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In silico prediction of molecular and functional annotation of hypothetical protein (ABC47680) of Acinetobacter venetianus |
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| รหัสดีโอไอ | |
| Creator | Sumaiya H. Omy |
| Title | In silico prediction of molecular and functional annotation of hypothetical protein (ABC47680) of Acinetobacter venetianus |
| Contributor | Sadia H. Tonny, Prodipto B. Angon, Zahirul A. Talukder |
| Publisher | Asia-Pacific Journal of Science and Technology |
| Publication Year | 2566 |
| Journal Title | Asia-Pacific Journal of Science and Technology |
| Journal Vol. | 28 |
| Journal No. | 3 |
| Page no. | 12 |
| Keyword | Acinetobactervenetianus, Bioinformatics tool, Hypothetical protein, Bacterial Genome, ParE_toxin |
| URL Website | https://www.tci-thaijo.org/index.php/APST |
| Website title | https://so01.tci-thaijo.org/index.php/APST/article/view/255092 |
| ISSN | 2539-6293 |
| Abstract | Acinetobacter venetianus is a non-motile coccobacilli bacterium that is aerobic, gram-negative, has positive catalytic activity, and exhibits negative oxidative behavior. Enormous data on hypothetical or uncharacterized proteins are available in the genomic database of the bacteria. Therefore, appropriate bioinformatics tools are essential for gaining a complete understanding of the bacterial genome. Several bioinformatics approaches were used in this study to determine the prognosis of structural and functional data of the targeted hypothetical protein. An in-silico approach was used to determine several features of the hypothetical protein (HP) (ABC47680) and compare the sequences of related proteins. Various bioinformatics tools were used, including NCBI-search, MEGA-7, ExPASy ProtPram, PSORTb, SWISS-MODEL, and PSIPRED for secondary structure predictions. Physicochemical properties, subcellular localization prediction, and identification were performed, followed by subsequent examination using several approaches. An alpha helix with an extended strand was the secondary predicted structure. After validating with different servers, the tertiary structure of the protein with maximum similarity in our study was revealed. Through functional annotation, the ParE toxin superfamily was discovered as domain containing an oligonucleotide-binding (OB)-fold protein with a beta barrel, and it's a virulent protein. The OB fold protein is involved in ribonucleic acid (RNA) binding, while ParE is involved in deoxy ribonucleic acid (DNA) damage repair and environmental stress response. The protein promotes plasmid partitioning while inhibiting the process of DNA replication and cell development. Our study on in silico prediction of hypothetical protein Acinetobacter venetianus could be used to combat crop pests, human activities, and distinctive environmental purposes. |
