The domain within your query sequence starts at position 16 and ends at position 400; the E-value for the Dynamitin domain shown below is 7.1e-129.

EPDVYETSDLPEDDQAEFDAEELSSTSVEHIIVNPNAAYDKFKDKRVGTKGLDFSDRIGK
TKRTGYESGDYEMLGEGLGVKETPQQKYQRLLHEVQELTTEVEKIKTTVKESATEEKLTP
VVLAKQLAALKQQLVASHLEKLLGPDAAINLADPDGALAKRLLLQLEATKSSKGSSGGKA
TAGAPPDSSLVTYELHSRPEQDKFSQAAKVAELEKRLTELEATVRCDQDAQNPLSAGLQG
ACLMETVELLQAKVSALDLAVLDQVEARLQSVLGKVNEIAKHKASVEDADTQNKVHQLYE
TIQRWSPVASTLPELVQRLVTIKQLHEQAMQFGQLLTHLDTTQQMMASSLKDNTALLTQV
QTTMRENLATVEGNFASIDARMKRL

Dynamitin

Dynamitin
PFAM accession number:PF04912
Interpro abstract (IPR028133):

Dynactin is a multiprotein complex necessary for the function of microtubule motor protein dynein. The dynein-dynactin complex is involved in a variety of cellular events, including membrane vesicle transport, mitotic spindle assembly and centrosome separation [(PUBMED:19935668), (PUBMED:9522459), (PUBMED:10047518)].

Dynamitin (dynactin subunit 2, DCTN2) is a subunit of the dynactin complex. In Saccharomyces cerevisiae it is also known as Jnm1. Dynactin contains two distinct structural domains: a projecting sidearm that interacts with dynein and an actin-like minifilament backbone that is thought to bind cargo. Dynamitin holds together both structural domains [(PUBMED:10525537)]. Dynamitin is implicated in cell adhesion by binding to macrophage-enriched myristoylated alanine-rice C kinase substrate (MacMARCKS) [(PUBMED:12082093)]. In mice, DCTN2 is involved in anchoring microtubules to centrosomes and may play a role in synapse formation during brain development [(PUBMED:9144527)].

GO process:microtubule-based process (GO:0007017)
GO component:dynactin complex (GO:0005869)

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