| IED ID | IndEnz0002000627 |
| Enzyme Type ID | protease000627 |
| Protein Name |
Aspartic protease SNP2 EC 3.4.23.- Protease 2 |
| Gene Name | SNP2 SNOG_02018 |
| Organism | Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Parastagonospora nodorum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta dothideomyceta Dothideomycetes Pleosporomycetidae Pleosporales Pleosporineae Phaeosphaeriaceae Parastagonospora Phaeosphaeria nodorum (Glume blotch fungus) (Parastagonospora nodorum) Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Parastagonospora nodorum) |
| Enzyme Sequence | MPSFTYLTAALALTSSVVASPVEKRDAFEVKQVAHGLHRKNGPAQIAKTLRKYGKAVPAHIQAAADNNAVVQADANTGSDPAVPSDQYDSSYLSPVTVGTSTVHLDFDTGSADLWVFSDLQAKSSLSGHDYYKTDASKRKSGYTWKISYGDGSGASGQVYTDKVTVGQVTATAQAVEAATSVSAQFSQDVDTDGLLGLAMSSINTVKPQQQTTWFDTVKSQLAKPLFAVTLKYHAAGTYDFGYIDSAKYTGAITYVNADASQGFWGFTASGYSVGTGATVSSSISGILDTGTTLMYVPAATAKAYYAKVSGAKLDSTQGGYVFPCSATLPNFSITVAGVKQTVPGKYINYAPITDGSSTCFGGMQPDTDIGQSIFGDIFLKSKYIVHDMSNGTPRLGFAQQAGVSS |
| Enzyme Length | 406 |
| Uniprot Accession Number | Q69IF8 |
| Absorption | |
| Active Site | ACT_SITE 108; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103; ACT_SITE 289; /evidence=ECO:0000255|PROSITE-ProRule:PRU01103 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.23.- |
| Enzyme Function | FUNCTION: Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. The scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in the active site. Shows a broad primary substrate specificity. Favors hydrophobic residues at the P1 and P1' positions. {ECO:0000250|UniProtKB:Q12567}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (1); Propeptide (1); Signal peptide (1) |
| Keywords | Aspartyl protease;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q12567}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 42,567 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |