Summary
Kelch motif
The kelch motif was initially discovered in Kelch (Q04652). In this protein there are six copies of the motif. It has been shown that Q04652 is related to Galactose Oxidase [1] for which a structure has been solved [2]. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in PF00064 PF00400 and PF00415.
Literature references
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Bork P, Doolittle RF; , J Mol Biol 1994;236:1277-1282.: Drosophila kelch motif is derived from a common enzyme fold. PUBMED:8126718
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Ito N, Phillips SE, Stevens C, Ogel ZB, McPherson MJ, Keen JN, Yadav KD, Knowles PF; , Nature 1991;350:87-90.: Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase. PUBMED:2002850
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Li X, Zhang D, Hannink M, Beamer LJ; , J Biol Chem 2004;279:54750-54758.: Crystal structure of the Kelch domain of human Keap1. PUBMED:15475350
InterPro entry 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.
Clan
This family is a member of clan Kelch (CL0002), which contains the following 3 members:
DUF1668 Kelch_1 Kelch_2External database links
| PANDIT: | PF01344 |
| SCOP: | 1gof |
| SYSTERS: | Kelch_1 |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
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Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | [1] |
| Previous IDs: | none |
| Type: | Repeat |
| Author: | Bateman A |
| Number in seed: | 222 |
| Number in full: | 7775 |
| Average length of the domain: | 45.90 aa |
| Average identity of full alignment: | 24 % |
| Average coverage of the sequence by the domain: | 7.74 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 47 | ||||||||||||
| Family (HMM) version: | 18 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Kelch_1 domain has been found.
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