v5.1.0.3
Cicer data from the Legume Information System
| Type | Homologous_superfamily |
| Description | Proteins can accumulate much damage as they age, such as the formation of isoaspartyl residues. Protein-L-isoaspartyl O-methyltransferase (PIMT) ( ) is a nearly ubiquitous enzyme that catalyses the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues, thereby playing a role in the repair or degradation of damaged proteins. The crystal structure of PIMT from the bacteria Thermotoga maritima has been determined and reveals an alpha/beta protein with three functional subdomains. The C-terminal subdomain is unique to the PIMT of T. maritime, with no similar sequences being found in PIMTs from other species [ ]. These sequences form an α/β subdomain in three layers, β/α/β, with a buried helix. |
| Short Name | PIM_MeTrfase_C |