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0  structures 387  species 0  interactions 1811  sequences 393  architectures

Family: Kelch_6 (PF13964)

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 is the Wikipedia entry entitled "Kelch protein". More...

Kelch protein Edit Wikipedia article

Kelch motif
1gof front.GIF
Identifiers
Symbol Kelch_1
Pfam PF01344
InterPro IPR006652
SCOP 1gof
SUPERFAMILY 1gof

Kelch proteins (and Kelch-like proteins) are a widespread group of proteins that contain multiple Kelch motifs. The kelch domain generally occurs as a set of five to seven kelch repeats that form a β-propeller tertiary structure. Kelch-repeat β-propellers are generally involved in protein-protein interactions, though the large diversity of domain architectures and limited sequence identity between kelch motifs make characterisation of the kelch superfamily difficult.

Structure[edit]

The N-terminus of several Kelch proteins contain other protein domains, including Discoidin, F-box, and Broad-complex, Tramtrack, Bric-a-Brac/Poxvirus and Zincfinger (BTB/POZ) domains. Kelch proteins may also have only a β-propeller architecture only. The BTB domain of kelch proteins (if present) allows the formation of homo- or heterodimers that mediate protein-protein interactions.

The C-terminus of Kelch proteins contains kelch repeats. Each kelch repeat is a sequence of 44-55 amino acids in length, usually occurring in clusters of 4 - 7 repeats.

Each kelch repeat forms a "blade" of the β-propeller fold, consisting of a four-stranded antiparallel β-sheet secondary structure, arranged radially around a central axis, packed onto its adjoining repeats via hydrophobic contacts.

Kelch-repeat β-propellers undergo a variety of binding interactions with other proteins, notably the actin filaments of a cell.

Function[edit]

Kelch like proteins are known to act as substrate adaptors for Cullin 3 ubiquitin ligases.

Organisms[edit]

The first Kelch protein (from which this family derives its name) was isolated from Drosophila, in which Kelch-mutant females lay sterile, cup-shaped eggs;[1] "Kelch" is German for "chalice", or "cup". Kelch proteins have also been isolated in many other animals, bacteria, fungi, and even virus (restricted to Poxviridae).

Human proteins containing Kelch motifs[edit]

ATRN; ATRNL1; CCIN; ENC1; FBXO42; GAN; HCFC1; HCFC2; IPP; IVNS1ABP; KBTBD10; KBTBD11; KBTBD2; KBTBD3; KBTBD4; KBTBD5; KBTBD6; KBTBD7; KBTBD8; KEAP1; KIAA1900; KLHDC1; KLHDC2; KLHDC3; KLHDC4; KLHDC5; KLHDC7A; KLHDC7B; KLHDC8A; KLHDC8B; KLHDC9; KLHL1; KLHL10; KLHL11; KLHL12; KLHL13; KLHL14; KLHL15; KLHL17; KLHL18; KLHL2; KLHL20; KLHL21; KLHL22; KLHL23; KLHL24; KLHL25; KLHL26; KLHL28; KLHL29; KLHL3; KLHL30; KLHL31; KLHL32; KLHL34; KLHL4; KLHL40; KLHL5; KLHL6; KLHL7; KLHL8; KLHL9; LZTR1; MEGF8; MKLN1; RABEPK; SARCOSIN;

References[edit]

  1. ^ UNDERSTANDING THE FUNCTION OF ACTIN-BINDING PROTEINS THROUGH GENETIC ANALYSIS OF DROSOPHILA OOGENESIS, by Andrew M. Hudson and Lynn Cooley; in the Annual Review of Genetics, Vol. 36: 455-488 (Volume publication date December 2002); retrieved December 12, 2013


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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
(179)
Full
(1811)
Representative proteomes NCBI
(11207)
Meta
(344)
RP15
(462)
RP35
(599)
RP55
(827)
RP75
(1125)
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  Seed
(179)
Full
(1811)
Representative proteomes NCBI
(11207)
Meta
(344)
RP15
(462)
RP35
(599)
RP55
(827)
RP75
(1125)
Alignment:
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  Seed
(179)
Full
(1811)
Representative proteomes NCBI
(11207)
Meta
(344)
RP15
(462)
RP35
(599)
RP55
(827)
RP75
(1125)
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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.

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Curation and family details

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Seed source: Jackhmmer:Q9CAE9
Previous IDs: none
Type: Repeat
Author: Coggill P
Number in seed: 179
Number in full: 1811
Average length of the domain: 52.00 aa
Average identity of full alignment: 22 %
Average coverage of the sequence by the domain: 10.77 %

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 25.3 25.3
Trusted cut-off 25.3 25.3
Noise cut-off 25.2 25.2
Model length: 50
Family (HMM) version: 1
Download: download the raw HMM for this family

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