InterPro domain: IPR017137

Arginine-tRNA-protein transferase catalyses the post-translational conjugation of arginine to the N terminus of a protein. In eukaryotes, this functions as part of the N-end rule pathway of protein degradation by conjugating a destabilising amino acid to the N-terminal aspartate or glutamate of a protein, targeting the protein for ubiquitin-dependent proteolysis [ 1 ]. In Saccharomyces cerevisiae, Cys20, 23, 94 and/or 95 are thought to be important for activity [ 2 ]. Of these, only Cys 94 appears to be completely conserved in this family.

This entry represents eukaryotic type arginyl-tRNA--protein transferase 1 ( 2.3.2.8 ) [ 3 ].

1. Alternative splicing results in differential expression, activity, and localization of the two forms of arginyl-tRNA-protein transferase, a component of the N-end rule pathway. Mol. Cell. Biol. 19, 182-93
2. Binding of phenylarsenoxide to Arg-tRNA protein transferase is independent of vicinal thiols. Biochemistry 34, 15829-37
3. Identification of mammalian arginyltransferases that modify a specific subset of protein substrates. Proc. Natl. Acad. Sci. U.S.A. 102, 10123-8