| IED ID | IndEnz0002018855 |
| Enzyme Type ID | protease018855 |
| Protein Name |
Carboxypeptidase Y homolog A EC 3.4.16.5 |
| Gene Name | CPYA CarbY |
| Organism | Trichophyton tonsurans (Scalp ringworm fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Trichophyton Trichophyton tonsurans (Scalp ringworm fungus) |
| Enzyme Sequence | MKFLTTGLLATAALAAAQEQQVLQAEDGMGQAPQRGSSIFDETLQKFQSSLEDGISHFWSEMKTNFKDYLPLISLPKKHTRRPDSEWDHVVRGADIESVWVQGADGEKRREIDGKLHNYDLRVKAVDPSKLGVDAGVKQYSGYLDDNDADKHLFYWFFESRNDPKNDPVVLWLNGGPGCSSLTGLFLELGPATIDKNLKVVSNPYSWNSNASVIFLDQPVNVGFSYSGSSVSDTVAAGKDIYALLTLFFKQFPEYATQDFHISGESYAGHYIPVFAAEILSHKNTNINLKSALIGNGLTDPLTQYPQYRPMACGEGGYPAVLDQGTCRSMDNSLERCLSLIETCYSSESAWICVPAAMYCNSAILAPYQQTGMNPYDVRNKCEDMASLCYPQLNVITEWLNQKSVMQALGVEVESYESCNSGINRDFLFHGDWMKPYHRLVPSVLEKIPVLIYAGDADFICNWLGNQAWTDALEWPGHKKFAEAKLEDLKIVDNKNKGKKIGQVKSSGNFTFMRIFGAGHMVPLNQPEASLEFLNRWLRGEWH |
| Enzyme Length | 543 |
| Uniprot Accession Number | A5YCB8 |
| 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 | 60,739 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |