The yeast ARGRII regulatory protein has homology with various RNases and DNA binding proteins.

Three regulatory proteins are involved in the post-transcriptional control of arginine metabolism in Saccharomyces cerevisiae: ARGRI, ARGRII and ARGRIII. The 880 amino acid ARGRII protein, like some DNA binding proteins, possesses in its N-terminal sequence a cysteine-rich region that presents homology to the zinc binding region of Escherichia coli aspartate transcarbamylase. ARGRII also has a region of 90 amino acids that is 30% homologous to the E. coli ARGR repressor. Moreover a 87 amino acid long sequence of ARGRII contains three stretches with significant homology to some viral, bacterial and pancreatic RNases. We propose a model in which the RNase-like sequence could regulate the expression of arginine anabolic messenger RNAs.