Analysis of fragment homology among 331bp myoglobin of green turtle (Chelonia mydas) with hypoxia-tolerant and hypoxia-intolerant organisms

Myoglobin protein plays significant role in intracellular oxygen storage and transcellular oxygen transport in the green turtle (Chelonia mydas). This globular protein contains amino acid compositions which have similarities between other species. This study aimed to analyse the fragment homology am...

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Bibliographic Details
Published in:IOP conference series. Earth and environmental science 2020-02, Vol.457 (1), p.12007
Main Authors: Puspitaningrum, R, Muthmainnah, Z, Anastasia, I M, Ruyani, S F
Format: Article
Language:English
Subjects:
Amino acid composition
Amino acids
Aquatic reptiles
Bioinformatics
Chelonia mydas
Composition
Genetic diversity
Homology
Hypoxia
Myoglobins
Organisms
Oxygen
oxygen homeostasis
Proteins
sea turtle conservation
Sequences
Structure-function relationships
Turtles
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Summary:Myoglobin protein plays significant role in intracellular oxygen storage and transcellular oxygen transport in the green turtle (Chelonia mydas). This globular protein contains amino acid compositions which have similarities between other species. This study aimed to analyse the fragment homology among 331bp myoglobin sequences of green turtle with hypoxia-tolerant and hypoxia-intolerant group organisms. Green turtle myoglobin sequences was aligned with 16 organisms for 84 amino acids number 71 to 154 in the N terminal region of the myoglobin protein. The data was analysed in BLASTX bioinformatics portal. The result showed that the percentage of similarity was 58%-93% with myoglobin in hypoxia-tolerant organisms and 79%-93% in hypoxia-intolerant organisms. Fragment homology in this study indicate the conserved positions of protein sequences during evolution in hypoxic tolerant organisms, which indicate that these positions may be important for the structure or function of myoglobin. Further study is needed to determine the difference of amino acid composition between these organisms.
ISSN:1755-1307
1755-1315
DOI:10.1088/1755-1315/457/1/012007