Dynein heavy chain, hydrolytic ATP-binding dynein motor region (IPR035699)

Short name: AAA_6

Overlapping homologous superfamilies

Domain relationships



Dyneins are multiprotein complexes that move cargo along microtubules in the minus end direction. The largest component of the dynein complex is the heavy chain. Its C terminus forms the motor unit [PMID: 27062277].

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 domain is the D1 unit of the motor and contains the hydrolytic ATP binding site [PMID: 11250194].

This is the AAA1 large (AAA1L) subdomain with the accompanying small subdomain (AAA1S). AAA1L, AAA1S and AAA2L enclose ADP.vanadate (ADP.Vi, ATP-hydrolysis transition state analogue). The AAA1L sensor-I loop, which varies in position depending on dynein's nucleotide state, swings in to contact AAA2L forming the important AAA1 nucleotide-binding site [PMID: 25470043].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0005524 ATP binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.