The domain within your query sequence starts at position 255 and ends at position 287; the E-value for the LisH domain shown below is 1.25e-3.

EKRALNFLVNEFLLKNNYKLTSITFSDENDDQD

LisH

Lissencephaly type-1-like homology motif
LisH
SMART accession number:SM00667
Description: Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.
Interpro abstract (IPR006594):

The 33-residue LIS1 homology (LisH) motif is found in eukaryotic intracellular proteins involved in microtubule dynamics, cell migration, nucleokinesis and chromosome segregation. The LisH motif is likely to possess a conserved protein-binding function and it has been proposed that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly. The LisH motif is found associated to other domains, such as WD-40, SPRY, Kelch, AAA ATPase, RasGEF, or HEAT [(PUBMED:11734546), (PUBMED:12384287), (PUBMED:12559565)].

The secondary structure of the LisH domain is predicted to be two alpha- helices [(PUBMED:11734546)].

GO function:protein binding (GO:0005515)
Family alignment:
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There are 25290 LisH domains in 24886 proteins in SMART's nrdb database.

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