IED ID | IndEnz0002001664 |
Enzyme Type ID | protease001664 |
Protein Name |
Signal peptidase complex catalytic subunit SEC11 EC 3.4.21.89 Secretory protein 11 Signal peptidase I |
Gene Name | SEC11 EC1118_1I12_2344g |
Organism | Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's yeast) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's yeast) |
Enzyme Sequence | MNLRFELQKLLNVCFLFASAYMFWQGLAIATNSASPIVVVLSGSMEPAFQRGDILFLWNRNTFNQVGDVVVYEVEGKQIPIVHRVLRQHNNHADKQFLLTKGDNNAGNDISLYANKKIYLNKSKEIVGTVKGYFPQLGYITIWISENKYAKFALLGMLGLSALLGGE |
Enzyme Length | 167 |
Uniprot Accession Number | C8ZAS4 |
Absorption | |
Active Site | ACT_SITE 44; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P15367; ACT_SITE 83; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P15367; ACT_SITE 109; /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); Glycosylation (1); Region (1); Topological domain (2); Transmembrane (1) |
Keywords | Endoplasmic reticulum;Glycoprotein;Hydrolase;Membrane;Protease;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 | 18,762 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |