{PDOC51998}
{PS51998; DEK_C}
{BEGIN}
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* DEK C-terminal (DEK-C) domain profile *
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The DEK-C domain was first detected in the C-terminal region of the chromatin-
associated protein  DEK.  The  DEK-C  domain  is  able  to bind DNA and induce
protein-protein interactions, but its function remains unknown [1].

The DEK  C-terminal  domain  consists  of three tightly packed, twisted alpha-
helices that  are  arranged  around a well-packed core of hydrophobic residues
(see <PDB:1Q1V>). The middle helix is the shortest and the C-terminal helix is
the longest. Despite the structural similarity with winged helix proteins, the
DNA-interaction mechanism  of the DEK C-terminal domain appears different from
that of  winged  helix  proteins, as it uses the second helix to interact with
DNA, whereas  other winged helix proteins use the third helix to interact with
DNA [2].

Some proteins known to contain a DEK-C domain are listed below:

 - Animal  DEK, a chromatin associated protein able to modify the structure of
   DNA and  originally  described  as  a proto-oncogene protein. DEK acts as a
   transcriptional inhibitor [1,2].
 - Arabidopsis thaliana DEK3, a chromatin-associated protein [3].
 - Animal   Slingshot   (SSH)   proteins,   phosphatases   that   specifically
   dephosphorylate and activate cofilin, an F-actin-severing protein [4].
 - Fungal chitin synthases (ChSs) [5,6].

The profile we developed covers the entire DEK-C domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: April 2022 / First entry.

[ 1] Kappes F., Scholten I., Richter N., Gruss C., Waldmann T.
     "Functional domains of the ubiquitous chromatin protein DEK."
     Mol. Cell. Biol. 24:6000-6010(2004).
     PubMed=15199153; DOI=10.1128/MCB.24.13.6000-6010.2004
[ 2] Devany M., Kotharu N.P., Matsuo H.
     "Solution NMR structure of the C-terminal domain of the human protein
     DEK."
     Protein. Sci. 13:2252-2259(2004).
     PubMed=15238633; DOI=10.1110/ps.04797104
[ 3] Waidmann S., Kusenda B., Mayerhofer J., Mechtler K., Jonak C.
     "A DEK domain-containing protein modulates chromatin structure and
     function in Arabidopsis."
     Plant. Cell. 26:4328-4344(2014).
     PubMed=25387881; DOI=10.1105/tpc.114.129254
[ 4] Takahashi K., Okabe H., Kanno S.I., Nagai T., Mizuno K.
     "A pleckstrin homology-like domain is critical for F-actin binding and
     cofilin-phosphatase activity of Slingshot-1."
     Biochem. Biophys. Res. Commun. 482:686-692(2017).
     PubMed=27865840; DOI=10.1016/j.bbrc.2016.11.095
[ 5] Sheng W., Yamashita S., Ohta A., Horiuchi H.
     "Functional differentiation of chitin synthases in Yarrowia
     lipolytica."
     Biosci. Biotechnol. Biochem. 77:1275-1281(2013).
     PubMed=23748777; DOI=10.1271/bbb.130111
[ 6] Fernandes C., Gow N.A.R., Gonçalves T.
     "The importance of subclasses of chitin synthase enzymes with myosin-like
     domains for the fitness of fungi."
     Fungal Biol. Rev. 30:1–14(2016).
     DOI=10.1016/j.fbr.2016.03.002

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