| IED ID | IndEnz0002010288 |
| Enzyme Type ID | protease010288 |
| Protein Name |
Endogenous retrovirus group K member 104 Pro protein HERV-K104 Pro protein HERV-K_5q13.3 provirus ancestral Pro protein EC 3.4.23.50 Protease Proteinase PR |
| Gene Name | HERV-K104 |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | WASQVSENRPVCKAIIQGKQFEGLVDTEADVSIIALNQWPKNWPKQKAVTGLVGIGTASEVYQSTEILHCLGPDNQESTVQPMITSIPLNLWGQDLLQQWGAEITMPAPLYSPTSQKIMTKMGYIPGKGLGKNEDGIKVPVEAKINQKREGIGYPF |
| Enzyme Length | 156 |
| Uniprot Accession Number | P63124 |
| Absorption | |
| Active Site | ACT_SITE 26; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Processing at the authentic HIV-1 PR recognition site and release of the mature p17 matrix and the p24 capsid protein, as a result of the cleavage of the -SQNY-|-PIVQ- cleavage site.; EC=3.4.23.50; |
| DNA Binding | |
| EC Number | 3.4.23.50 |
| Enzyme Function | FUNCTION: Retroviral proteases have roles in the processing of the primary translation products and the maturation of the viral particle. Endogenous Pro proteins may have kept, lost or modified their original function during evolution (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Domain (2) |
| Keywords | Aspartyl protease;ERV;Hydrolase;Protease;Reference proteome;Ribosomal frameshifting;Transposable element |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Autoproteolytically processed at the N-terminus. Expected C-terminal autoprocessing not detected. The sequence shown is that of the processed Pro protein (By similarity). {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 17,121 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |