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  • 1Department of Biotechnology, Koneru Lakshmaiah Education Foundation, Vaddeswaram, AP, India.

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Summary

This study analyzes ATP-dependent RNA helicase q96c10.1, revealing conserved residues and active site characteristics. Findings aid in its functional annotation as a potential helicase.

Keywords:
MODELLERRNA helicaseflexibilityinnate immunitymotif

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Bioinformatics

Background:

  • ATP-dependent RNA helicases are crucial enzymes with diverse biological roles.
  • Understanding the active site residues of human protein q96c10.1 is essential for inferring its function.
  • Existing annotations require detailed structural and functional insights.

Purpose of the Study:

  • To structurally and functionally characterize the human ATP-dependent RNA helicase q96c10.1.
  • To identify key active-site residues and their conservation patterns.
  • To infer the enzyme's role and evolutionary relationships.

Main Methods:

  • Bioinformatic tools (InterPro, GO, CDD, ProTaram, Modeller, ConSurf, CASTp, Cabs-flex) were used for protein annotation and analysis.
  • Sequence homology and structural conservation analyses were performed.
  • Protein-protein interaction analysis identified DDX58 as a top partner.

Main Results:

  • 124 out of 259 homologs showed high residue conservation, clustered into 7 clades.
  • The active site exhibited low sequence conservation, with only 9 out of 42 residues conserved.
  • Limited structural fluctuation was observed in conserved active-site residues compared to the wild type.

Conclusions:

  • The study provides functional, sequence similarity, and phylogenetic information for annotating q96c10.1 as a potential helicase.
  • Conserved sequence segments and topological flexibility differ from other subfamily members.
  • The findings contribute to a deeper understanding of RNA helicase mechanisms.