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.
D000595:Amino Acid Sequence; D001120:Arginine / Q000378:metabolism*; D002352:Carrier Proteins / Q000502:physiology; D004271:DNA, Fungal / Q000235:genetics; D004268:DNA-Binding Proteins / Q000502:physiology*; D005786:Gene Expression Regulation; D005800:Genes, Fungal; D008969:Molecular Sequence Data; D016601:RNA-Binding Proteins; D012260:Ribonucleases / Q000502:physiology*; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid; D014157:Transcription Factors / Q000502:physiology*; D014158:Transcription, Genetic
D002352:Carrier Proteins; D004271:DNA, Fungal; D004268:DNA-Binding Proteins; D016601:RNA-Binding Proteins; D014157:Transcription Factors; D001120:Arginine; D012260:Ribonucleases