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InterPro: IPR019782 WD40 repeat 2

Protein matchesHelp
UniProtKB
Matches:
21107 proteins
AccessionHelp IPR019782 WD40_repeat_2
TypeHelp Repeat
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR019781 WD40 repeat, subgroup
Found in IPR000664 Lethal(2) giant larvae protein
IPR001632 G-protein, beta subunit
IPR009146 Groucho/transducin-like enhancer
IPR011046 WD40 repeat-like-containing domain
IPR015505 Coronin
IPR015943 WD40/YVTN repeat-like-containing domain
IPR016346 Guanine nucleotide-binding protein, beta subunit
IPR016391 Coatomer, alpha subunit
IPR016453 Coatomer, beta' subunit
IPR017149 Glutathione degradosome, DUG2
IPR017233 WD repeat protein 35
IPR017251 Apoptotic protease-activating factor 1
IPR017252 Dynein regulator
IPR017383 Actin-related protein 2/3 complex, subunit 1
IPR017399 WD repeat protein 23
IPR017422 WD repeat protein 55
IPR017986 WD40-repeat-containing domain
Contains IPR019775 WD40 repeat, conserved site
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

WD-40 repeats (also known as WD or beta-transducin repeats) are short ~40 amino acid motifs, often terminating in a Trp-Asp (W-D) dipeptide. WD40 repeats usually assume a 7-8 bladed beta-propeller fold, but proteins have been found with 4 to 16 repeated units, which also form a circularised beta-propeller structure. WD-repeat proteins are a large family found in all eukaryotes and are implicated in a variety of functions ranging from signal transduction and transcription regulation to cell cycle control and apoptosis. Repeated WD40 motifs act as a site for protein-protein interaction, and proteins containing WD40 repeats are known to serve as platforms for the assembly of protein complexes or mediators of transient interplay among other proteins. The specificity of the proteins is determined by the sequences outside the repeats themselves. Examples of such complexes are G proteins (beta subunit is a beta-propeller), TAFII transcription factor, and E3 ubiquitin ligase [1, 2]. In Arabidopsis spp., several WD40-containing proteins act as key regulators of plant-specific developmental events.

The repeat profile in this entry represents the central core of the domain (positions 9 to 23).

Structural linksHelp
PDB - click here
SCOP: b.69.4.1 , b.69.4.2
CATH: 2.130.10.10

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR019782 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O14727 Apoptotic protease-activating factor 1

O89053 Coronin-1A

P07834 Cell division control protein 4

Q11176 Actin-interacting protein 1

Q24246 Dynein intermediate chain, cytosolic

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR002182 NB-ARC
IPR019775 WD40 repeat, conserved site
IPR017986 WD40-repeat-containing domain
IPR015505 Coronin
IPR015048 Domain of unknown function DUF1899
IPR019782 WD40 repeat 2
IPR001810 Cyclin-like F-box
IPR015049 Domain of unknown function DUF1900
IPR019781 WD40 repeat, subgroup
IPR011029 DEATH-like
IPR017251 Apoptotic protease-activating factor 1
IPR011046 WD40 repeat-like-containing domain
IPR001680 WD40 repeat
IPR001315 Caspase Recruitment
IPR020472 G-protein beta WD-40 repeat, region
IPR000767 Disease resistance protein
IPR015943 WD40/YVTN repeat-like-containing domain
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Li D, Roberts R.
WD-repeat proteins: structure characteristics, biological function, and their involvement in human diseases.
Cell. Mol. Life Sci. 58 2085-97 2001 [PubMed: 11814058]
http://dx.doi.org/10.1007/PL00000838
2. Smith TF, Gaitatzes C, Saxena K, Neer EJ.
The WD repeat: a common architecture for diverse functions.
Trends Biochem. Sci. 24 181-5 1999 [PubMed: 10322433]
http://dx.doi.org/10.1016/S0968-0004(99)01384-5

Additional ReadingHelp
Hao B, Oehlmann S, Sowa ME, Harper JW, Pavletich NP.
Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases.
Mol. Cell 26 2007 131-43 [PubMed: 17434132]
http://dx.doi.org/10.1016/j.molcel.2007.02.022
Nolen BJ, Pollard TD.
Insights into the influence of nucleotides on actin family proteins from seven structures of Arp2/3 complex.
Mol. Cell 26 2007 449-57 [PubMed: 17499050]
http://dx.doi.org/10.1016/j.molcel.2007.04.017
Gilman AG.
G proteins: transducers of receptor-generated signals.
Annu. Rev. Biochem. 56 1987 615-49 [PubMed: 3113327]
http://dx.doi.org/10.1146/annurev.bi.56.070187.003151
Larsen NA, Al-Bassam J, Wei RR, Harrison SC.
Structural analysis of Bub3 interactions in the mitotic spindle checkpoint.
Proc. Natl. Acad. Sci. U.S.A. 104 2007 1201-6 [PubMed: 17227844]
http://dx.doi.org/10.1073/pnas.0610358104
Duronio RJ, Gordon JI, Boguski MS.
Comparative analysis of the beta transducin family with identification of several new members including PWP1, a nonessential gene of Saccharomyces cerevisiae that is divergently transcribed from NMT1.
Proteins 13 1992 41-56 [PubMed: 1594577]
http://dx.doi.org/10.1002/prot.340130105
Johnston CA, Kimple AJ, Giguere PM, Siderovski DP.
Structure of the parathyroid hormone receptor C terminus bound to the G-protein dimer Gbeta1gamma2.
Structure 16 2008 1086-94 [PubMed: 18611381]
http://dx.doi.org/10.1016/j.str.2008.04.010
Cheever ML, Snyder JT, Gershburg S, Siderovski DP, Harden TK, Sondek J.
Crystal structure of the multifunctional Gbeta5-RGS9 complex.
Nat. Struct. Mol. Biol. 15 2008 155-62 [PubMed: 18204463]
http://dx.doi.org/10.1038/nsmb.1377
Neer EJ, Schmidt CJ, Nambudripad R, Smith TF.
The ancient regulatory-protein family of WD-repeat proteins.
Nature 371 1994 297-300 [PubMed: 8090199]
http://dx.doi.org/10.1038/371297a0
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InterPro 23.1