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InterPro: IPR011659 WD40-like Beta Propeller

Protein matchesHelp
UniProtKB
Matches:
2491 proteins
AccessionHelp IPR011659 PD40
TypeHelp Repeat
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR011042 Six-bladed beta-propeller, TolB-like
IPR012393 Peptidase S41B, tricorn core peptidase
IPR014167 Tol-Pal system beta propeller repeat-containing protein, TolB
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.

This region appears to be related to the IPR001680 repeat. This model is likely to miss copies within a sequence.

Structural linksHelp
SCOP: b.68.4.1
CATH: 2.120.10.30
Database linksHelp
PANDIT: PF07676
Blocks: IPB011659
Pfam Clan: CL0186.10

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR011659 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
A7UKV4 Dipeptidyl-peptidase 5

P0A855 Protein tolB

P95871 Tricorn protease homolog

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR012393 Peptidase S41B, tricorn core peptidase
IPR005151 Peptidase S41
IPR014167 Tol-Pal system beta propeller repeat-containing protein, TolB
IPR011044 Quinoprotein amine dehydrogenase, beta chain-like
IPR011042 Six-bladed beta-propeller, TolB-like
IPR001478 PDZ/DHR/GLGF
IPR011659 WD40-like Beta Propeller
IPR007195 TolB, N-terminal
IPR001375 Peptidase S9, prolyl oligopeptidase, catalytic domain
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
Carr S, Penfold CN, Bamford V, James R, Hemmings AM.
The structure of TolB, an essential component of the tol-dependent translocation system, and its protein-protein interaction with the translocation domain of colicin E9.
Structure 8 2000 57-66 [PubMed: 10673426]
http://dx.doi.org/10.1016/S0969-2126(00)00079-4
Abergel C, Bouveret E, Claverie JM, Brown K, Rigal A, Lazdunski C, Benedetti H.
Structure of the Escherichia coli TolB protein determined by MAD methods at 1.95 A resolution.
Structure 7 1999 1291-300 [PubMed: 10545334]
http://dx.doi.org/10.1016/S0969-2126(00)80062-3
Loftus SR, Walker D, Mate MJ, Bonsor DA, James R, Moore GR, Kleanthous C.
Competitive recruitment of the periplasmic translocation portal TolB by a natively disordered domain of colicin E9.
Proc. Natl. Acad. Sci. U.S.A. 103 2006 12353-8 [PubMed: 16894158]
http://dx.doi.org/10.1073/pnas.0603433103
Bonsor DA, Grishkovskaya I, Dodson EJ, Kleanthous C.
Molecular mimicry enables competitive recruitment by a natively disordered protein.
J. Am. Chem. Soc. 129 2007 4800-7 [PubMed: 17375930]
http://dx.doi.org/10.1021/ja070153n
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