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Fig. 5. Comparison of the deduced amino acid sequences in domains II and III of
calpains from arthropods, nematode and human. Amino acid sequences were
aligned using ClustalW (see Materials and methods). Broken lines indicate gaps
for optimizing alignment. Amino acid residues that are identical or similar in
all the sequences are highlighted in black; gray shading indicates identical
or similar amino acids in most of the sequences. Asterisks indicate residues
of the catalytic triad (C, H, N). Open inverted triangles indicate conserved
residues in two non-EF-hand Ca2+-binding regions in domain II.
Roman numerals indicate boundaries between domains. Numbers at the right
indicate amino acid positions, numbered from the N-terminus of each protein.
Boxes with broken lines indicate locations of two acidic amino acid expansions
found in Ha-CalpM, but not in Gl-CalpM; one (DDSDD) is positioned near the end
of domain II and the other (DDDDDDDDDDRG) is located in the acidic loop region
in domain III. Human calpain 3 contains a unique insertion sequence in domain
II. Accession numbers: C. elegans TRA-3, NP502751; Dm-CalpA,
NP477047; Dm-CalpB, NP524016; human calpain 1, AAH08751 human calpain 3,
NP058813; human calpain 5, JC5772; Ha-CalpM, AAM88579
