OCRE: a novel domain made of imperfect, aromatic-rich octamer repeats

Bioinformatics. 2005 Mar;21(6):699-702. doi: 10.1093/bioinformatics/bti065. Epub 2004 Oct 14.

Abstract

In this study, we describe a novel domain, OCRE, which is shared by the recently identified angiogenic factor VG5Q and a specific family of RNA-binding motif proteins. The OCRE domain is characterized by a 5-fold, imperfectly repeated octameric sequence, which includes a triplet of often-conserved aromatic amino acids predicted to form a beta-strand and in which the slightly modified fifth repeat might act as a repeat terminator. Although the function of this domain remains to be elucidated, the domain architecture of OCRE containing proteins and experimental data suggest a role in RNA metabolism and/or in signalling pathways activated by the tumor necrosis factor superfamily of cytokines.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Angiogenic Proteins / chemistry*
  • Angiogenic Proteins / metabolism*
  • Hydrocarbons, Aromatic / chemistry
  • Hydrocarbons, Aromatic / metabolism
  • Intracellular Signaling Peptides and Proteins / chemistry*
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Pattern Recognition, Automated / methods
  • Protein Structure, Tertiary
  • RNA / chemistry*
  • RNA / metabolism*
  • Sequence Alignment / methods
  • Sequence Analysis, Protein / methods*
  • Sequence Homology, Amino Acid
  • Structure-Activity Relationship

Substances

  • AGGF1 protein, human
  • Angiogenic Proteins
  • Hydrocarbons, Aromatic
  • Intracellular Signaling Peptides and Proteins
  • RBM14 protein, human
  • RNA