Detail Information for IndEnz0002005997
IED ID IndEnz0002005997
Enzyme Type ID protease005997
Protein Name Carboxypeptidase Y homolog A
EC 3.4.16.5
Gene Name CPYA CarbY
Organism Trichophyton equinum (Horse ringworm fungus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Trichophyton Trichophyton equinum (Horse ringworm fungus)
Enzyme Sequence MKFLTTGLLATAALAAAQEQQVLQAEDGMGQAPQRGSSIFDETLQKFQSSLEDGISHFWSEMKTNFKDYLPLISLPKKHTRRPDSEWDHVVRGADIESVWVQGADGEKRREIDGKLHNYDLRVKAVDPSKLGVDAGVKQYSGYLDDNDADKHLFYWFFESRNDPKNDPVVLWLNGGPGCSSLTGLFLELGPATIDKNLKVVSNPYSWNSNASVIFLDQPVNVGFSYSGSSVSDTVAAGKDVYALLTLFFKQFPEYATQDFHISGESYAGHYIPVFAAEILSHKNTNINLKSALIGNGLTDPLTQYPQYRPMACGEGGYPAVLDQGTCRSMDNSLERCLSLIETCYSSESAWVCVPAAMYCNSAILAPYQQTGMNPYDVRNKCEDMASLCYPQLNVITEWLNQKSVMQALGVEVESYESCNSGINRDFLFHGDWMKPYHRLVPSVLEKIPVLIYAGDADFICNWLGNQAWTDALEWPGHKKFAEAKLEDLKIVDNKNKGKKIGQVKSSGNFTFMRIFGAGHMVPLNQPEASLEFLNRWLRGEWH
Enzyme Length 543
Uniprot Accession Number B8XGR4
Absorption
Active Site ACT_SITE 266; /evidence=ECO:0000255|PROSITE-ProRule:PRU10074; ACT_SITE 458; /evidence=ECO:0000255|PROSITE-ProRule:PRU10074; ACT_SITE 520; /evidence=ECO:0000255|PROSITE-ProRule:PRU10074
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Release of a C-terminal amino acid with broad specificity.; EC=3.4.16.5; Evidence={ECO:0000255|PROSITE-ProRule:PRU10074};
DNA Binding
EC Number 3.4.16.5
Enzyme Function FUNCTION: Vacuolar carboxypeptidase involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (5); Glycosylation (2); Propeptide (1); Signal peptide (1)
Keywords Carboxypeptidase;Disulfide bond;Glycoprotein;Hydrolase;Protease;Signal;Vacuole;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..17; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 60,711
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda