Functional Information from GO Data
| Chain | GOid | namespace | contents |
| C | 0004252 | molecular_function | serine-type endopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| C | 0008236 | molecular_function | serine-type peptidase activity |
| D | 0004252 | molecular_function | serine-type endopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| D | 0008236 | molecular_function | serine-type peptidase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00136 |
| Number of Residues | 12 |
| Details | SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. AYVVDSGInvnH |
| Chain | Residue | Details |
| C | ALA158-HIS169 | |
| site_id | PS00137 |
| Number of Residues | 11 |
| Details | SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtIGG |
| Chain | Residue | Details |
| C | HIS193-GLY203 | |
| site_id | PS00138 |
| Number of Residues | 11 |
| Details | SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAtPhIVG |
| Chain | Residue | Details |
| C | GLY347-GLY357 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 168 |
| Details | Domain: {"description":"Inhibitor I9","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 546 |
| Details | Domain: {"description":"Peptidase S8","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |