IED ID | IndEnz0002006553 |
Enzyme Type ID | protease006553 |
Protein Name |
Pheromone-processing carboxypeptidase KEX1 EC 3.4.16.6 Carboxypeptidase D |
Gene Name | KEX1 CAGL0G01232g |
Organism | Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Nakaseomyces Nakaseomyces/Candida clade Candida glabrata (Yeast) (Torulopsis glabrata) Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) |
Enzyme Sequence | MLHATVLPILLWLATLAYGFDRKEFLVDGNELPGFTKLKNTKHWTVPKMYAGHLPATRDNDTQYFFWKFENKKTKKNDETPLIIWLNGGPGCSSMAGALMEIGPFRLNKKAEVIKNDGSWHMRGSVLFLDQPVGTGFSYSKEDNEVSELDEVADNFMVFLQNYYATFPDDKDRELILAGESYAGQFIPYFTKAIIKFNEQQRDENSKINIKVMFIGNGWLDPKRQYLSYVPFSLEKGIIKKEDPAFKDILKQHETCQNYINSDHTGHSELSYPPCEAVLGKIISQDKTQCINVYKFDEYDSYPSCGLEWPVDTKFTKQFLTDKKVLAALHANDERSWIECRPDVKLENIKAKPAIELIPSLLESGIELILFNGNKDLICNTLGIDNVLKHLQWEGETGFTDEVQIFDWVYRDDLKSDKEKVAGTVKYERQLTLITIEDGSHMVSYDKALISRGILDMYYDDVLLVHRDGKDTLISSKDGDIDGYLEDDKSQDENKDNESEDESEDENDSDDESDGKEGDKQENKPDDSDDESDEEDDDEDEDDEDDDDDDDDDDGDDEDKKGDQNSHPSHGDMNGGLDNDLETGGEYYQDEDEEGSNFKAFFLILSLVSAFIIVAAFYISDYIKSRRHPILVDGDGRSRLNKSVTWASDIENGSFDIEDDDPEFGTEGMEDNMELEDVFSIDEEDEEQLEGVVPESTRKSKKGSKKKGKYFSVPNDDSAEDIELQDIERH |
Enzyme Length | 730 |
Uniprot Accession Number | Q6FTM9 |
Absorption | |
Active Site | ACT_SITE 181; /evidence=ECO:0000255|PROSITE-ProRule:PRU10074; ACT_SITE 376; /evidence=ECO:0000255|PROSITE-ProRule:PRU10074; ACT_SITE 441; /evidence=ECO:0000255|PROSITE-ProRule:PRU10074 |
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 (3); 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 | 83,259 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |