v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | The N-terminal region of the the PH1510 protein (1510-N or PH1510-N) from archaebacterium Pyrococcus horikoshii has been shown to possess serine protease activity and has a Ser-Lys catalytic dyad, preferentially cleaving hydrophobic substrates. It is structurally related to ClpP. In the genome of Pyrococcus horikoshii, PH1510 is homologous to the genes nfed (nodulation formation efficiency D) [ ].PH1510 (MEROPS identifier S49.005) is thought to be a signal peptide peptidase, which degrades the membrane-bound signal peptide after it has been released from secreted proteins [ ]. The peptidase domain is followed by a C-terminal NfeD domain []. |
| Short Name | PH1510-N |