| IED ID | IndEnz0002001129 |
| Enzyme Type ID | protease001129 |
| Protein Name |
Neutral protease 2 homolog NFIA_031120 EC 3.4.24.39 Deuterolysin NFIA_031120 |
| Gene Name | NFIA_031120 |
| Organism | Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Aspergillus fischeri Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
| Enzyme Sequence | MKITALASAILAVVHGALALPARAPALDITLSQVNNTRIKAVVKNSGSEKITFVHLNFFNDPSPVKKVSLYRNATEVEFTGIKQRLRSDGLSNEALTTLAPGATYEDEFDIASTANLTQGGPVTVRTQGFVPIAMNNKIAGYIPYSSNELELEVDAVKAVAVPASIKPLDRRTKITSSCTGDRAAVLNTALRNAASIAGKAANAASSGSSALFAEYFKSTSGNIRSAVAARLKAVASEASLNGGGSTTYYCSDPYGYCDSNVLAYTLPSTNEVVNCELFYTLQEVTNDCHGQDQATTIIHEFTHAPGVYPPGTEDLGYGYSAATALSANNALNNADSYALFANAVYLNCQGQTGGQTMWDGNSQPGQTAPGTQTMWDGNSQPGQTEPGTQTMWDGNSQPGQTEPGTQTMWDGNSQPGQTEPGTQTMWDGNSQPGQTEPCTQTMWDGSSEPGQTEPDAHTTWGNFYQA |
| Enzyme Length | 467 |
| Uniprot Accession Number | A1DA48 |
| Absorption | |
| Active Site | ACT_SITE 301; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| 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); Region (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..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 49,367 |
| Kinetics | |
| Metal Binding | METAL 300; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 304; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 315; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |