The domain within your query sequence starts at position 431 and ends at position 470; the E-value for the Kelch domain shown below is 4.1e0.



SMART accession number:SM00612
Description: -
Interpro abstract (IPR006652):

Kelch is a 50-residue motif, named after the Drosophila mutant in which it was first identified [(PUBMED:8453663)]. This sequence motif represents one beta-sheet blade, and several of these repeats can associate to form a beta-propeller. For instance, the motif appears 6 times in Drosophila egg-chamber regulatory protein (also known as ring canal kelch protein), creating a 6-bladed beta-propeller. The motif is also found in mouse protein MIPP [(PUBMED:8453663)] and in a number of poxviruses. In addition, kelch repeats have been recognised in alpha- and beta-scruin [(PUBMED:7593276), (PUBMED:7822422)], and in galactose oxidase from the fungus Dactylium dendroides [(PUBMED:8126718), (PUBMED:2002850)]. The structure of galactose oxidase reveals that the repeated sequence corresponds to a 4-stranded anti-parallel beta-sheet motif that forms the repeat unit in a super-barrel structural fold [(PUBMED:8182749)].

The known functions of kelch-containing proteins are diverse: scruin is an actin cross-linking protein; galactose oxidase catalyses the oxidation of the hydroxyl group at the C6 position in D-galactose; and kelch may have a cytoskeletal function, as it is localised to the actin-rich ring canals that connect the 15 nurse cells to the developing oocyte in Drosophila [(PUBMED:7593276)]. Nevertheless, based on the location of the kelch pattern in the catalytic unit in galactose oxidase, functionally important residues have been predicted in glyoxal oxidase [(PUBMED:8126718)].

This entry represents a type of kelch sequence motif that comprises one beta-sheet blade.

GO function:protein binding (GO:0005515)
Family alignment:
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There are 151337 Kelch domains in 35376 proteins in SMART's nrdb database.

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