| IED ID | IndEnz0002006989 |
| Enzyme Type ID | protease006989 |
| Protein Name |
Mitochondrial presequence protease EC 3.4.24.- |
| Gene Name | CYM1 YALI0F21615g |
| Organism | Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Dipodascaceae Yarrowia Yarrowia lipolytica (Candida lipolytica) Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) |
| Enzyme Sequence | MLRLKSLKKPVQAVVRRFATTSAPTLSVGDNIHGFNVLRTKEIPEFDLQATLLEHSTGAQHLHIARDDSNNVFSIGFKTNPPDRTGVPHILEHTTLCGSEKYQVRDPFFKMLNRSLANFMNAMTAQDYTFYPFATTNATDMKNLRDVYLDATLKPLLRELDFSQEGWRLENEDSKDKTSPIILKGVVFNEMKGQMSNAAYAFYIRYLEKIYPSLNNSGGDPLVIPELTYEGLKKFHADHYNPSNAKTFSYGDISVADHLEALNAKFENCEISKTPGNTERLPLEFSSAAENTRIVEEGPIDTLLDTSKQHKMSMSWLMGSPKDIYESFCVKIISSLLIDGHSSPLHQKLIDSGLGSSYSPNTGLDSAPGANIFSVGLQGVTESDLTKVETVILDTIKTTVAEGFDKGRIDGLLHQTELARKDQNAKFGMALMNGVLPGWFNQVDPLEALEWNSVLDRFNKDMEADPEFLQKVMKKYLLDNKYFHFQMNPNPDYEKNVQEKEDEILTDKLAKLTESDKEEIFETGANLEKMQEEPENLDCLPTLHVSDIPRSKPRVALEHTKNPYPIQWRLAPTNGLTYFHSISSLEGLPHEYYPFLPLFTSSLTFLGTKDKTMGQLEDEIKLNTGGLDFSVSCSSSPLSLPSSQLNFAMDGVALDKNVETMFGLFQELLRNTDFTNVEKLKTMIAASTANLSNALAQSGHSFAMLRAASDISPVKKIDDILGGVAQVRFLSELAAKSEQQLVDEVIPKLQEIAKFALTREQRFAVTCGQDMQTKNDELVRKFAESFETNESPFNISSLSIPMTTPTSTLFKLPFQVNYAGIAIPGVPYTHADGAPLQVLANMLTHKHLHREIREKGGAYGGGASYNPTDGFFSYYSYRDPNLERTLQTCQEAGEWSVKKDWSSSDLQEAKLSLFQRIDAPISVKSEGMALYANGLTYEQREKRRRQLLDVAVDDVKRVAKQYLVNPSGYSVAALGPGYETMDKKKWTVLE |
| Enzyme Length | 990 |
| Uniprot Accession Number | Q6C0U8 |
| Absorption | |
| Active Site | ACT_SITE 92; /note=Proton acceptor; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: ATP-independent protease that degrades mitochondrial transit peptides after their cleavage. Also degrades other unstructured peptides (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Metal binding (3); Transit peptide (1) |
| Keywords | Hydrolase;Metal-binding;Metalloprotease;Mitochondrion;Protease;Reference proteome;Transit peptide;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 110,840 |
| Kinetics | |
| Metal Binding | METAL 89; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 93; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 190; /note=Zinc; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |