American Journal of Life Sciences

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Bioinformatics Analysis of the Structure and Function of CG17196 Protein of Drosophila Melanogaster

Received: 25 May 2015    Accepted: 06 June 2015    Published: 01 July 2015
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Abstract

Recent studies have suggested that chimeric genes may account for the formation and evolution of new genes and functional divergence. However, the biological function of the new chimeric gene CG17196 of Drosophila melanogaster remains unknown, therefore, this study aims to analyze the structure and function of CG17196 protein using bioinformatics methods. Based on the amino acid sequence of CG17196 protein from NCBI database, the bioinformatics analyses were performed, including protein physical and chemical properties, transmembrane region, signal peptide, subcellular localization, domain, tertiary structure, and the phylogenetic tree of CG17196 related proteins from different species. The results showed that CG17196 protein was an unstable hydrophobic protein, performing biological function in the endoplasmic reticulum. It contained DHHC-type zinc finger domain and three transmembrane regions, but without signal peptide. The prediction result of gene ontology showed that the chance that the CG17196 protein actually had palmitoyltransferase activity was 70%. CG17196 protein and its related proteins in Schizosaccharomyces pombe, Ashbya gossypii, Dictyostelium discoideum and Arabidopsis thaliana showed high homology. In conclusion, CG17196 protein belongs to DHHC protein family and contains palmitoyltransferase activity, which may participate in the protein palmitoylation in the endoplasmic reticulum of Drosophila melanogaster, providing theoretical references for further systematic research on the function and evolution of new chimera CG17196.

DOI 10.11648/j.ajls.20150304.13
Published in American Journal of Life Sciences (Volume 3, Issue 4, August 2015)
Page(s) 268-273
Creative Commons

This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.

Copyright

Copyright © The Author(s), 2024. Published by Science Publishing Group

Keywords

Chimeric Gene, New Genes, Palmitoylation, Bioinformatics, Drosophila Melanogaster

References
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Author Information
  • Medical College, Henan University of Science and Technology, Luoyang, Henan, China

  • Medical College, Henan University of Science and Technology, Luoyang, Henan, China

  • Medical College, Henan University of Science and Technology, Luoyang, Henan, China

  • Medical College, Henan University of Science and Technology, Luoyang, Henan, China

  • Medical College, Henan University of Science and Technology, Luoyang, Henan, China

  • Medical College, Henan University of Science and Technology, Luoyang, Henan, China

  • Medical College, Henan University of Science and Technology, Luoyang, Henan, China

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  • APA Style

    Hongchao Liu, Xianming Zou, Yiming Wang, Xuanlong Du, Qian Wang, et al. (2015). Bioinformatics Analysis of the Structure and Function of CG17196 Protein of Drosophila Melanogaster. American Journal of Life Sciences, 3(4), 268-273. https://doi.org/10.11648/j.ajls.20150304.13

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    ACS Style

    Hongchao Liu; Xianming Zou; Yiming Wang; Xuanlong Du; Qian Wang, et al. Bioinformatics Analysis of the Structure and Function of CG17196 Protein of Drosophila Melanogaster. Am. J. Life Sci. 2015, 3(4), 268-273. doi: 10.11648/j.ajls.20150304.13

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    AMA Style

    Hongchao Liu, Xianming Zou, Yiming Wang, Xuanlong Du, Qian Wang, et al. Bioinformatics Analysis of the Structure and Function of CG17196 Protein of Drosophila Melanogaster. Am J Life Sci. 2015;3(4):268-273. doi: 10.11648/j.ajls.20150304.13

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  • @article{10.11648/j.ajls.20150304.13,
      author = {Hongchao Liu and Xianming Zou and Yiming Wang and Xuanlong Du and Qian Wang and Junbao Xie and Xinming Tu},
      title = {Bioinformatics Analysis of the Structure and Function of CG17196 Protein of Drosophila Melanogaster},
      journal = {American Journal of Life Sciences},
      volume = {3},
      number = {4},
      pages = {268-273},
      doi = {10.11648/j.ajls.20150304.13},
      url = {https://doi.org/10.11648/j.ajls.20150304.13},
      eprint = {https://download.sciencepg.com/pdf/10.11648.j.ajls.20150304.13},
      abstract = {Recent studies have suggested that chimeric genes may account for the formation and evolution of new genes and functional divergence. However, the biological function of the new chimeric gene CG17196 of Drosophila melanogaster remains unknown, therefore, this study aims to analyze the structure and function of CG17196 protein using bioinformatics methods. Based on the amino acid sequence of CG17196 protein from NCBI database, the bioinformatics analyses were performed, including protein physical and chemical properties, transmembrane region, signal peptide, subcellular localization, domain, tertiary structure, and the phylogenetic tree of CG17196 related proteins from different species. The results showed that CG17196 protein was an unstable hydrophobic protein, performing biological function in the endoplasmic reticulum. It contained DHHC-type zinc finger domain and three transmembrane regions, but without signal peptide. The prediction result of gene ontology showed that the chance that the CG17196 protein actually had palmitoyltransferase activity was 70%. CG17196 protein and its related proteins in Schizosaccharomyces pombe, Ashbya gossypii, Dictyostelium discoideum and Arabidopsis thaliana showed high homology. In conclusion, CG17196 protein belongs to DHHC protein family and contains palmitoyltransferase activity, which may participate in the protein palmitoylation in the endoplasmic reticulum of Drosophila melanogaster, providing theoretical references for further systematic research on the function and evolution of new chimera CG17196.},
     year = {2015}
    }
    

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  • TY  - JOUR
    T1  - Bioinformatics Analysis of the Structure and Function of CG17196 Protein of Drosophila Melanogaster
    AU  - Hongchao Liu
    AU  - Xianming Zou
    AU  - Yiming Wang
    AU  - Xuanlong Du
    AU  - Qian Wang
    AU  - Junbao Xie
    AU  - Xinming Tu
    Y1  - 2015/07/01
    PY  - 2015
    N1  - https://doi.org/10.11648/j.ajls.20150304.13
    DO  - 10.11648/j.ajls.20150304.13
    T2  - American Journal of Life Sciences
    JF  - American Journal of Life Sciences
    JO  - American Journal of Life Sciences
    SP  - 268
    EP  - 273
    PB  - Science Publishing Group
    SN  - 2328-5737
    UR  - https://doi.org/10.11648/j.ajls.20150304.13
    AB  - Recent studies have suggested that chimeric genes may account for the formation and evolution of new genes and functional divergence. However, the biological function of the new chimeric gene CG17196 of Drosophila melanogaster remains unknown, therefore, this study aims to analyze the structure and function of CG17196 protein using bioinformatics methods. Based on the amino acid sequence of CG17196 protein from NCBI database, the bioinformatics analyses were performed, including protein physical and chemical properties, transmembrane region, signal peptide, subcellular localization, domain, tertiary structure, and the phylogenetic tree of CG17196 related proteins from different species. The results showed that CG17196 protein was an unstable hydrophobic protein, performing biological function in the endoplasmic reticulum. It contained DHHC-type zinc finger domain and three transmembrane regions, but without signal peptide. The prediction result of gene ontology showed that the chance that the CG17196 protein actually had palmitoyltransferase activity was 70%. CG17196 protein and its related proteins in Schizosaccharomyces pombe, Ashbya gossypii, Dictyostelium discoideum and Arabidopsis thaliana showed high homology. In conclusion, CG17196 protein belongs to DHHC protein family and contains palmitoyltransferase activity, which may participate in the protein palmitoylation in the endoplasmic reticulum of Drosophila melanogaster, providing theoretical references for further systematic research on the function and evolution of new chimera CG17196.
    VL  - 3
    IS  - 4
    ER  - 

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