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¡¶±±·½Ô°ÒÕ¡·[ISSN:1001-0009/CN:23-1247/S]

Issue:

2016Äê13

Page:

93-97

Research Field:

Publishing date:

Info

Title:

Bioinformatics Analysis of the ª«PAPª« Gene Analogs in ª«Brassica napus

Author(s):

ZOU Chunyang; ZANG Xin; YANG Dongzhi; CAO Gangqiang; JIAO Sikai

(School of Life Science,Zhengzhou University,Zhengzhou,Henan 450001)

Keywords:

Brassica napus; PAPª« gene; bioinformatics; function prediction

PACS:

-

DOI:

10.11937/bfyy.201613025

Abstract:

Bioinformatics network database and softwares were used to analyse and predict the biological properties of the ª«PAP ª«(purple acid phosphatase)gene analogs encoding protein in ª«Brassica napusª«.The physical and chemical properties,structure and function of the protein were predicted,in the cause of providing a theoretical foundation for the further study on the adjustment mechanism of phosphorus absorption and utilization ofª« Brassica napusª«.The results indicated that the gene encoded a length of 481 amino acid protein.The molecular formular was C2520ªªH3714ªªN666ªªO719ªªS19ªª.Its molecular weight was 55.45 kDa and the PI was 6.35.It was predicted that the protein was hydrophilic,secretary protein and instability,and there was a signal peptide.The protein had 3 transmembrane helical regions,3 coiled coil structures,39 potentialªª phosphorylation sites and 3 N-glycosylated sites.It was mainly located in the Golgi apparatus.Homologous analysis showed that the gene had the close genetic relationship with ª«Brassica napusª« ª«PAPª«12,and orthologous to ª«PAPª«12-5ªª.Random coil,extend chains and ¦Á-helix were the main secondary strructions of the protein,and it had obvious 10 helices and 26 folds.The protein had ª«PAPª«¡¯s conserved domains,which belonged to metal phosphodiesterase super family(MPP).The conserved domain analysis showed that it had two conserved motifs,seven metal-coordinating residues and six specific type functional sites,which predicted that the gene belonged to ª«Brassica napusª« ª«PAPª« gene family.Bioinformatics analysis and the protein structure and function prediction could provide theoretical guidance for further research on ª«Brassica napus PAPª«.ª¤

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