One comes from analysis of what are called protein domains.

This has led, in recent years, to a focus on families of protein domains.

There appears to be two protein domains of similar size.

These are usually separate proteins or can occur as protein domains.

The function of this protein domain has been difficult to elucidate.

This protein domain is involved in the control of Yop release.

Furthermore, its structure makes it very difficult to predict the protein domain's function.

The protein domain is found in regulators that control splicing.

Other targets include, for example, the protein domains beyond the active site of IN.

This protein domain is thought to have a SH3-like barrel structure.

This protein domain is highly important to cell survival.

The Pfam database contains information about protein domains and families.

This protein domain, has an important function in forming pili.

This protein domain, often found in bacterial species, is actually of viral origin.

This protein domain is known to contain one short alpha helix.

The structure of this protein domain contains a globular fold.

This protein domain belongs to a family of evolutionarily related proteins.

This strand acts as a hinge, and can bring the two protein domains closer together.

This protein domain has a conserved region of around 80 residuea.

The beta helix is a type of solenoid protein domain.

The precise function of this protein domain remains unknown.

The function of this protein domain, in animals, is to aid progression through the cell cycle.

This protein domain is only found in viruses.

The model entry describes a protein domain in longer eukaryotic proteins.

The protein domain Ste50p has a role in detecting pheromones for mating.