InterPro domain: IPR041983

This entry represents the ZZ-type Zinc finger found in ADA2-like proteins, including transcriptional adapter 2 (TADA2) from animals and plants, and Ada2 from yeasts. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding [ 1 ].

Ada2 is a component of the SAGA/ADA coactivator complex, which regulates numerous cellular processes by coordinating histone acetylation [ 2 , 3 ].

There are two Drosophila Ada2 homologues, dAda2a and dAda2b. dAda2b is a component of Spt-Ada-Gcn5-acetyltransferase (SAGA) complexes, while dAda2a associates with dGcn5 but is not incorporated into dSAGA-type complexes [ 4 ].

Mammalian TADA2 is a component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. The ATAC complex is involved in mammalian development, histone acetylation, cell cycle progression, and prevention of apoptosis during embryogenesis [ 5 ].

1. ZZ domain of CBP: an unusual zinc finger fold in a protein interaction module. J. Mol. Biol. 343, 1081-93
2. The SANT domain of Ada2 is required for normal acetylation of histones by the yeast SAGA complex. J. Biol. Chem. 277, 8178-86
3. Genome-wide mapping of the coactivator Ada2p yields insight into the functional roles of SAGA/ADA complex in Candida albicans. Mol. Biol. Cell 20, 2389-400
4. Two Drosophila Ada2 homologues function in different multiprotein complexes. Mol. Cell. Biol. 23, 3305-19
5. The double-histone-acetyltransferase complex ATAC is essential for mammalian development. Mol. Cell. Biol. 29, 1176-88