The domain within your query sequence starts at position 3461 and ends at position 3691; the E-value for the AAA_9 domain shown below is 6.7e-59.

LLTDDVEISRWGSQGLPPDELSVQNGILTTRASRFPLCIDPQQQALNWIKRKEEKNNLRV
ASFNDPDFLKQLEMSIKYGTPFLFHDVDEYIDPVIDSVLEKNIKTSQGRQFIILGDKEVD
YDSNFRLYLNTKLANPRYSPSVFGKAMVINYTVTLKGLEDQLLSVLVAYERRELEEQREH
LIQETSENKNLLKDLEDSLLRELATSTGNMLDNVELVQTLEETKSKATEVS

AAA_9

AAA_9
PFAM accession number:PF12781
Interpro abstract (IPR035706):

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 380 kDa motor unit of dynein belongs to the AAA class of chaperone-like ATPases. The core of the 380 kDa 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 D5 ATP-binding region of the motor, but has lost its P-loop [(PUBMED:11250194)].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry AAA_9