{PDOC00985} {PS01279; PCMT} {BEGIN} ********************************************************************* * Protein-L-isoaspartate(D-aspartate) O-methyltransferase signature * ********************************************************************* Protein-L-isoaspartate(D-aspartate) O-methyltransferase (EC 2.1.1.77) (PCMT) [1] (which is also known as L-isoaspartyl protein carboxyl methyltransferase) is an enzyme that catalyzes the transfer of a methyl group from S- adenosylmethionine to the free carboxyl groups of D-aspartyl or L-isoaspartyl residues in a variety of peptides and proteins. The enzyme does not act on normal L-aspartyl residues L-isoaspartyl and D-aspartyl are the products of the spontaneous deamidation and/or isomerization of normal L-aspartyl and L- asparaginyl residues in proteins. PCMT plays a role in the repair and/or degradation of these damaged proteins; the enzymatic methyl esterification of the abnormal residues can lead to their conversion to normal L-aspartyl residues. PCMT is a well-conserved and widely distributed cytosolic protein of about 24 Kd. As a signature pattern, we selected a conserved region in the central part of this enzyme. -Consensus pattern: [GSAED]-[DN]-G-x(2)-G-[FYWLV]-x(3)-[GSA]-[PTL]-[FY]- [DNSHE]-x-I -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: December 2004 / Pattern and text revised. [ 1] Kagan R.M., McFadden H.J., McFadden P.N., O'Connor C., Clarke S. "Molecular phylogenetics of a protein repair methyltransferase." Comp. Biochem. Physiol. 117b:379-385(1997). -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}