The domain within your query sequence starts at position 634 and ends at position 743; the E-value for the DIL domain shown below is 6.19e-34.
QMLAYLFFFSGTLLLNQVLDKGPSLSCFHWPRGVQVCARLQQFLEWARSAGLGAPAERFF RKLSCTLHLLATPRAQLIQMSWATLRVTFPALNPAQLHRLLTQYQLASAM
DIL |
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| SMART accession number: | SM01132 |
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| Description: | The DIL domain has no known function. |
| Interpro abstract (IPR002710): | The myosin superfamily consists of at least 15 distinct classes of presumed actin-based molecular motors. All members of the superfamily share a similar motor domain and a tail portion which is diagnostic of the class [ (PUBMED:11212352) ]. Class V myosins are actin-based molecular motors that function in relatively long-range movements of many intracellular cargoes including organelles, membrane vesicles, and mRNA [ (PUBMED:10931864) ]. These motors are ubiquitously found in all eukaryotes. Class V myosins are characterised by the presence of a conserved globular domain at the C terminus of the tail portion: the dilute domain [ (PUBMED:7667878) ]. Myosin V moves via attachment of its amino terminal head (motor) domain to actin cables; its carboxyl terminal dilute domain anchors it to cargoes via attachments to organelle-specific receptors [ (PUBMED:10931864) (PUBMED:15684027) ]. The dilute domain is also found in the afadin family. Afadins are nectin and actin filament-binding proteins that connect nectin to the actin cytoskeleton [ (PUBMED:12456712) ]. The dilute domain of afadin appears to be responsible for actin stress fibre formation [ (PUBMED:25712270) ]. |
| Family alignment: |
There are 6872 DIL domains in 6863 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
- Structure (3D structures containing this domain)
- Links (links to other resources describing this domain)
