{PDOC51821}
{PS51821; VELVET}
{BEGIN}
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* Velvet domain profile *
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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  beta-sandwich  composed  of seven
antiparallel beta-strands  (see  <PDB:4N6Q>). One side of the beta-sandwich is
involved in dimer formation, whereas the other one is flanked by several loops
of which  two  fold  into  an  alpha-helix.  These alpha-helical fragments are
located between beta-strands 2 and 3 and at the C-terminus [1,2].

The profile we developed covers the entire velvet domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: November 2016 / First entry.

[ 1] Bayram O., Braus G.H.
     "Coordination of secondary metabolism and development in fungi: the
     velvet family  of regulatory proteins."
     FEMS Microbiol. Rev. 36:1-24(2012).
     PubMed=21658084; DOI=10.1111/j.1574-6976.2011.00285.x
[ 2] Ahmed 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.
     "The velvet family of fungal regulators contains a DNA-binding domain
     structurally similar to NF-kappaB."
     PLoS Biol. 11:E1001750-E1001750(2013).
     PubMed=24391470; DOI=10.1371/journal.pbio.1001750

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