| IED ID | IndEnz0002002698 |
| Enzyme Type ID | protease002698 |
| Protein Name |
Bifunctional peptidase and 3S -lysyl hydroxylase Jmjd7 EC 1.14.11.63 EC 3.4.-.- JmjC domain-containing protein 7 Jumonji domain-containing protein 7 L-lysine 3S -hydroxylase Jmjd7 |
| Gene Name | Jmjd7 |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MAEAALEAVRRALQEFPAAARDLNVPRVVPYLDEPPSPLCFYRDWVCPNRPCIIRNALQHWPALQKWSLSYLRATVGSTEVSVAVTPDGYADAVRGDRFVMPAERRLPISHVLDVLEGRAQHPGVLYVQKQCSNLPTELPQLLSDIESHVPWASESLGKMPDAVNFWLGDASAVTSLHKDHYENLYCVVSGEKHFLLHPPSDRPFIPYNLYTPATYQLTEEGTFRVVDEEAMEKVPWIPLDPLAPDLTQYPSYSQAQALHCTVRAGEMLYLPALWFHHVQQSHGCIAVNFWYDMEYDLKYSYFQLMDTLTRATGLD |
| Enzyme Length | 316 |
| Uniprot Accession Number | P0C872 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-lysyl-[protein] + O2 = (3S)-3-hydroxy-L-lysyl-[protein] + CO2 + succinate; Xref=Rhea:RHEA:57152, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15133, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:141492; EC=1.14.11.63; Evidence={ECO:0000250|UniProtKB:P0C870}; |
| DNA Binding | |
| EC Number | 1.14.11.63; 3.4.-.- |
| Enzyme Function | FUNCTION: Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monooxygenase (PubMed:28847961) (By similarity). Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation (PubMed:28847961). Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity (PubMed:28847961). Additionally, may play a role in protein biosynthesis by modifying the translation machinery. Acts as Fe(2+) and 2-oxoglutarate-dependent monooxygenase, catalyzing (S)-stereospecific hydroxylation at C-3 of 'Lys-22' of DRG1 and 'Lys-21' of DRG2 translation factors (TRAFAC), promoting their interaction with ribonucleic acids (RNA) (By similarity). {ECO:0000250|UniProtKB:P0C870, ECO:0000269|PubMed:28847961}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (20); Chain (1); Disulfide bond (1); Domain (1); Helix (11); Metal binding (3); Turn (3) |
| Keywords | 3D-structure;Aminopeptidase;Cytoplasm;Disulfide bond;Hydrolase;Iron;Metal-binding;Monooxygenase;Nucleus;Oxidoreductase;Protease;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P0C870}. Cytoplasm {ECO:0000250|UniProtKB:P0C870}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 4QSZ; 4QU2; |
| Mapped Pubmed ID | 14681479; 29459673; |
| Motif | |
| Gene Encoded By | |
| Mass | 35,917 |
| Kinetics | |
| Metal Binding | METAL 178; /note=Iron; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00538; METAL 180; /note=Iron; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00538; METAL 277; /note=Iron; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU00538 |
| Rhea ID | RHEA:57152 |
| Cross Reference Brenda | 1.14.11.63; |