| IED ID | IndEnz0002007937 |
| Enzyme Type ID | protease007937 |
| Protein Name |
Neutral protease 2 homolog SNOG_10522 EC 3.4.24.39 Deuterolysin SNOG_10522 |
| Gene Name | SNOG_10522 |
| 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 | MKVSSQLAVAALASFATAASVDVHKRETPLSVKLAASGNSEVKVTLTNNGEKTLNLLSKGTFLDEQLPVEKVQMYAAGGSDKVAFEGMKVRLLTSGLKADDFVTLAAGETKEITVETAALHSLHEGGDFDVFAKGALPFAEGASTELAGALDYESNKLSMTIDGAQAASVAKALNKRTAIGSSCTGTKLSTVRTALSNCARLANAAASAATSGTKLTTYFKTTSSASTVAARLRAVASDCGSTSSRTTTNCNDPYSGCSSNVLAYTVPSANFITYCPIFFSALPALASTCHGQDQATTALHEETHAPGVYSPGTQDNGYGYAAATALSANQALNNADSYALYANAINLNC |
| Enzyme Length | 350 |
| Uniprot Accession Number | Q0UCJ2 |
| Absorption | |
| Active Site | ACT_SITE 302; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage of bonds with hydrophobic residues in P1'. Also 3-Asn-|-Gln-4 and 8-Gly-|-Ser-9 bonds in insulin B chain.; EC=3.4.24.39; |
| DNA Binding | |
| EC Number | 3.4.24.39 |
| Enzyme Function | FUNCTION: Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Shows high activities on basic nuclear substrates such as histone and protamine (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (2); Metal binding (3); Propeptide (1); Signal peptide (1) |
| Keywords | Cleavage on pair of basic residues;Disulfide bond;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 35,981 |
| Kinetics | |
| Metal Binding | METAL 301; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 305; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 316; /note=Zinc; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.39; |