From The Gypsy Database

hATd dimerization domain is present in ZNF452/SCAND3 variants of SCAN/KRAB cellular integrases.

hATd dimerization domain (pfam05699 in Conserved Domain Database) has been described in Activator (Ac) and Hermes TRs (Essers et al. 2000; Michel et al. 2003) belonging to hAT family of transposable elements. It was reported to be the most highly conserved region of hAT TRs and involved in the required TR oligomerization to assemble the transpososome (synaptic complex). Nevertheless, Hickman et al. 2005 argue that hATd domain is a misnomer (not involved in dimerization ) and according to Hermes structure features hATd conserved residues do not form an independent folding unit but have an important role in joining into a functional whole residues separated in sequence.

The hATd domain has also been described in DREF factors (DNA replication related element binding factors) of Drosophila and humans (Hirose et al. 1996; Esposito et al. 1999; Ohshima et al. 2003). DREF factors are transcriptional regulators and in humans the hATd domain has been reported to play an essential role in hDREFs self association, and also required for nuclear accumulation, DNA binding activity and granular pattern formation (Yamashita et al. 2007).

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