Table of Contents
Molecular Biology International
Volume 2016 (2016), Article ID 9156735, 8 pages
http://dx.doi.org/10.1155/2016/9156735
Research Article

Analyses of Physcomitrella patens Ankyrin Repeat Proteins by Computational Approach

1Graduate Program in Experimental Medicine, McGill University, Montreal, QC, Canada H2X 0A8
2Graduate Program in Biological Sciences, University of Manitoba, Winnipeg, MB, Canada R3T 2N2

Received 7 March 2016; Revised 18 May 2016; Accepted 25 May 2016

Academic Editor: Abdelali Hannoufa

Copyright © 2016 Niaz Mahmood and Nahid Tamanna. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Ankyrin (ANK) repeat containing proteins are evolutionary conserved and have functions in crucial cellular processes like cell cycle regulation and signal transduction. In this study, through an entirely in silico approach using the first release of the moss genome annotation, we found that at least 54 ANK proteins are present in P. patens. Based on their differential domain composition, the identified ANK proteins were classified into nine subfamilies. Comparative analysis of the different subfamilies of ANK proteins revealed that P. patens contains almost all the known subgroups of ANK proteins found in the other angiosperm species except for the ones having the TPR domain. Phylogenetic analysis using full length protein sequences supported the subfamily classification where the members of the same subfamily almost always clustered together. Synonymous divergence (dS) and nonsynonymous divergence (dN) ratios showed positive selection for the ANK genes of P. patens which probably helped them to attain significant functional diversity during the course of evolution. Taken together, the data provided here can provide useful insights for future functional studies of the proteins from this superfamily as well as comparative studies of ANK proteins.