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IPR002410 is a Peptidase S33.
<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 entry represents a group of serine peptidase belonging to peptidase family S33 (clan SC). They include prolinases (Pro-Xaa dipeptidase, [ec:3.4.13.18]), prolyl aminopeptidases ([ec:3.4.11.5]), and L-amino acid amidases.</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 | Proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. | ||
| 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. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | Proline iminopeptidase [Medicago truncatula] gi|357507583|ref|XP_003624080.1| | 9 | ||
| – | PREDICTED: proline iminopeptidase-like [Glycine max] gi|356554862|ref|XP_003545761.1| | 9 | ||
| – | PREDICTED: proline iminopeptidase-like [Glycine max] gi|356554862|ref|XP_003545761.1| | 13 | ||
| – | PREDICTED: proline iminopeptidase-like [Glycine max] gi|356554862|ref|XP_003545761.1| | 12 | ||
| – | Proline iminopeptidase; TAIR: AT3G61540.1 alpha/beta-Hydrolases superfamily protein; Swiss-Prot: sp|P46547|PIP_AERSO Proline iminopeptidase; TrEMBL-Plants: tr|A0A0B2S853|A0A0B2S853_GLYSO Proline iminopeptidase; Found in the gene: LotjaGi1g1v0481500 | 9 | ||
| – | Proline iminopeptidase; TAIR: AT2G14260.1 proline iminopeptidase; Swiss-Prot: sp|P93732|PIP_ARATH Proline iminopeptidase; TrEMBL-Plants: tr|I1ME45|I1ME45_SOYBN Proline iminopeptidase; Found in the gene: LotjaGi1g1v0665000 | 10 | ||
| – | Proline iminopeptidase; TAIR: AT2G14260.1 proline iminopeptidase; Swiss-Prot: sp|P93732|PIP_ARATH Proline iminopeptidase; TrEMBL-Plants: tr|I1ME45|I1ME45_SOYBN Proline iminopeptidase; Found in the gene: LotjaGi1g1v0665000 | 12 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| TIGR01249 | TIGRFAM | 1 | 14.29 |