Fig. 1: Analysis of a family of proline-rich cathelicidin orthologs identified in ruminants.
From: Rumicidins are a family of mammalian host-defense peptides plugging the 70S ribosome exit tunnel
Amino acid sequences of rumicidins after in silico processing of corresponding precursor proteins by elastase are presented in the colored boxes. The description box is presented at the top. Most of the rumicidins bear the C-terminal GKR tripeptide, which is a signal for an additional stage of post-translational modification by peptidylglycine alpha-amidating monooxygenase. This enzyme cleaves the C-terminal GKR (marked with a red arrow) and then amidates of the carboxyl group of the preceding amino acid residue. Such modifications occur in other proline-rich cathelicidins (for example, in the bovine Bac5 and porcine PR-3910) and may play an important role in providing resistance to carboxypeptidases.
