The MYND-type zinc finger was called after the three best characterized members of the family (MYeloid translocation protein 8 (MTG8/ETO), Nervy protein and Deaf-1) [1]. In MTG8 and Bop proteins this domain is important for the recruitment of a repressive complexe containing histone deacetylase (HDAC) activity [2,3]. In M2-type chronic leukemia where AML1 is fused to MTG8, AML1, normaly a transcriptional activator, is converted into a transcriptional repressor. The MYND domain of MTG8 is essential for this conversion and seems to function by recruiting the nuclear co-repressor N-CoR/mSin3A and HDACs complexes to DNA sites specified by AML1 [2].

The MYND-type zinc finger contains 8 amino acids that can coordinate 2 zinc atoms.

Some proteins containing a MYND-type zinc finger are listed below:

• Mammalian MTG8/ETO protein. MTG8 is part of a high molecular weight complex that contains co-repressors and HDACs.
• Drosophila Nervy protein, a homologue of MTG8.
• Animal Deformed epidermal autoregulatory factor 1 (Deaf-1). It was first identified in drosophila as a sequence-specific DNA binding protein that was isolated as a putative cofactor of the Hox protein Deformed (Dfd).
• Vertebrate Bop protein. In mouse it is expressed specifically in cardiac and muscle precursors before differentiation of these lineages.
• Mammalian programmed cell death protein 2 (PDCD2/RP8). It interacts with N-CoR/mSin3A complexes and with Host cell factor 1 (HCF1), a component of the C1 complex [4].
• Adenovirus 5 E1A-binding protein (BS69). It binds to the transactivation domain of the adenovirus type 5 E1A 32 kda protein (289R) and inhibits its transactivating activity.

The profile and the pattern we developed cover the whole domain.