I/LWEQ domain
SMART accession number:SM00307
Description: Thought to possess an F-actin binding function.
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)
Family alignment:
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There are 1612 ILWEQ domains in 1610 proteins in SMART's nrdb database.

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