Amino acid sequence alignments of human Pol δ C-terminal domain with CTDs of Pol α, Pol ϵ, and Pol ζ. The alignment was performed by ClustalW with default parameters and then adjusted manually to align the metal-binding cysteines. Secondary structure predictions were made using Phyre software (45). Conserved metal-binding cysteines, α-helices, and β-strands are highlighted in yellow, red, and cyan, respectively. In p125C and p353C, the first cysteines in MBS1 and MBS2 and the second cysteine in MBS2 are located in the α-helices.