IDDomainSpotter

IDDomainSpotter identifies domain organization within long intrinsically disordered protein regions by detecting sequence-based compositional biases such as hydrophilicity, enrichment of disorder-promoting residues (Proline, Serine, Threonine), and depletion of positively charged residues (Arginine, Lysine).

Key Features:

• Sequence-Based Analysis: Assesses domain organization in proteins with intrinsically disordered regions exceeding 50 residues.
• Compositional Bias Utilization: Identifies putative domains by analyzing compositional biases, focusing on hydrophilicity and enrichment of Proline, Serine, Threonine and depletion of Arginine and Lysine.
• Visualization Capabilities: Visualizes domain organization to elucidate structural properties and molecular functions retained within disordered regions.

Scientific Applications:

• Transcription Factor Analysis: Applied to identify domains in transcription factors such as p53, GCR, NAC46, MYB28, and MYB29 that link DNA-binding domains to other disordered regions and are enriched in hydrophilic and disorder-promoting residues.
• Biophysical Characterization: Revealed identified domains to be extended, dynamic, and highly disordered, implicating roles in protein interactions and regulatory mechanisms.
• Conservation Across Species: Demonstrated conservation of such domains across various transcription factors from different families and life domains, indicating evolutionary importance.

Methodology:

IDDomainSpotter employs a sequence-based approach to detect compositional biases indicative of domain organization within intrinsically disordered regions, focusing on amino-acid trait distributions (hydrophilicity, Proline/Serine/Threonine enrichment, Arg/Lys depletion).