Superdomains in the protein structure hierarchy: The case of PTP-C2

Protein Sci. 2015 May;24(5):874-82. doi: 10.1002/pro.2664. Epub 2015 Mar 31.

Abstract

Superdomain is uniquely defined in this work as a conserved combination of different globular domains in different proteins. The amino acid sequences of 25 structurally and functionally diverse proteins from fungi, plants, and animals have been analyzed in a test of the superdomain hypothesis. Each of the proteins contains a protein tyrosine phosphatase (PTP) domain followed by a C2 domain. Four novel conserved sequence motifs have been identified, one in the PTP domain and three in the C2 domain. All contribute to the PTP-C2 domain interface in PTEN, a tumor suppressor, and all are more conserved than the PTP signature motif, HCX3 (K/R)XR, in the 25 sequences. We show that PTP-C2 was formed prior to the fungi, plant, and animal kingdom divergence. A superdomain as defined here does not fit the usual protein structure classification system. The demonstrated existence of one superdomain suggests the existence of others.

Keywords: domain; evolution; hierarchy; protein; structure; superdomain.

MeSH terms

  • Amino Acid Sequence / genetics*
  • Animals
  • Casein Kinase II / chemistry
  • Casein Kinase II / genetics
  • Catalytic Domain / genetics*
  • Conserved Sequence / genetics
  • Fungi / chemistry
  • Humans
  • Models, Molecular
  • PTEN Phosphohydrolase / chemistry*
  • PTEN Phosphohydrolase / genetics
  • Plants / chemistry
  • Protein Binding
  • Protein Structure, Tertiary*
  • Protein Tyrosine Phosphatases / chemistry
  • Protein Tyrosine Phosphatases / genetics
  • Sequence Homology, Amino Acid

Substances

  • Casein Kinase II
  • Protein Tyrosine Phosphatases
  • PTEN Phosphohydrolase
  • PTEN protein, human