| IED ID | IndEnz0002016464 |
| Enzyme Type ID | protease016464 |
| Protein Name |
Probable di- and tripeptidase DUG2 EC 3.4.-.- Deficient in utilization of glutathione protein 2 GSH degradosomal complex subunit DUG2 |
| Gene Name | DUG2 YBR281C YBR2018 |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MYDSRGVALHSELIHRWNHAFSILSIVAFPKKRLLFAGSQDSKILVFDLPTYNLIHTIRLGESQEETHTRSSVLCLTGSEDENFLFSGGADSLVRIWSIGEKTIRDDFLPVTEIATVYSVTDIGDIFSLAYLDSLETIVFGCQNASLLYVENLIQKIEKKSSDGVENINKLPHRRYDKFFDSLGPTGYSSNSLSQTSLTSLQENCGAAIIEVPSENIIKYAHYGFIYSINKLCPRFNQLLEKSSRTSGAEHIISSAGDGISKLWEFSKDKGQNTVKISLINDKIDNEDSVISQTIEFPFLYCGLTDGIIKIWDLNTQQIISTLKTKHESDVISISVYMDHVFAIDESGITHFYQNQVNHWNPQQGKILSSEIFSKSNAGSVSLLTGGSDGSLTLWDITSLLSAVPLSSNSPINASSTLQTTNLWAAYQSASLNNEEMLNTLRELISFQTVSQSKDTTNTLSLRRCAIYLQQLFLKFGATNSQLFPLPDGGNPVVFAYFQGNGKVSQVKGAKKKRILWYGHYDVISSGNTFNWNTDPFTLTCENGYLKGRGVSDNKGPLVSAIHSVAYLFQQGELVNDVVFLVEGSEEIGSASLKQVCEKYHDIIGKDIDWILLSNSTWVDQEHPCLNYGLRGVINAQIKVWSDKPDGHSGLNGGVYDEPMVNLVKIVSKLQNEQNEIMIPNFYSPLKDLTEEEYQRFQKITELANIDENTTVQDLITNWTKPSLSMTTVKFSGPGNITVIPKSVTMGISIRLVPEQSVEQVKRDLKAYLEESFKQLKSQNHLEIKVLNEAEGWLGDPTNHAYQILKDEITTAWDVEPLLVREGGSISCLRMLERIFDAPAVQIPCGQSTDNGHLANENLRIKNWSNLTEILSKVFNRL |
| Enzyme Length | 878 |
| Uniprot Accession Number | P38149 |
| Absorption | |
| Active Site | ACT_SITE 522; /evidence=ECO:0000250; ACT_SITE 586; /note=Proton acceptor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.-.- |
| Enzyme Function | FUNCTION: Component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond. {ECO:0000269|PubMed:17179087}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Metal binding (5); Repeat (6) |
| Keywords | Cytoplasm;Dipeptidase;Hydrolase;Metal-binding;Metalloprotease;Nucleus;Protease;Reference proteome;Repeat;WD repeat;Zinc |
| Interact With | Itself; P53871 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10341424; 10688190; 11283351; 11805837; 16429126; 16554755; 19536198; 20675578; 22034500; 22170048; 22277648; 22684328; 23198979; 23217712; 24040173; 25817432; |
| Motif | |
| Gene Encoded By | |
| Mass | 98,071 |
| Kinetics | |
| Metal Binding | METAL 520; /note=Zinc 2; /evidence=ECO:0000250; METAL 553; /note=Zinc 1; /evidence=ECO:0000250; METAL 553; /note=Zinc 2; /evidence=ECO:0000250; METAL 587; /note=Zinc 1; /evidence=ECO:0000250; METAL 853; /note=Zinc 1; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |