The domain within your query sequence starts at position 1793 and ends at position 2023; the E-value for the AAA_6 domain shown below is 7e-149.

YSYEYLGNTPRLVITPLTDRCYITLTQSLHLIMGGAPAGPAGTGKTETTKDLGRALGTMV
YVFNCSEQMDYKSCGNIYKGLAQTGAWGCFDEFNRISVEVLSVIAVQVKCVQDAIRAKKK
KFNFLGEIISLVPTVGIFITMNPGYAGRTELPENLKALFRPCAMVVPDFELICEIMLVAE
GFLDARLLARKFITLYTLCKELLSKQDHYDWGLRAIKSVLVVAGSLKRGDP

AAA_6

AAA_6
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 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 D1 unit of the motor and contains the hydrolytic ATP binding site [(PUBMED:11250194)].

GO function:ATP binding (GO:0005524)

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