In silico structural analysis, classification, and functional annotation of uncharacterized protein from Corbicula fluminea
TL;DR
Results confirmed the HSP70 sequence from C. fluminea as a member of HSP70 family and provide foundational insights into its structural and functional characteristics, contributing to the understanding of molecular chaperone biology in bivalves and informing future applications in biotechnology.
Abstract
Heat shock protein 70 (HSP70) chaperones are essential molecular machines that facilitate the folding, assembly, and stabilization of numerous client proteins through ATP-dependent cycles of substrate binding and release. An uncharacterized protein sequence from Corbicula fluminea was initially annotated to contain domains with potential biotechnological relevance. This study employed in silico approaches using online tools for protein characterization including BLASTp, ExPASy, I-TASSER, EzMol, DeepLoc, SMART, and MEGA 12 software to determine its structural characteristics, classification, and potential functional role. Results revealed the presence of a conserved Pfam HSP70 domain (positions 6–612) and a Pfam MreB_Mbl domain (positions 116–384), along with a low-complexity region (positions 615–646). Subcellular localization prediction indicated a cytoplasmic distribution. Multiple sequence alignment and phylogenetic reconstruction using the Maximum Likelihood method showed that the HSP70 sequence from C. fluminea is closely related to known HSP70 sequences from related species, confirming its taxonomic placement within HSP70 protein family. Collectively, these results confirmed the protein as a member of HSP70 family and provide foundational insights into its structural and functional characteristics, contributing to the understanding of molecular chaperone biology in bivalves and informing future applications in biotechnology.