MoonProt 3.0

MoonProt 3.0 catalogs and annotates moonlighting proteins—single polypeptide chains that perform two or more distinct biochemical or biophysical functions—encompassing over 500 expert-curated entries with associated structural and functional information.

Key Features:

• Comprehensive Annotations: Expert-curated entries include functional descriptions, structural data, and organismal context for each moonlighting protein.
• Structural Data: Integrates structural information from the Protein Data Bank (PDB) and classifications from CATH and SCOP.
• Predicted Features: Provides computational predictions of disorder regions and transmembrane helices for annotated proteins.
• Diverse Biological Representation: Contains examples across multiple taxa, including humans, plants, and archaea, reflecting evolutionary diversity.
• Functional Insights: Details distinct biochemical or biophysical functions performed by single polypeptides and their physiological relevance.
• Disease Associations: Documents connections between moonlighting proteins and diseases, including reported relationships to disease mechanisms.
• Organismal Context: Specifies the types of organisms in which multiple functions have been observed and relates these observations to organismal biology.

Scientific Applications:

• Protein Function and Evolution Studies: Enables comparative analyses of multifunctional proteins to study evolution of protein function.
• Mechanistic Investigations: Supports research into molecular mechanisms underlying distinct moonlighting activities of single polypeptides.
• Disease Research: Facilitates investigation of how moonlighting proteins contribute to disease mechanisms and organismal health.
• Therapeutic Target and Biomarker Discovery: Provides annotations and structural context useful for identifying potential therapeutic targets and biomarkers.

Methodology:

Integrates structural data from the Protein Data Bank (PDB), CATH and SCOP classifications, and computational predictions of disorder regions and transmembrane helices.