Detail Information for IndEnz0002006553
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