InterPro domain: IPR004273

This entry represents the C-terminal region of dynein heavy chain. The chain also contains ATPase activity and microtubule binding ability and acts as a motor for the movement of organelles and vesicles along microtubules. Dynein is also involved in cilia and flagella movement. The dynein subunit consists of at least two heavy chains and a number of intermediate and light chains [ 1 ]. The 380kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380kDa motor unit contains a concatenated chain of six AAA modules, of which four correspond to the ATP binding sites with P-loop signatures described previously, and two are modules in which the P loop has been lost in evolution. This C-terminal domain carries the D6 region of the dynein motor where the P-loop has been lost in evolution but the general structure of a potential ATP binding site appears to be retained [ 2 ].

1. Molecular characterization of a cytoplasmic dynein from Dictyostelium. J. Eukaryot. Microbiol. 41, 645-51
2. Model for the motor component of dynein heavy chain based on homology to the AAA family of oligomeric ATPases. Structure 9, 93-103