Figure 2

Figure 2

Comparison of the amino acid sequences of ZBED domain between LOC569044 protein and other zebrafish ZBED proteins. (A) The alignment of amino acids of BED domains among zebrafish ZBED proteins. The DNA-binding BED domain was characterized by the signature C^x2C^xnH^x3-5H (xn indicates a variable spacer; yellow color). Blue color indicates that at least one amino acid residue among zebrafish ZBED proteins was identical to that of LOC569044 protein, while the red color indicates amino acid residue in all zebrafish ZBED proteins entirely identical to that of the LOC569044 protein. *: indicates that the amino acid residue is identical among all species examined. (B) Using the WebLogos (version 2.8.2) to analyze the consensus residues of amino acid and nucleic acid of conserved zinc finger BED domain (i) and hAT dimerization region (ii), respectively. The larger size of alphabetic letters represent a higher degree of consensus. (C) A predicted protein structure of LOC569044 protein. Four views of the predicated protein structures were demonstrated by a 180-degree rotation. Positions of N- and C-termini are labeled. Positions of the three domains are labeled by red boxes, and a hAT dimerization region is labeled by pink box.