The domain within your query sequence starts at position 1 and ends at position 203; the E-value for the AAA_6 domain shown below is 4e-84.



PFAM accession number:PF12774
Interpro abstract (IPR035699):

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 [ (PUBMED: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 [ (PUBMED: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 [ (PUBMED:25470043) ].

GO function:ATP binding (GO:0005524)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry AAA_6