During maturation, most proteins undergo different posttranslational modifications. In most simple cases, signal peptidases remove the signal or leader peptide from the precursors of the secretory proteins during their translocation across the ER membrane. For biologically active proteins, such as enzymes, regulatory and defense proteins, toxins, etc., additional maturation-regulating mechanisms were shown to proceed with limited proteolysis of inactive precursors by specific enzymes. A number of specific enzymes from different cell types selectively cleave proproteins at specific processing sites. In this work, we analyzed the sequences of protein precursors synthesized in the excretory glands of different animals and identified new, non-traditional processing sites. They differ from the motifs previously identified in secreted proteins' precursors and enabled us to reconstruct the sequence of events leading to the conversion of protein precursors into the final products (mature proteins). We also found that in animals, the maturation mechanism of secretory and excretory proteins and the set of enzymes involved are species specific. The processing sites identified in protein precursors in this study are useful for a more detailed genome analysis and more accurate mature protein sequence prediction.