Figure 4.9A. Conserved catalytic motifs in the caspase-like superfamily of proteases.

Figure 4.9AConserved catalytic motifs in the caspase-like superfamily of proteases

A. Multiple alignment of the catalytic motifs around the two active residues (His and Cys) of caspases (Csp, top group), paracaspases (PC, middle group), and metacaspases; see more about these proteases in 6.4.4. Note the conservation in the stretches preceding each of the catalytic residues and corresponding to the two main β-strands of the caspase domain (see panel B). Conserved hydrophobic residues are highlighted in yellow; conserved small residues (Gly, Ser, Ala, Cys) are shown on a green background. The species abbreviations are: Hs, human; Ce, C. elegans; Dd, Dictyostelium; Ml, M. loti; Sc, yeast; At, Arabidopsis; Rsph, Rhodobacter sphaeroides; Gsul, Geobacter sulfurreducens.

From: Chapter 4, Principles and Methods of Sequence Analysis

Cover of Sequence - Evolution - Function
Sequence - Evolution - Function: Computational Approaches in Comparative Genomics.
Koonin EV, Galperin MY.
Boston: Kluwer Academic; 2003.
Copyright © 2003, Kluwer Academic.

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