IED ID | IndEnz0002014610 |
Enzyme Type ID | protease014610 |
Protein Name |
Mitochondrial presequence protease EC 3.4.24.- |
Gene Name | cym1 AFUA_4G07910 |
Organism | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
Enzyme Sequence | MLRSFSGAGKCKCRIPVSRQPVCGRSLRISSTLTPWNQSRRAASTVTSLDSFPNVGEKLHGFTVQEKKHVPELHLTAVRLKHDKTDADYLHVAREDKNNVFGIGFKTNPPDATGVPHILEHTTLCGSEKYPIRDPFFKMLPRSLSNFMNAFTSADHTTYPFATTNRQDFQNLLSVYLDATLHPLLKEEDFRQEGWRLGPEDPRSILTQGEQSKGNLQSEDVVFKGVVYNEMKGQISDANYLYYIKYRESICPSLNNSGGDPQYITDLTHQQLVDFSKRNYHPSNAKILTYGDMPLSVHLKQIGEVLDGFEKGQADTDVKLPLDLSRGPLNVTVPGPIDTFASEDKQYKTSTSWYMGDTTDVVETFSVGILSSLLLDGYGSPMYRALIEGGLGSSFTPNTGLDSSGRVPIFSVGLTGVSEADAPKVKSTIKRVFEESLSSGFNDEKVQGFLHQLELALRHKTANFGIGVMEKTLSSWFNGSNPMKELSWNEVIDEFKKKYEQGGYLESLMQKYLMNDNCLTFTMVGTPSYNKDLDDQEMVRKEKKLSELVERHGSVEQAVSALAEEELQLLKIQEEAQNADLSCLPSLRVEDISREKERKPVRESKMDDIDVVWREAPTNGLTYFQALNSFEELPDDLRLLLPLFNDCIMRLGTGDKTMEQWEDLIKLKTGGITTSTLHTSSPTELGKFREGLQFSGYALDNNIPDMLQILTTLVTETDFTSPHAPAMIQELLRMTTNGALDAVAGSGHRYALNAAAAGLSRSFWVQEQQSGLAQLQATANLLRDAESSPERLAELIDKLRLIQSFAISKGSGLRVRMVCEPSSASQNEIVLQKWLAGLPRNRSPTSPLDHTSVNSVANRVFYDLPYKVYYSGLAMQTVPFIDPSSAPLSVLSQLLTHKYLHPEIREKGGAYGAGASNGPIKGFFAFTSYRDPNPVNSLKVFQNSGIFARDRAWSDRELAEAKLGIFQGLDAPMSVDEEGARYFMSGVTHEMDQRWREQVLDVTAKDVNEVAQKFLVEGSRQSICLLGEKKDWADSDDWEVRKLSMNASGEPVIDPLSQDGAVASA |
Enzyme Length | 1065 |
Uniprot Accession Number | Q4WP38 |
Absorption | |
Active Site | ACT_SITE 120; /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 | 118,563 |
Kinetics | |
Metal Binding | METAL 117; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 121; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 230; /note=Zinc; catalytic; /evidence=ECO:0000250 |
Rhea ID | |
Cross Reference Brenda |