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IPR001733 is a Peptidase S26B.
<p>Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes [[cite:PUB00003576]]. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identified, these being grouped into clans on the basis of structural similarity and other functional evidence [[cite:PUB00003576]]. Structures are known for members of the clans and the structures indicate that some appear to be totally unrelated, suggesting different evolutionary origins for the serine peptidases [[cite:PUB00003576]].</p> <p>Not withstanding their different evolutionary origins, there are similarities in the reaction mechanisms of several peptidases. Chymotrypsin, subtilisin and carboxypeptidase C have a catalytic triad of serine, aspartate and histidine in common: serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base [[cite:PUB00003576]]. The geometric orientations of the catalytic residues are similar between families, despite different protein folds [[cite:PUB00003576]]. The linear arrangements of the catalytic residues commonly reflect clan relationships. For example the catalytic triad in the chymotrypsin clan (PA) is ordered HDS, but is ordered DHS in the subtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) [[cite:PUB00003576], [cite:PUB00000522]].</p> <p>This group of serine peptidases belong to MEROPS peptidase family S26 (signal peptidase I family, clan SF), subfamily S26B.</p> <p>Eukaryotic microsomal signal peptidase is involved in the removal of signal peptides from secretory proteins as they pass into the endoplasmic reticulum lumen [[cite:PUB00003576]]. The peptidase is more complex than its mitochondrial and bacterial counterparts, containing a number of subunits, ranging from two in the chicken oviduct peptidase, to five in the dog pancreas protein [[cite:PUB00003576]]. They share sequence similarity with the bacterial leader peptidases (family S26A), although activity here is mediated by a serine/histidine dyad rather than a serine/lysine dyad [[cite:PUB00003576]]. Archaeal signal peptidases also belong to this group.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Biological process | Signal peptide processing | The proteolytic removal of a signal peptide from a protein during or after transport to a specific location in the cell. | ||
| Molecular function | Peptidase activity | Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid. | ||
| Cellular component | Membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: signal peptidase complex catalytic subunit SEC11C-like [Cucumis sativus] gi|449468994|ref|XP_004152206.1| | 7 | ||
| – | PREDICTED: signal peptidase complex catalytic subunit SEC11C-like [Glycine max] gi|356561967|ref|XP_003549247.1| | 4 | ||
| – | Signal peptidase I; TAIR: AT1G52600.1 Peptidase S24/S26A/S26B/S26C family protein; Swiss-Prot: sp|Q9BY50|SC11C_HUMAN Signal peptidase complex catalytic subunit SEC11C; TrEMBL-Plants: tr|I3ST46|I3ST46_LOTJA Signal peptidase I; Found in the gene: LotjaGi3g1v0010300 | 14 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd06530 | CDD | 1 | 33.33 |