IED ID | IndEnz0002009227 |
Enzyme Type ID | protease009227 |
Protein Name |
Ubiquitin thioesterase OTU1 EC 3.4.19.12 |
Gene Name | GA18292 |
Organism | Drosophila pseudoobscura pseudoobscura (Fruit fly) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora obscura group pseudoobscura subgroup Drosophila pseudoobscura Drosophila pseudoobscura pseudoobscura (Fruit fly) |
Enzyme Sequence | MTGSFSVKLKSKKGQFIVKDLNQNTTLGELKTRIAQATAIQELQLHVLVGYPPKPLDLSENRENQNLKTVGINSGETLIVEEKAGAAGPTSTPLASGSGSSTMEDDEALARRLQAEEDAEHLRQVSSGGSIETGALNIVQSLEPVISPEESGPNGNFNGILLKKVVPADNSCLFTSIRFVLNGKVDNEGSEMMRHIIAQEVSADTQQYNDAVLGKSNSDYCAWIQKADSWGGAIEVSILSNYYGIEIDVVDIQNAIINRFGEDKNFGLRVFLLFDGIHYDPLYMETQQNSVPATIFPVEEMGVYQQAEQIANEAKSSRQFTNVDKFTLRCMDCDVMLVGQGQAQEHAKKTGHENFEEI |
Enzyme Length | 358 |
Uniprot Accession Number | Q29FC9 |
Absorption | |
Active Site | ACT_SITE 169; /evidence=ECO:0000250|UniProtKB:Q96FW1; ACT_SITE 172; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q5VVQ6; ACT_SITE 278; /evidence=ECO:0000250|UniProtKB:Q5VVQ6; ACT_SITE 352; /evidence=ECO:0000250|UniProtKB:Q96FW1 |
Activity Regulation | |
Binding Site | BINDING 277; /note=Substrate; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:Q5VVQ6 |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q5VVQ6}; |
DNA Binding | |
EC Number | 3.4.19.12 |
Enzyme Function | FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (4); Binding site (1); Chain (1); Domain (2); Region (6); Zinc finger (1) |
Keywords | Hydrolase;Metal-binding;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway;Zinc;Zinc-finger |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 39,210 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |