InterPro domain: IPR034164

This entry represents a domain found in a group of pepsin-like aspartic proteases. They are found in mammals, plants, fungi and bacteria and are classified by MEROPS as members of the peptidase family A1 (pepsin A, clan AA) [ 1 ]. Proteins containing this domain also include the fungal enzymes mucorpepsin (A01.013) [ 2 ], polyporopepsin (A01.019) [ 3 ], CtsD peptidase from Aspergillus (A01.077) [ 4 ] and CnAP1 peptidase from Cryptococcus neoformans (A01.078) [ 5 ]; plasmepsins from the malaria parasite Plasmodium (A01.021, A01.022, A01.023, A01.043, A01.059) [ 6 ] and necepsin-1 from the hookworm Necator (A01.053) [ 7 ], which degrade host hemoglobin; and shewasin A from the bacterium Shewanella (A01.095) [ 8 ].

1. Families of aspartic peptidases, and those of unknown catalytic mechanism. Meth. Enzymol. 248, 105-20
2. Structure-Based Design of Mucor pusillus Pepsin for the Improved Ratio of Clotting Activity/Proteolytic Activity in Cheese Manufacture. Protein Pept. Lett. 22, 660-7
3. Crystal structure of aspartic proteinase from Irpex lacteus in complex with inhibitor pepstatin. J. Mol. Biol. 341, 1227-35
4. Isolation, activity and immunological characterisation of a secreted aspartic protease, CtsD, from Aspergillus fumigatus. Protein Expr. Purif. 53, 216-24
5. Identification and characterization of an aspartyl protease from Cryptococcus neoformans. FEBS Lett. 581, 3882-6
6. Structural studies of vacuolar plasmepsins. Biochim. Biophys. Acta 1824, 207-23
7. Hookworm aspartic protease, Na-APR-2, cleaves human hemoglobin and serum proteins in a host-specific fashion. J. Infect. Dis. 187, 484-94
8. Shewasin A, an active pepsin homolog from the bacterium Shewanella amazonensis. FEBS J. 278, 3177-86