48.9%, 52.2%, 60.4%, and 50% amino acid identity with the three schistosome pro-GRNs. However, a large stretch of amino acids present in the S. mansoni pro-GRN breaks the second GRN domain, and so does an additional amino acid stretch present in all three schistosome pro-GRNs in domain three. BgGRN and S. japonicum granulin possess predicted secretion signal peptide domain in residues 1–18 and cleavage sites between residues 18 and 19. S. mansoni granulin has a predicted signal peptide from residues 1–26 and cleavage site between 26 and 27. The S. hematobium granulin sequence does not possess a traditional signal peptide that can be identified using predictive software.