There are a total of 38 completely conserved residues across these 10 species, corresponding to 10.76% conservation.

Usually, three conserved residues on the β-sheet are very important for this recognition process.

Output was prepared using a 50% threshold for identical and conserved residues.

Shading highlights the conserved residues in each of the three motifs.

A subclade comparison was carried out to analyze the conserved residues.

Consensus sequence motifs are specified rather than completely conserved residues.

The method highlights conserved residues within clusters which often have functional significance.

It also contains 26 highly conserved residues and several post-translation modifications.

In these latter cases, the role of the conserved residues in protein function is not known.

The conserved residues are those involved in zinc binding or the hydrophobic core of the protein.

Also, some statistics pertaining the number and percentage of matched and conserved residues are printed.

The only conserved residues in these structures are those involved in the recognition of the carboxy terminal.

Neither the predicted secondary structure, nor the pattern of the conserved residues revealed an obvious relationship with any previously recognized fold.

A conserved residue of Ddx19 is shown to be crucial for complex formation in vitro and in vivo.

The presence of these highly conserved residues in plant myosins suggests that they are capable of motor function.

Substitutions for the conserved residues abolish repression.

GAK is 57% homologous to auxilin if conserved residues are included in the comparison.

It is named EAL after its conserved residues.

Instead, based on the spacing of the conserved residues, the motif probably forms a short alpha-helix that can be embedded into different protein folds.

Many other conserved residues in TGF-β are thought to form secondary structure through hydrophobic interactions.

The core of the barrel consists of an extended hydrogen bonding network of highly conserved residues.

However many examples of DHHC domains are known that do not contain all these conserved residues.

Conserved residues on one face of the barrel and adjacent loops form the putative RNA-binding site.

G6PD is negatively regulated by acetylation on lysine 403 (K403), an evolutionarily conserved residue.

Of the highly conserved residues (Table 1), the Gs of subdomain I show the most variability.