The C-terminal region of the prokaryotic topoisomerases has been solved for multiple species.

The C-terminal region defines the functional domain, which is in itself sufficient for proteolytic activity.

This is due to the highly charged C-terminal regions of the molecules.

Its C-terminal region lacks any homology to the calmodulin-like domain of other calpains.

It also interacts with the C-terminal region of the E1-like atg7 enzyme.

A multiple sequence alignment performed with the C-terminal regions (see Fig.

Based on sequence variation in the C-terminal region of the p72 gene 22 genotypes have been identified.

The membrane-binding is due to an amphiphilic α-helix within the C-terminal region of the protein.

Only the extreme of the C-terminal region shows a significant sequence divergence.

The C-terminal region contains a high degree of α-helical structures.

The C-terminal region of the prokaryotic topoisomerases has been solved for multiple species.

The C-terminal region defines the functional domain, which is in itself sufficient for proteolytic activity.

This is due to the highly charged C-terminal regions of the molecules.

Its C-terminal region lacks any homology to the calmodulin-like domain of other calpains.

It also interacts with the C-terminal region of the E1-like atg7 enzyme.

A multiple sequence alignment performed with the C-terminal regions (see Fig.

Based on sequence variation in the C-terminal region of the p72 gene 22 genotypes have been identified.

The membrane-binding is due to an amphiphilic α-helix within the C-terminal region of the protein.

Only the extreme of the C-terminal region shows a significant sequence divergence.

The C-terminal region contains a high degree of α-helical structures.