IED ID | IndEnz0002002629 |
Enzyme Type ID | protease002629 |
Protein Name |
DNA damage-inducible protein 1 EC 3.4.23.- |
Gene Name | DDI1 CAGL0I06787g |
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 | MQLTVTNDVNGEVYGPLELSGDMMLMDLVALLEVDCAFESGKQQLYFNGKELKPDVEKTLEELGIGNDDLIVIRGQPVSSNSIANSTSAIELDDDAYVEQFRLQLLSNSALRNSLRMPFADIDSLVNDPQQFKTHMGPVIIQRRRMQSAMPTNPYGIPDEEYKKLMTNPEDPEHKKRLQELQDKQLIDEQLRNALEYTPEVFAQVSMLYINMEINGHPVKAFVDSGAQMTIISPRLAEKTELKRFIDNRFIGEARGVGTGKILGRVHQVQVKIETQFIPCSFVVLDSNVDLLLGLDMLKRHQACIDLEKNVLRIAGTETKFLGEAEIPKGTSFDAVGNPQPPVEIKESADHSKKKMKTSFTITPKVKPVKADNLLNNSSPMGNTGRTFPEKTIKQLMDLGFSRQEVIQALVSTNGNAEFAASLLFQ |
Enzyme Length | 426 |
Uniprot Accession Number | Q6FQE9 |
Absorption | |
Active Site | ACT_SITE 224; /evidence=ECO:0000305 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.23.- |
Enzyme Function | FUNCTION: Probable aspartic protease. May be involved in the regulation of exocytosis. Acts as a linker between the 19S proteasome and polyubiquitinated proteins via UBA domain interactions with ubiquitin for their subsequent degradation. Required for S-phase checkpoint control. {ECO:0000250|UniProtKB:I7HUG0, ECO:0000250|UniProtKB:P40087}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Domain (2) |
Keywords | Aspartyl protease;Cytoplasm;Hydrolase;Protease;Protein transport;Reference proteome;Transport |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 47,570 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |