SMART: Pfam domain Kelch

The domain within your query sequence starts at position 250 and ends at position 292; the E-value for the Kelch_1 domain shown below is 2.9e-9.

GCAAHAAVAVGHHVYMFGGMTATGALNMMYKYHTEKQHWTVLQ

Kelch_1

PFAM accession number:	PF01344
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)

PFAM accession number:

PF01344

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)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Kelch_1