v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | This entry represents the N-terminal substrate-binding domain of the Lon protease. This ATP-dependent enzyme, a serine peptidase belonging to the MEROPS peptidase family S16, is conserved in archaeal, bacterial and eukaryotic organisms and catalyses rapid turnover of short-lived regulatory proteins and many damaged or denatured proteins. In eukaryotes, the majority of the proteins are located in the mitochondrial matrix [ , ]. In yeast, Pim1, is located in the mitochondrial matrix and required for mitochondrial function. It is constitutively expressed but is increased after thermal stress, suggesting that Pim1 may play a role in the heat shock response [].The structure of this domain has been determined and it represents a general protein and polypeptide interaction domain [ , , , ]. |
| Short Name | Lon_prtase_N |