| IED ID | IndEnz0002010003 |
| Enzyme Type ID | protease010003 |
| Protein Name |
Proteinase K EC 3.4.21.64 Endopeptidase K Tritirachium alkaline proteinase |
| Gene Name | PROK |
| Organism | Parengyodontium album (Tritirachium album) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Hypocreales Cordycipitaceae Parengyodontium Parengyodontium album (Tritirachium album) |
| Enzyme Sequence | MRLSVLLSLLPLALGAPAVEQRSEAAPLIEARGEMVANKYIVKFKEGSALSALDAAMEKISGKPDHVYKNVFSGFAATLDENMVRVLRAHPDVEYIEQDAVVTINAAQTNAPWGLARISSTSPGTSTYYYDESAGQGSCVYVIDTGIEASHPEFEGRAQMVKTYYYSSRDGNGHGTHCAGTVGSRTYGVAKKTQLFGVKVLDDNGSGQYSTIIAGMDFVASDKNNRNCPKGVVASLSLGGGYSSSVNSAAARLQSSGVMVAVAAGNNNADARNYSPASEPSVCTVGASDRYDRRSSFSNYGSVLDIFGPGTSILSTWIGGSTRSISGTSMATPHVAGLAAYLMTLGKTTAASACRYIADTANKGDLSNIPFGTVNLLAYNNYQA |
| Enzyme Length | 384 |
| Uniprot Accession Number | P06873 |
| Absorption | |
| Active Site | ACT_SITE 144; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 174; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 329; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of keratin, and of other proteins with subtilisin-like specificity. Hydrolyzes peptide amides.; EC=3.4.21.64; |
| DNA Binding | |
| EC Number | 3.4.21.64 |
| Enzyme Function | FUNCTION: Hydrolyzes keratin at aromatic and hydrophobic residues. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (19); Chain (1); Disulfide bond (2); Domain (2); Helix (9); Metal binding (5); Propeptide (1); Sequence conflict (8); Signal peptide (1); Turn (6) |
| Keywords | 3D-structure;Calcium;Direct protein sequencing;Disulfide bond;Hydrolase;Metal-binding;Protease;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..15 |
| Structure 3D | Electron microscopy (29); X-ray crystallography (168) |
| Cross Reference PDB | 1BJR; 1CNM; 1EGQ; 1HT3; 1IC6; 1OYO; 1P7V; 1P7W; 1PEK; 1PFG; 1PJ8; 1PTK; 2DP4; 2DQK; 2DUJ; 2G4V; 2HD4; 2HPZ; 2ID8; 2PKC; 2PQ2; 2PRK; 2PWA; 2PWB; 2PYZ; 2V8B; 3AJ8; 3AJ9; 3D9Q; 3DDZ; 3DE0; 3DE1; 3DE2; 3DE3; 3DE4; 3DE5; 3DE6; 3DE7; 3DVQ; 3DVR; 3DVS; 3DW1; 3DW3; 3DWE; 3DYB; 3GT3; 3GT4; 3I2Y; 3I30; 3I34; 3I37; 3L1K; 3OSZ; 3PRK; 3PTL; 3Q40; 3Q5G; 3QMP; 4B5L; 4DJ5; 4FON; 4WOB; 4WOC; 4ZAR; 5AMX; 5AVJ; 5AVK; 5B1D; 5B1E; 5CW1; 5I9S; 5K7S; 5KXU; 5KXV; 5MJL; 5ROC; 5ROD; 5ROE; 5ROF; 5ROG; 5ROH; 5ROI; 5ROJ; 5ROK; 5ROL; 5ROM; 5RON; 5ROO; 5ROP; 5ROQ; 5ROR; 5ROS; 5ROT; 5ROU; 5ROV; 5ROW; 5ROX; 5ROY; 5ROZ; 5RP0; 5RP1; 5RP2; 5RP3; 5RP4; 5RP5; 5RP6; 5RP7; 5RP8; 5RP9; 5RPA; 5RPB; 5RPC; 5RPD; 5RPE; 5RPF; 5RPG; 5RPH; 5RPI; 5RPJ; 5RPK; 5RPL; 5RPM; 5RPN; 5RPO; 5RPP; 5RPQ; 5RPR; 5RPS; 5RPT; 5RPU; 5RPV; 5RPW; 5RPX; 5RPY; 5RPZ; 5UVL; 5WHW; 5WJG; 5WJH; 5WRC; 6CL7; 6CL8; 6CL9; 6CLA; 6CLB; 6FJS; 6J43; 6K2P; 6K2R; 6K2S; 6K2T; 6K2V; 6K2W; 6K2X; 6K8M; 6KKF; 6LAW; 6MH6; 6N4U; 6PKJ; 6PKK; 6PKL; 6PKM; 6PKN; 6PKO; 6PKP; 6PKQ; 6PKR; 6PKS; 6PKT; 6PQ0; 6PQ4; 6PU4; 6PU5; 6QF1; 6QXV; 6RUG; 6RUH; 6RUK; 6RUN; 6RUW; 6RVE; 6RVG; 6RZP; 6TXG; 6V8R; 6ZET; 6ZEU; 6ZEV; 7A68; 7A9F; 7A9K; 7A9M; 7C0P; 7JSY; 7NJJ; 7S4Z; |
| Mapped Pubmed ID | 10737944; 11258922; 11438752; 11886076; 17139083; 17327674; 1894649; 19020357; 19255463; 19686853; 20124702; 20382990; 22102227; 22505256; 22706161; 25641793; 27050125; 27275145; 28192420; 28361898; 28386083; 28875031; 29097720; 29706530; 30224955; 30289409; 30661853; 30794865; 31098022; 31316815; 31422911; 31490500; 31576224; 31576225; 32266561; 32280322; 3271105; 32735770; 32850967; 32966481; 33007196; 34076593; 34076595; 8253733; 8340410; 8811735; 8976553; |
| Motif | |
| Gene Encoded By | |
| Mass | 40,300 |
| Kinetics | |
| Metal Binding | METAL 121; /note=Calcium 2; via carbonyl oxygen; METAL 280; /note=Calcium 1; via carbonyl oxygen; METAL 282; /note=Calcium 1; via carbonyl oxygen; METAL 305; /note=Calcium 1; METAL 365; /note=Calcium 2 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.64; |