The Prosite Scan analysis showed three eukaryotic thiol
protease domains at 134–145, 278–288 and 299–318
along with their cysteine (Cys140), histidine (His280)
and asparagine (Asn304) active site residues, respectively
(Fig. 1). In addition, 20 other high probability
common motifs were observed. These 20 motifs belong
to 4 different sites including phosphorylation, myristoylation,
glycosylation and amidation groups. SignalP
analysis showed a peak at 18th position of CsCath L
amino acid sequence, thus predicting it as the cleavage
site of deduced amino acid sequence. Hence, it is predicted that the signal peptide comprises the region of
CsCath L between 1 and 17. Further analysis revealed
that CsCath L contains an inhibitor region along with
its peptidase C1 super family active domain at 30–90,
which belongs to inhibitor 29 superfamily.