Scooby Domain Prediction

Scooby Domain Prediction predicts globular domains within protein sequences by leveraging observed lengths and hydrophobicities of known protein structures to identify candidate regions for structural characterization.


Key Features:

  • Hydrophobicity- and length-based prediction: Uses sequence hydrophobicity profiles together with observed lengths from known protein structures to distinguish regions likely to form globular domains from unstructured regions.
  • No homology requirement: Assigns domains without relying on homology searches against sequence databases.
  • Local property calculations: Computes average hydrophobicity, secondary structure propensity, and domain boundary predictions from sequence data.
  • High-throughput performance: Optimized for rapid domain assignment across large sets of sequences.

Scientific Applications:

  • Domain identification: Detects candidate globular domains within uncharacterized protein sequences for downstream analysis.
  • Structural target selection: Identifies regions suitable for experimental three-dimensional structure determination.
  • Protein engineering: Informs studies of domain architecture and stability for engineering and design efforts.
  • Novel protein characterization: Facilitates analysis of proteins lacking detectable homologs by sequence-based structural prediction.

Methodology:

Analyzes protein sequences using hydrophobicity profiles and observed lengths from known protein structures to predict globular regions and assign domain boundaries, comparing predictions with known structural data and without using homology searches.

Topics

Details

Tool Type:
web application
Operating Systems:
Linux, Windows, Mac
Programming Languages:
Java
Added:
2/10/2017
Last Updated:
11/25/2024

Operations

Publications

George RA, Lin K, Heringa J. Scooby-domain: prediction of globular domains in protein sequence. Nucleic Acids Research. 2005;33(Web Server):W160-W163. doi:10.1093/nar/gki381. PMID:15980446. PMCID:PMC1160142.

Documentation