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InterPro: IPR011046 WD40 repeat-like-containing domain

Protein matchesHelp
UniProtKB
Matches:
27621 proteins
AccessionHelp IPR011046 WD40_repeat-like_dom
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR015943 WD40/YVTN repeat-like-containing domain
Children IPR017986 WD40-repeat-containing domain
Found in IPR000009 Protein phosphatase 2A, regulatory subunit PR55
IPR000664 Lethal(2) giant larvae protein
IPR004083 Regulatory associated protein of TOR
IPR009146 Groucho/transducin-like enhancer
IPR011387 Translation initiation factor eIF-2A
IPR013863 Vacuolar import/degradation, Vid27-related
IPR015048 Domain of unknown function DUF1899
IPR015049 Domain of unknown function DUF1900
IPR015505 Coronin
IPR016346 Guanine nucleotide-binding protein, beta subunit
IPR016391 Coatomer, alpha subunit
IPR016453 Coatomer, beta' subunit
IPR016528 Vacuolar protein sorting-associated protein 11
IPR016616 Bardet-Biedl syndrome 2 protein
IPR016902 Vacuolar protein sorting-associated protein 41
IPR017149 Glutathione degradosome, DUG2
IPR017169 Anaphase-promoting complex, subunit 4
IPR017217 BLOC-2 complex, Hps5 subunit
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
Contains IPR001632 G-protein, beta subunit
IPR001680 WD40 repeat
IPR013577 Lethal giant larvae homologue 2
IPR018067 Protein phosphatase 2A, regulatory subunit PR55, conserved site
IPR019417 Protein of unknown function DUF2415
IPR019573 Serine/threonine-protein phosphatase 2A, subunit B, N-terminal
IPR019578 Serine-threonine phosphatase 2A, subunit B, alpha/ beta central domain
IPR019775 WD40 repeat, conserved site
IPR019781 WD40 repeat, subgroup
IPR019782 WD40 repeat 2
IPR020389 Aggregative adherence fimbria I, AAF/I
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 structures of several WD40 repeat-containing proteins have been determined, including the beta-1 subunit of the signal-transducing G protein heterotrimer, the C-terminal domain of yeast Tup1, the C-terminal domain of Groucho/tle1, the Cdc4 propeller domain, the bovine Arp2/3 complex 41 kDa subunit ARPC1, and actin interacting protein 1.

Structural linksHelp
PDB - click here

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR011046 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
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
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
Milam SL, Nicely NI, Feeney B, Mattos C, Clark AC.
Rapid folding and unfolding of Apaf-1 CARD.
J. Mol. Biol. 369 2007 290-304 [PubMed: 17408690]
http://dx.doi.org/10.1016/j.jmb.2007.02.105
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InterPro 23.1