|SMART accession number:||SM00612|
|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, 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; neuraminidase hydrolyses sialic acid residues from glycoproteins; 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)|
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- Evolution (species in which this domain is found)
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- Structure (3D structures containing this domain)
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