PROSITE documentation PDOC51821
Velvet domain profile


The fungus-specific velvet family of regulatory proteins plays a key role in coordinating secondary metabolism and differenciation 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, wich 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 [1,2].

The velvet domain is an RHD-like domain (see <PDOC00924>) related to NF-kappaB. It folds into a highly twisted β-sandwich composed of seven antiparallel β-strands (see <PDB:4N6Q>). 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 [1,2].

The profile we developed covers the entire velvet domain.

Last update:

November 2016 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

VELVET, PS51821; Velvet domain profile  (MATRIX)


1AuthorsBayram O. Braus G.H.
TitleCoordination of secondary metabolism and development in fungi: the velvet family of regulatory proteins.
SourceFEMS Microbiol. Rev. 36:1-24(2012).
PubMed ID21658084

2AuthorsAhmed Y.L. Gerke J. Park H.-S. Bayram O. Neumann P. Ni M. Dickmanns A. Kim S.C. Yu J.-H. Braus G.H. Ficner R.
TitleThe velvet family of fungal regulators contains a DNA-binding domain structurally similar to NF-kappaB.
SourcePLoS Biol. 11:E1001750-E1001750(2013).
PubMed ID24391470

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