| IED ID | IndEnz0002008947 | 
| Enzyme Type ID | protease008947 | 
| Protein Name | 
                        
                            
                                Cuticle-degrading serine protease  EC 3.4.21.- Neutral serine protease Aoz1 Aoz PII  | 
                    
| Gene Name | |
| Organism | Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491) (Nematode-trapping fungus) (Didymozoophaga oligospora) | 
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina Orbiliomycetes Orbiliales Orbiliaceae Orbilia Orbilia oligospora (Nematode-trapping fungus) (Arthrobotrys oligospora) Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491) (Nematode-trapping fungus) (Didymozoophaga oligospora) | 
| Enzyme Sequence | MLTNGLISLLAIAGLATNAFAGPIRKVSNAGAAGAIADKYIVVLKKGLSDSAVSKHTNRISSFHSNVARDLTGARAHGVGRKFRFSSTGFNGYVGGFDKATLQEILNSPEVDYVEQDTVVTTYAEQTDSTWGLDRISHEDYSAPYTYEYDETAAGAGTTVYVIDTGIRISHDEFQTVNGSSRATWGFNSVDKTDSDGNGHGTHCAGTIAGKTYGVSKKAKVVAVKVLSAGGSGSTAGVVSGMNWVAENATPNFSVASMSLGGSKSAALNTAVDAIFNAGITIVVAAGNENQDAKNVSPASAPNAITVGAIDSSNKIASFSNWGTLIDVFAPGVGVLSSWATSDKETKTISGTSMACPHVAGLAAYYISASEGGADPATITDKITSSAVSGQVTGNIRGSPNKIAYNGYA | 
| Enzyme Length | 409 | 
| Uniprot Accession Number | G1X8P8 | 
| Absorption | |
| Active Site | ACT_SITE 164; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 200; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 353; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 | 
| Activity Regulation | ACTIVITY REGULATION: Inhibited by PMSF, SSI, the peptide Phe-Val and by Phe, but not by EDTA. {ECO:0000269|PubMed:8757725}. | 
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- | 
| Enzyme Function | FUNCTION: Hydrolyzes gelatin, casein, the chromogenic substrate azocoll and the cuticle of the nematode P.redivivus. Immobilizes P.redivivus. | 
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (2); Glycosylation (2); Propeptide (1); Sequence conflict (1); Signal peptide (1) | 
| Keywords | Collagen degradation;Direct protein sequencing;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen | 
| Interact With | |
| Induction | INDUCTION: By easily metabolized forms of nitrogen, including ammonia, nitrate and amino acids, and by glucose. {ECO:0000269|PubMed:8757725}. | 
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | 
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 | 
| Structure 3D | |
| Cross Reference PDB | - | 
| Mapped Pubmed ID | - | 
| Motif | |
| Gene Encoded By | |
| Mass | 41,914 | 
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |