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InterPro: IPR007472 Arginine-tRNA-protein transferase, C-terminal

Protein matchesHelp
UniProtKB
Matches:
601 proteins
AccessionHelp IPR007472 Arg-tRNA-P_Trfase_C
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR017137 Arginine-tRNA-protein transferase 1, eukaryotic
IPR017138 Arginine-tRNA-protein transferase, predicted, prokaryotic
GO Term annotationHelp
Process GO:0016598 protein arginylation
Function GO:0004057 arginyltransferase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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 terminus 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. N-terminal cysteine is sometimes modified [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 the C-terminal region of the enzyme arginine-tRNA-protein transferase, found in both eukaryotic and prokaryotic enzymes.

Database linksHelp
Enzyme: EC:2.3.2.8
PANDIT: PF04377
Blocks: IPB007472

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR007472 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O95260 Arginyl-tRNA--protein transferase 1

O96539 Arginyl-tRNA--protein transferase 1

P16639 Arginyl-tRNA--protein transferase 1

Q9Z2A5 Arginyl-tRNA--protein transferase 1

Q9ZT48 Arginyl-tRNA--protein transferase 1

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR017137 Arginine-tRNA-protein transferase 1, eukaryotic
IPR007471 Arginine-tRNA-protein transferase, N-terminal
IPR007472 Arginine-tRNA-protein transferase, C-terminal
ModBase

PublicationsHelp
1. Kwon YT, Kashina AS, Varshavsky A.
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 1999 [PubMed: 9858543]
http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=9858543
2. Li J, Pickart CM.
Binding of phenylarsenoxide to Arg-tRNA protein transferase is independent of vicinal thiols.
Biochemistry 34 15829-37 1995 [PubMed: 7495814]
http://dx.doi.org/10.1021/bi00048a028

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InterPro 23.1