| IED ID | IndEnz0002007723 |
| Enzyme Type ID | protease007723 |
| Protein Name |
Carboxypeptidase Y homolog A EC 3.4.16.5 |
| Gene Name | CPYA SNOG_02053 |
| Organism | Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Parastagonospora nodorum) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta dothideomyceta Dothideomycetes Pleosporomycetidae Pleosporales Pleosporineae Phaeosphaeriaceae Parastagonospora Phaeosphaeria nodorum (Glume blotch fungus) (Parastagonospora nodorum) Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Parastagonospora nodorum) |
| Enzyme Sequence | MRVAASALLAGAASAAVAPQQQILKFPSSFSELKEDLWSKPLHNLEESLKSLTGEAKATWDEVATMYPESFDKAAFFSTPKPHTRKHDSEWDHIVKGADVQSVWVENAQGEKEREIDGKLEQFDLRVKKVDPSVLGVDKVKQYSGYLDDNEEDKHLFYWFFESRNDPKNDPVVLWLNGGPGCSSLMGLFMELGPASVMKDGKLKHNDYSWNANASVIFLDQPVNVGYSYSSGSVSNTVAAGKDIYALLTLFFKQFPEYSKQPFHISGESYAGHYIPVFASEILSHKKRNINLQSVLIGNGLTDGLTQYEYYRPMACGEGGWPAVLDESSCQAMDNAYPRCASLIENCYKSESVWSCVPASIYCNNAMIGPYQRTGQNVYDVRRPCGDNQLCYDEIDYISAFLNKKEVMKAVGAEVSSYDSCNFDINRNFLLQGDWMKPYHRVVPGLLEEIPVLVYAGDADYICNWLGNKAWTEALEWKGHEEYKKAEMKDFKIDGDGKKVGEVKSSGNFTFMKIHAGGHMVPFDQPEASLEMVNRWLSGEFWE |
| Enzyme Length | 543 |
| Uniprot Accession Number | Q0V1R1 |
| Absorption | |
| Active Site | ACT_SITE 269; /evidence=ECO:0000255|PROSITE-ProRule:PRU10074; ACT_SITE 460; /evidence=ECO:0000255|PROSITE-ProRule:PRU10074; ACT_SITE 519; /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;Reference proteome;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 | 61,071 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |