| IED ID | IndEnz0002002980 |
| Enzyme Type ID | protease002980 |
| Protein Name |
Pheromone-processing carboxypeptidase KEX1 EC 3.4.16.6 Carboxypeptidase D |
| Gene Name | KEX1 LELG_05440 |
| Organism | Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Candida/Lodderomyces clade Lodderomyces Lodderomyces elongisporus Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus) |
| Enzyme Sequence | MLISSIYTICLFIITSVLAIPPKEGSDSDPAKQYLVTDLPGLHENIDDDFKPIMYAGQVELFPENNTMYFFWKFTDPKKSTDSAYSKRSIFWLNGGPGCSSMDGALLETGPFRINQDEKVVMNNGSWHKAGDVVYVDQPAGTGFSYTDQGKWLHDLPDMAFYFLKFMEKYYEIYPEEIDNDIYFAGESYAGQYIPYIADAILKRNAKLEEGQKKYNLKSLLIGNGWVSPNEQSLSYLPFFIENKLIDKENPRWMELLGDHEKCQRIVDGIDSKFDDKELNPAELDSNLCEGILTKLLSATVNGDGADDDQRCINMYDFTLRDSWPGCGINWPFELKYVTPFLRNDEVKHDLNLRVMKTWRECSGRVGRNFNAQHSFPSVHLLPDLLKQVPIILFSGMNDIICNSKGTLQYVLKLNWNGRKGFENPDAKLDWIHDDKKVGYVIQERNLTFIDIYNSSHMVPYDLPEVSRALLEIATNNYDIRDVDETNQNLVTYPLGVQKKGKIEVNPPSTPSSNDDSTTSETSDSQPDTVSSAGTSAEAETETEAEPTVNKVARLIQLAVILIVIWGLYLLYASWRARPSPIMKKNGGNGRKKNVQWADQLSRFEEEADASQLKGFFAKTMDRFRTTEGQGSYARAQSDDYIDDIELGEGIGETQLDDFIIGSDDEREGELEQPTHKSGNMDTDTNKNMKNSSNESKNKNTV |
| Enzyme Length | 702 |
| Uniprot Accession Number | A5E751 |
| Absorption | |
| Active Site | ACT_SITE 188; /evidence=ECO:0000255|PROSITE-ProRule:PRU10075; ACT_SITE 399; /evidence=ECO:0000255|PROSITE-ProRule:PRU10075; ACT_SITE 457; /evidence=ECO:0000255|PROSITE-ProRule:PRU10075 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential release of a C-terminal arginine or lysine residue.; EC=3.4.16.6; |
| DNA Binding | |
| EC Number | 3.4.16.6 |
| Enzyme Function | FUNCTION: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (3); Glycosylation (4); Region (2); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | Apoptosis;Carboxypeptidase;Glycoprotein;Golgi apparatus;Hydrolase;Membrane;Protease;Reference proteome;Signal;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Single-pass type I membrane protein {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 | 79,550 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |