| IED ID | IndEnz0002007907 |
| Enzyme Type ID | protease007907 |
| Protein Name |
Signal peptidase complex catalytic subunit sec11 EC 3.4.21.89 Signal peptidase I |
| Gene Name | sec11 NFIA_064460 |
| Organism | Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Aspergillus fischeri Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus) |
| Enzyme Sequence | MLSFLSSNLSSTRQSLAQVLNFALVLSTAFMLWKGLSVFTASSSPIVVVLSGSMEPAFQRGDLLFLWNRSPRAELGEIVVYNVRGKDIPIVHRVVRTFPQIEGKAKKVKEVTEASSVPPNMLLTKGDNNIADDTELYAKNQDFLHREEDIVGSVRGYMPMVGYVTIMLSEHPWLKTVLLGIMGLMVILQREQ |
| Enzyme Length | 192 |
| Uniprot Accession Number | A1D6D8 |
| Absorption | |
| Active Site | ACT_SITE 53; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P15367; ACT_SITE 92; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P15367; ACT_SITE 133; /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 | 21,426 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |