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0  structures 235  species 2  interactions 698  sequences 211  architectures

Family: Kelch_2 (PF07646)

Summary: Kelch motif

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This is the Wikipedia entry entitled "Kelch motif". More...

Kelch motif Edit Wikipedia article

Kelch motif
PDB 1gof EBI.jpg
Structure of Galactose oxidase containing kelch repeats.[1]
Identifiers
Symbol Kelch_1
Pfam PF01344
InterPro IPR006652
SMART Kelch
SCOP 1gof
SUPERFAMILY 1gof
OPM superfamily 384
OPM protein 3ii7
Kelch motif
Identifiers
Symbol Kelch_2
Pfam PF07646
Pfam clan CL0186
InterPro IPR011498
SCOP 1gof
SUPERFAMILY 1gof
Galactose oxidase, central domain
Identifiers
Symbol Kelch_3
Pfam PF13415
Pfam clan CL0186
Galactose oxidase, central domain
Identifiers
Symbol Kelch_4
Pfam PF13418
Pfam clan CL0186
Kelch motif
Identifiers
Symbol Kelch_5
Pfam PF13854
Pfam clan CL0186
Kelch motif
Identifiers
Symbol Kelch_6
Pfam PF13964
Pfam clan CL0186

The Kelch motif is a region of protein sequence found widely in proteins from bacteria and eukaryotes.[2] This sequence motif is composed of about 50 amino acid residues which form a structure of a four stranded beta-sheet "blade". This sequence motif is found in between six and eight copies per protein which fold together to form a larger circular solenoid structure called a beta-propeller domain.

Proteins containing Kelch motifs[edit]

The Kelch motif is widely found in eukaryotic and bacterial species. Notably the human genome contains around 100 proteins containing the Kelch motif. Within individual proteins the motif occurs multiple times. For example, the motif appears 6 times in Drosophila egg-chamber regulatory protein. The motif is also found in mouse protein MIPP[3] and in a number of poxviruses. In addition, kelch repeats have been recognised in alpha- and beta-scruin,[4][5] and in galactose oxidase from the fungus Dactylium dendroides.[6][7]

Structure[edit]

The structure of galactose oxidase reveals that the repeated Kelch sequence motif corresponds to a 4-stranded anti-parallel beta-sheet motif that forms the repeat unit in a super-barrel structural fold commonly known as a beta propeller.[8]

Function[edit]

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;
  • 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.[4]

See also[edit]

References[edit]

  1. ^ Ito N, Phillips SE, Stevens C, et al. (March 1991). "Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase". Nature 350 (6313): 87–90. doi:10.1038/350087a0. PMID 2002850. 
  2. ^ Adams J, Kelso R, Cooley L (January 2000). "The kelch repeat superfamily of proteins: propellers of cell function". Trends Cell Biol. 10 (1): 17–24. doi:10.1016/S0962-8924(99)01673-6. PMID 10603472. 
  3. ^ Xue F, Cooley L (1993). "kelch encodes a component of intercellular bridges in Drosophila egg chambers". Cell 72 (5): 681–693. doi:10.1016/0092-8674(93)90397-9. PMID 8453663. 
  4. ^ a b Way M, Sanders M, Matsudaira P, Chafel M, Knight A, Tu YH (1995). "beta-Scruin, a homologue of the actin crosslinking protein scruin, is localized to the acrosomal vesicle of Limulus sperm". J. Cell Sci. 108: 3155–3162. PMID 7593276. 
  5. ^ Way M, Sakai J, Sanders M, Garcia C, Matsudaira P (1995). "Sequence and domain organization of scruin, an actin-cross-linking protein in the acrosomal process of Limulus sperm". J. Cell Biol. 128 (1): 51–60. doi:10.1083/jcb.128.1.51. PMC 2120335. PMID 7822422. 
  6. ^ Doolittle RF, Bork P (1994). "Drosophila kelch motif is derived from a common enzyme fold". J. Mol. Biol. 236 (5): 1277–1282. doi:10.1016/0022-2836(94)90056-6. PMID 8126718. 
  7. ^ Keen JN, Ito N, Phillips SE, Stevens C, Ogel ZB, McPherson MJ, Yadav KD, Knowles PF (1991). "Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase". Nature 350 (6313): 87–90. doi:10.1038/350087a0. PMID 2002850. 
  8. ^ Ito N, Phillips SE, Yadav KD, Knowles PF (1994). "Crystal structure of a free radical enzyme, galactose oxidase". J. Mol. Biol. 238 (5): 794–814. PMID 8182749. 

External links[edit]

This article incorporates text from the public domain Pfam and InterPro IPR006652

This article incorporates text from the public domain Pfam and InterPro IPR011498

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Kelch motif Provide feedback

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

  1. Bork P, Doolittle RF; , J Mol Biol 1994;236:1277-1282.: Drosophila kelch motif is derived from a common enzyme fold. PUBMED:8126718 EPMC:8126718

  2. 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 EPMC:2002850

  3. 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 EPMC:15475350


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR011498

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.

Gene Ontology

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Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan Beta_propeller (CL0186), which has the following description:

This large clan contains proteins that contain beta propellers. These are composed of between 6 and 8 repeats. The individual repeats are composed of a four stranded sheet. The clan includes families such as WD40 Pfam:PF00400 where the individual repeats are modeled. The clan also includes families where the entire propeller is modeled such as Pfam:PF02239 usually because the individual repeats are not discernible. These proteins carry out a very wide diversity of functions including catalysis.

The clan contains the following 60 members:

Apc4_WD40 Arylesterase Arylsulfotran_2 Arylsulfotrans Beta_propel CNH Coatomer_WDAD CPSF_A Cytochrom_D1 DPPIV_N DUF1513 DUF1668 DUF1900 DUF2415 DUF3312 DUF4652 DUF839 eIF2A FG-GAP FG-GAP_2 Glu_cyclase_2 Gmad1 GSDH IKI3 Kelch_1 Kelch_2 Kelch_3 Kelch_4 Kelch_5 Kelch_6 Lactonase Ldl_recept_b Lgl_C LVIVD Me-amine-dh_H MRJP Nbas_N Neisseria_PilC NHL Nucleoporin_N Nup160 PD40 Pectate_lyase22 Peptidase_S9_N Phytase-like PQQ PQQ_2 PQQ_3 RAG2 RCC1 RCC1_2 Reg_prop SBBP SBP56 SdiA-regulated SGL Str_synth TcdB_toxin_midN VCBS WD40

Alignments

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  Seed
(42)
Full
(698)
Representative proteomes NCBI
(6336)
Meta
(157)
RP15
(102)
RP35
(166)
RP55
(239)
RP75
(334)
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  Seed
(42)
Full
(698)
Representative proteomes NCBI
(6336)
Meta
(157)
RP15
(102)
RP35
(166)
RP55
(239)
RP75
(334)
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  Seed
(42)
Full
(698)
Representative proteomes NCBI
(6336)
Meta
(157)
RP15
(102)
RP35
(166)
RP55
(239)
RP75
(334)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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 HMMER3.

Pfam alignments:

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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 View help on the curation process

Seed source: Context Domains
Previous IDs: none
Type: Repeat
Author: Finn RD
Number in seed: 42
Number in full: 698
Average length of the domain: 51.00 aa
Average identity of full alignment: 22 %
Average coverage of the sequence by the domain: 11.00 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.3 21.3
Trusted cut-off 21.3 21.3
Noise cut-off 21.2 21.2
Model length: 49
Family (HMM) version: 10
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 2 interactions for this family. More...

Kelch_1 Kelch_2