| Summary: | Heat-shock proteins (HSP) are conserved chaperones crucial for protein degradation, maturation, and refolding. These adenosine triphosphate dependent chaperones were classified based on their molecular mass that ranges between 10–100 kDA, including; <i>HSP10</i>, <i>HSP40</i>, <i>HSP70</i>, <i>HSP90</i>, <i>HSPB1</i>, <i>HSPD</i>, and <i>HSPH1</i> family. HSPs are essential for cellular responses and imperative for protein homeostasis and survival under stress conditions. This study performed a computational analysis of the HSP protein family to better understand these proteins at the molecular level. Physiochemical properties, multiple sequence alignment, and phylogenetic analysis were performed for 64 HSP genes in the <i>Bubalus bubalis</i> genome. Four genes were identified as belonging to the <i>HSP90</i> family, 10 to <i>HSP70</i>, 39 to <i>HSP40</i>, 8 to <i>HSPB</i>, one for each <i>HSPD</i>, <i>HSPH1</i>, and <i>HSP10</i>, respectively. The aliphatic index was higher for <i>HSP90</i> and <i>HSP70</i> as compared to the <i>HSP40</i> family, indicating their greater thermostability. Grand Average of hydropathicity Index values indicated the hydrophilic nature of <i>HSP90</i>, <i>HSP70</i>, and <i>HSP40</i>. Multiple sequence alignment indicated the presence of highly conserved consensus sequences that are plausibly significant for the preservation of structural integrity of proteins. In addition, this study has expanded our current knowledge concerning the genetic diversity and phylogenetic relatedness of HSPs of buffalo with other mammalian species. The phylogenetic tree revealed that buffalo is more closely related to <i>Capra hircus</i> and distantly associated with <i>Danio rerio</i>. Our findings provide an understanding of HSPs in buffalo at the molecular level for the first time. This study highlights functionally important HSPs and indicates the need for further investigations to better understand the role and mechanism of HSPs.
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