DNA-binding domain found in DNA repair protein complementing XP-A cells (XPA), yeast DNA repair protein RAD14 and similar proteins
The family includes DNA repair protein complementing XP-A cells (XPA), yeast DNA repair protein RAD14, zinc transporter 9 (ZNT9) and similar proteins. XPA, also known as xeroderma pigmentosum group A-complementing protein (XPAC), is involved in DNA excision repair. It initiates repair by binding to damaged sites with various affinities, depending on the photoproduct and the transcriptional state of the region. Rad14 is involved in nucleotide excision repair. It binds specifically to damaged DNA and is required for the incision step. Rad14 is a component of the nucleotide excision repair factor 1 (NEF1) complex consisting of Rad1, Rad10 and Rad14. ZNT9, also known as solute carrier family 30 member 9 (SLC30A9), may act as a zinc transporter involved in intracellular zinc homeostasis and may also play a role as nuclear receptor coactivator. The model corresponds to the DNA-binding domain found in XPA and Rad14. It consists of a conserved N-terminal zinc-binding subdomain and a C-terminal alpha/beta fold subdomain. ZNT9 contains only C-terminal alpha/beta fold subdomain but lacks of N-terminal zinc-binding subdomain.