Figure 1. The CaRF DNA binding domain is highly conserved across evolution.

CaRF amino acid sequences were obtained from the NCBI and Ensembl databases by BLAST similarity to mammalian CaRF (Table S2). Sequences were aligned using ClustalW. a) Phylogram representing the evolutionary distances between CaRF sequences in six species. b) Percent identity and similarity among amino acids in each domain of CaRF. The diagrams are drawn to scale and show four distinct domains of CaRF [14]. From left to right these are the N-terminus (corresponding to human coding exons 1–5), the DNA binding domain and nuclear localization signal (DBD/NLS, coding exons 6–7), an intermediate domain (coding exons 8–10), and the transcriptional activation domain (TAD, coding exons 11–14). The numbers between each pair of sequences show the percent of amino acids within that domain that are identical/conserved between that pair within each domain. Identity and conservation of amino acids were called by ClustalW, and insertions were scored as non-conserved amino acids. c) Sequence alignment of the DBD/NLS domain across all six species. Identical amino acids are highlighted black, conserved amino acids are gray and nonconserved changes are white.