The Crustacean hyperglycemic hormones (CHHs) are an ever extending family o
f crustacean hormones mainly involved in carbohydrate metabolism, molt and
reproduction. In this paper, we drew together 32 available CHH sequences, a
nd applied the techniques of multiple sequence alignment, motif searching a
nd amino acid conservation analysis to the characterization of the molecule
s independently of their biological function. The analysis clearly showed t
hat the proteins clustered into two groups (CHH and VIH). Amino acid conser
vation analysis also subdivided the VIH group into sequences involved in re
production (RIH) or in molt (MIH). Motif searching identified five motifs i
n each group of mature hormones. Motifs A2 and A3 were conserved in all seq
uences while motifs Al and A1' were specific of the CHH and VIH groups resp
ectively. This approach demonstrated the S. gregaria ion transport peptides
as true members of the CHH group. The two main groups, CHH and VIH, are al
so discussed in terms of functional homogeneity.