IED ID | IndEnz0002007484 |
Enzyme Type ID | protease007484 |
Protein Name |
Signal peptidase complex catalytic subunit SEC11 EC 3.4.21.89 Signal peptidase I |
Gene Name | SEC11 Lema_P074660 |
Organism | Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8) (Blackleg fungus) (Phoma lingam) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta dothideomyceta Dothideomycetes Pleosporomycetidae Pleosporales Pleosporineae Leptosphaeriaceae Leptosphaeria Leptosphaeria maculans species complex Leptosphaeria maculans (Blackleg fungus) (Phoma lingam) Leptosphaeria maculans 'brassicae' group Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8) (Blackleg fungus) (Phoma lingam) |
Enzyme Sequence | MLGVSGMQPRQLAAQILNFALVLSTAFMMWKGLSVVSDSSSPIVVVLSGSMEPAFQRGDLLFLWNRGLDTQVGEIVVYNVKGKDIPIVHRVVRRYGGGKTPLRLLTKGDNNIADDTELYATSQSFLTRKEDVVGSVVGFIPFVGYVTILLSENPWMKQVMLGLMGVMVVLQRE |
Enzyme Length | 173 |
Uniprot Accession Number | E5A8D2 |
Absorption | |
Active Site | ACT_SITE 50; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P15367; ACT_SITE 89; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P15367; ACT_SITE 115; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P15367 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.; EC=3.4.21.89; Evidence={ECO:0000250|UniProtKB:P15367}; |
DNA Binding | |
EC Number | 3.4.21.89 |
Enzyme Function | FUNCTION: Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids (By similarity). {ECO:0000250|UniProtKB:P15367, ECO:0000250|UniProtKB:P67812}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Region (1); Topological domain (2); Transmembrane (1) |
Keywords | Endoplasmic reticulum;Hydrolase;Membrane;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P15367}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P15367}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 19,034 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |