Detail Information for IndEnz0002007484
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