The domain within your query sequence starts at position 2383 and ends at position 2533; the E-value for the I_LWEQ domain shown below is 4.3e-51.

NAADDGQWSQGLISAARMVAAATSSLCEAANASVQGHASEEKLISSAKQVAASTAQLLVA
CKVKADQDSEAMKRLQAAGNAVKRASDNLVRAAQKAAFGKADDDDVVVKTKFVGGIAQII
AAQEEMLKKERELEEARKKLAQIRQQQYKFL

I_LWEQ

I_LWEQ
PFAM accession number:PF01608
Interpro abstract (IPR002558):

The I/LWEQ domain is a ~250-residue actin-binding module that is found in the C termini of functionally diverse proteins from yeast to mammals. The I/LWEQ domain contains four conserved blocks and has been named after the conserved initial residues of blocks 1-4. The I/LWEQ domain is generally found near the C terminus and in association with other domains, such as FERM or ENTH. The I/LWEQ domain has been shown to bind to F-actin and to bundle actin filaments [(PUBMED:9159132), (PUBMED:10581178), (PUBMED:16415883)].

The I/LWEQ domain contains a proteolysis resistant-core that has an all-alpha-helical structure composed of five long down-up-down-up-down antiparallelhelices connected by short loops and one short connecting alpha helix arranged in a progressive topology. The proteolysis-resistant core is followed by a C-terminal latch region that adopts an alpha-helical conformation. The latch region can mediate oligomerization of I/LWEQ domains, possibly as dimers, and this seems to enhance the F-actin-binding ability of the proteolysis-resistant core [(PUBMED:16415883)].

It's worth noting that the I/LWEQ domain has also been called the talin-HIP1/R/Slap2p actin- tethering C-terminal homology (THATCH) domain (HIP1/R/Slap2p denotes similarity of Slap2p to HIP1 and HIP1R) [(PUBMED:6415883)].

GO function:actin binding (GO:0003779)

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