Sequence alignment analysis on human Dicer

This data includes three Figures that are showing the sequence alignment analysis on human Dicer. Figure one: (A) Analysis of the DUF283 domain within human Dicer. Primary sequence alignment analysis of the DUF283 domain was performed based on Arabidopsis DUF283. Secondary structure prediction of hDicer DUF283 domain was also shown as indicated. (B) Sequence alignment of different RNase III domains was performed, based on the structure of Aquifex RNase III. All RNase III domains are mainly made of 9 a-helices as indicated. Red triangles mark the highly conserved amino acids in all the RNase III domains responsible for binding magnesium ions. Blue triangles indicate the residues responsible for dimerization. Figure two: Conservation of hDicer DExD/H-box helicase domain with its homologues. Sequence alignment among the helicase domains of RLH family members. Figure three: Conservation of Dicer’s DExD/H-box helicase domains among different species. Sequence alignment of DExD/H-box helicase domains from human, mouse, zebrafish, chicken, Arabidopsis and Drosophila.本数据集涵盖三张展示人类Dicer（Dicer）蛋白序列比对分析的图。 图1：(A) 人类Dicer的DUF283结构域（DUF283 domain）分析：基于拟南芥DUF283结构域，开展了人类Dicer DUF283结构域的一级序列比对分析，并如标注所示呈现了hDicer DUF283结构域的二级结构预测结果。(B) 基于Aquifex核糖核酸酶III（RNase III）的结构，开展不同核糖核酸酶III（RNase III）结构域的序列比对分析。所有核糖核酸酶III结构域均主要由9个α-螺旋构成，如标注所示。红色三角标记所有核糖核酸酶III结构域中负责结合镁离子的高度保守氨基酸残基；蓝色三角标注参与二聚化作用的氨基酸残基。 图2：人类Dicer的DExD/H盒解旋酶结构域（DExD/H-box helicase domain）与其同源蛋白的保守性分析：呈现了RLH家族（RLH family）成员解旋酶结构域的序列比对结果。 图3：不同物种中Dicer的DExD/H盒解旋酶结构域的保守性分析：涵盖了人类、小鼠、斑马鱼、鸡、拟南芥以及果蝇的DExD/H盒解旋酶结构域的序列比对结果。