The domain within your query sequence starts at position 7 and ends at position 85; the E-value for the ATE_N domain shown below is 3.3e-29.



PFAM accession number:PF04376
Interpro abstract (IPR007471):

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

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

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 [ (PUBMED:16492767) ].

GO process:protein arginylation (GO:0016598)
GO function:arginyltransferase activity (GO:0004057)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry ATE_N