IPR038491
Velvet domain superfamily
InterPro entry
Short name | Velvet_dom_sf |
Overlapping entries |
Description
The fungus-specific velvet family of regulatory proteins plays a key role in coordinating secondary metabolism and differentiation processes such as asexual or sexual sporulation and sclerotia or fruiting body formation. These velvet regulators are present in most parts of the fungal kingdom from chytrids to basidiomycetes. Velvet proteins interact with each other, alone ("homodimers"), in various combinations ("heterodimers"), and also with other proteins. The velvet proteins share a homologous region comprising about 150 amino acids, which lack significant sequence similarity to any other known proteins. The velvet domain is involved in specific DNA binding as well as in the dimerization of the different velvet proteins, resulting in the formation of homo- and heterodimers
[2, 1].
The velvet domain is an RHD-like domain related to NF-kappaB. It folds into a highly twisted β-sandwich composed of seven antiparallel β-strands. One side of the β-sandwich is involved in dimer formation, whereas the other one is flanked by several loops of which two fold into an α-helix. These α-helical fragments are located between β-strands 2 and 3 and at the C terminus
[2, 1].
References
1.The velvet family of fungal regulators contains a DNA-binding domain structurally similar to NF-κB. Ahmed YL, Gerke J, Park HS, Bayram O, Neumann P, Ni M, Dickmanns A, Kim SC, Yu JH, Braus GH, Ficner R. PLoS Biol. 11, e1001750, (2013). View articlePMID: 24391470
2.Coordination of secondary metabolism and development in fungi: the velvet family of regulatory proteins. Bayram O, Braus GH. FEMS Microbiol. Rev. 36, 1-24, (2012). View articlePMID: 21658084
Contributing Member Database Entry
- CATH-Gene3D:G3DSA:2.60.40.3960
Representative structure
4n6q: Crystal structure of VosA velvet domain