IED ID | IndEnz0002010262 |
Enzyme Type ID | protease010262 |
Protein Name |
Neutral protease 2 homolog SNOG_10522 EC 3.4.24.39 Deuterolysin SNOG_10522 |
Gene Name | BC1G_10098 |
Organism | Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Leotiomycetes Helotiales Sclerotiniaceae Botrytis Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea) Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea) |
Enzyme Sequence | MATLGVDNNVLEVTLVAGENAVVHASVKNVGAEDLNLLSYGSLFDTAPVQKINVYEGETAVPFKGVLRAIQRTDLAPEVFHTLAAGETFETSFNAAEVHDLSTSTYTFVAEGAIPFAKAGSTEISDSIIFKSNAITVSVDGEAAKSVAKAIPSSIDRRTVLQSGCSTSQRSATTQALSYCASLARAASTAASSGSSTKFSEYFKTTSSSTRSVVAARLSAVASQCSSLTSGSTKYYCTDVYGYCESNVLAYTIPSTNEIVNCPIYYSALPALTGTCHAQDRATTTLHEFTHAPATYSPGTADNGYGYAAATALTSARAVLNADSYALYANAIYVGC |
Enzyme Length | 336 |
Uniprot Accession Number | A6SBW7 |
Absorption | |
Active Site | ACT_SITE 288; /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); Signal peptide (1) |
Keywords | Cleavage on pair of basic residues;Disulfide bond;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Zinc;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 35,038 |
Kinetics | |
Metal Binding | METAL 287; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 291; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 302; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
Rhea ID | |
Cross Reference Brenda |