Figure 1.
Figure 1. Sequence homology between EHZF and human OAZ. (A) Comparison of the amino acid sequences of EHZF and OAZ. The alignment was performed with the ClusteralW/fasta program (European Bioformatics Institute, Cambridgeshire, UK). Zinc fingers are underlined. The overall homology of the amino acid sequences was 63.5%. (B) Homology of the 30 zinc fingers of EHZF with those of OAZ. The zinc fingers are numbered 1-30 as described,8 and the percentage of amino acids identical between EHZF and the OAZ sequence is calculated for each zinc finger. The regions of OAZ reported to be responsible for interactions with the CCGCCC motif, Xvent BRE activation, Smad 1/4, or Olf/EBF interaction are indicated as described.8 (C) The first 80 amino acids of EHZF, which contain the N-terminal domain not present in OAZ, were analyzed using the Blastp alignment Mview program.16 The amino acids highlighted in gray are those shared by multiple proteins.

Sequence homology between EHZF and human OAZ. (A) Comparison of the amino acid sequences of EHZF and OAZ. The alignment was performed with the ClusteralW/fasta program (European Bioformatics Institute, Cambridgeshire, UK). Zinc fingers are underlined. The overall homology of the amino acid sequences was 63.5%. (B) Homology of the 30 zinc fingers of EHZF with those of OAZ. The zinc fingers are numbered 1-30 as described, and the percentage of amino acids identical between EHZF and the OAZ sequence is calculated for each zinc finger. The regions of OAZ reported to be responsible for interactions with the CCGCCC motif, Xvent BRE activation, Smad 1/4, or Olf/EBF interaction are indicated as described. (C) The first 80 amino acids of EHZF, which contain the N-terminal domain not present in OAZ, were analyzed using the Blastp alignment Mview program.16  The amino acids highlighted in gray are those shared by multiple proteins.

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