Sequence alignment analysis on human Dicer

Published: 13-04-2018| Version 1 | DOI: 10.17632/bkz8c3js49.1
Contributors:
Zhongmin Liu,
Jia Wang,
Hang Cheng,
Xin Ke,
Lei Sun,
Qiangfeng Cliff Zhang,
Hong-Wei Wang

Description

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.

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