Domain

N-end aminoacyl transferase, N-terminal (IPR007471)

Short name: N-end_Aminoacyl_Trfase_N

Overlapping homologous superfamilies

None.

Domain relationships

None.

Description

This entry represents the N-terminal region of aminoacyl-transferases found in both eukaryotic (Arginine-tRNA-protein transferase) and prokaryotic (Aspartate/glutamate leucyltransferase) enzymes.

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 [PMID: 9858543]. In Saccharomyces cerevisiae, Cys20, 23, 94 and/or 95 are thought to be important for activity [PMID: 7495814]. Of these, only Cys 94 appears to be completely conserved in this family.

Aspartate/glutamate leucyltransferase (also known as bacterial protein transferase or Bpt) functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate. This protein shows sequence similarity to the eukaryotic N-end rule pathway component arginyl-transferase Ate1 [PMID: 16492767].

GO terms

Biological Process

GO:0016598 protein arginylation

Molecular Function

GO:0004057 arginyltransferase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
Pfam