InterPro domain: IPR015943

This superfamily represents a WD40/YVTN repeat-like domain. Both the WD40 and the YVTN repeated motifs consist of about 40 residues, and although they consist of distinct sequences, they do share a similar structure. Structurally, both the WD40 and the YVTN repeated motifs form seven-bladed propellers (although some members can contain eight blades), which consist of seven 4-stranded beta-sheets.

The WD40-type repeat domain is found in the beta-1 subunit of the signal-transducing G protein [ 1 ], in yeast Tup1 protein [ 2 ], in Groucho [ 3 ], in the yeast cell cycle protein Cdc4 [ 4 ] and in actin-interacting protein 1 [ 5 ].

The YVTN-type repeat domain is found in archaeal surface layer proteins (SLPs) that protect cells from extreme environments [ 6 ], in quinohemoprotein amine dehydrogenase (QHNDH) [ 7 ], and in methylamine dehydrogenase [ 8 ].

1. A molecular mechanism for the phosphorylation-dependent regulation of heterotrimeric G proteins by phosducin. Mol. Cell 3, 649-60
2. Structure of the C-terminal domain of Tup1, a corepressor of transcription in yeast. EMBO J. 19, 3016-27
3. Crystal structure of the C-terminal WD40 repeat domain of the human Groucho/TLE1 transcriptional corepressor. Structure 10, 751-61
4. Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase. Cell 112, 243-56
5. Identification of functional residues on Caenorhabditis elegans actin-interacting protein 1 (UNC-78) for disassembly of actin depolymerizing factor/cofilin-bound actin filaments. J. Biol. Chem. 279, 31697-707
6. Archaeal surface layer proteins contain beta propeller, PKD, and beta helix domains and are related to metazoan cell surface proteins. Structure 10, 1453-64
7. Structure of the phenylhydrazine adduct of the quinohemoprotein amine dehydrogenase from Paracoccus denitrificans at 1.7 A resolution. Acta Crystallogr. D Biol. Crystallogr. 59, 1551-6
8. Refined crystal structure of methylamine dehydrogenase from Paracoccus denitrificans at 1.75 A resolution. J. Mol. Biol. 276, 131-49