IED ID | IndEnz0002002623 |
Enzyme Type ID | protease002623 |
Protein Name |
Mitochondrial presequence protease EC 3.4.24.- |
Gene Name | cym1 AN3853 |
Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
Enzyme Sequence | MLRSYLHLGRHRTPAFRQPLGRLLRPTASILQYAQSRTLASVSSLESLPEVGDQLHGFTVQEKKQVPELHLTAIRLRHDKTHADYLHIAREDKNNVFGIGFKTNPPDATGVPHILEHTTLCGSEKYPIRDPFFKMLPRSLSNFMNAFTSSDHTMYPFATTNQQDFQNLLSVYLDATMHPLLKEEDFRQEGWRLGPEDPRAIQTQEGNLKPEDILFKGVVYNEMKGQMSDANYLYWIRFQESIFPAINNSGGDPQHITDLTHKQLVEFSKKNYNPSNAKIITYGDMPLADHLKQVGGVLNDFSKGAVDTTVKLPIELRGPINVTVPGPIDTFVSEDRQFKTSTSWYMGDITDTVETFSAGILSSLLLDGYGSPMYKALIESGLGSSFTPNTGLDTSGKIPIFSIGVTGVSEEQAPRVKEEIQRVLQETLQRGFNDEKVQGFLHQLELALRHKTANFGLGVIQKTFTSWFNGSDPMKELAWNEVINAFKSRYEKGGYLEALMQKYLINDNCLTFTMVGTPSFNKELDDKEMARKEKKFEQLTQQHGSVEKAVTELAKAELQLLEVQEKAQHADLSCLPSLRVEDISRQKEHKPVRESKVEGTDIVWREAPTNGLTYFQAVNAFADLPDDLRLLLPLFNDAIMRLGTPTRTMEQWEDLIKLKTGGVSTSNFHTTSPTEMGKYTEGLQFSGFALDKNVPDMLEILTALVTETDFTSPSAPAMIQELLRLTTNGALDAVAGTGHRYALNAAAAGLSRSFWAQEQTSGLAQLQATANLLRDAETSPERLAELIEKLRLIQSFAISKTSGLRVRLVCEPASSTQNESVLQRWVTGLPKVPSPTSQPQRFDLSTPSKKAFYDLPYKVYYSGLALPTVPFTHSSSATLSVLSQLLTHNYLHPEIREKGGAYGAGASNGPVKGLFAFTSYRDPNPANTLKVFKNSGVFARDRAWSDREINEAKLGIFQGLDAPVSVDEEGSRYFLNGITHEMDQRWREQVLDVTAKDVNEVAQTFLVDGTRRSVCLLGEKKDWAESEGWEVRKLSMNPNGSNIPSGDAA |
Enzyme Length | 1049 |
Uniprot Accession Number | Q5B6H7 |
Absorption | |
Active Site | ACT_SITE 116; /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 | 117,040 |
Kinetics | |
Metal Binding | METAL 113; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 117; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 222; /note=Zinc; catalytic; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |