Your browser is unable to support new features implemented in HTML5 and CSS3 to render this site as intended. Your experience may suffer from functionality degradation but the site should remain usable. We strongly recommend the latest version of Google Chrome, OS X Safari or Mozilla Firefox. As Safari is bundled with OS X, if you are unable to upgrade to a newer version of OS X, we recommend using an open source browser. Dismiss message
IPR033823 is a Nucellin.
<p>Nucellin (MEROPS identifier A01.073) is an important regulator of a nucellar cell's progressive degradation after ovule fertilization. This degradation is a characteristic of programmed cell death. Nucellin is a plant aspartic endopeptidase specifically expressed in nucellar cells during degradation [[cite:PUB00081352], [cite:PUB00081779]]. The enzyme is characterized by having two aspartic endopeptidase catalytic site motifs, Asp-Thr-Gly-Ser in the N-terminal and Asp-Ser-Gly-Ser in the C-terminal region, and two other regions nearly identical to two regions of plant aspartic proteases. An aspartic endopeptidase is a bilobal enzyme, with each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. One lobe may be evolved from the other through ancient gene-duplication event. Although the three-dimensional structures of the two lobes are very similar, the amino acid sequences are more divergent, except for the conserved catalytic site motif [[cite:PUB00081352]].</p> <p>This entry represents the peptidase domain of nucellin.</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 |
|---|---|---|---|---|
| Molecular function | Aspartic-type endopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: aspartic proteinase Asp1-like [Glycine max] gi|356554625|ref|XP_003545645.1| | 21 | ||
| – | PREDICTED: aspartic proteinase Asp1-like [Glycine max] gi|356554625|ref|XP_003545645.1| | 21 | ||
| – | Eukaryotic aspartyl protease family protein; TAIR: AT1G77480.1 Eukaryotic aspartyl protease family protein; Swiss-Prot: sp|Q0IU52|ASP1_ORYSJ Aspartic proteinase Asp1; TrEMBL-Plants: tr|A0A0B2QFW9|A0A0B2QFW9_GLYSO Aspartic proteinase Asp1; Found in the gene: LotjaGi1g1v0158000 | 22 | ||
| – | Eukaryotic aspartyl protease family protein; TAIR: AT1G44130.1 Eukaryotic aspartyl protease family protein; Swiss-Prot: sp|Q0IU52|ASP1_ORYSJ Aspartic proteinase Asp1; TrEMBL-Plants: tr|A0A0B2QFW9|A0A0B2QFW9_GLYSO Aspartic proteinase Asp1; Found in the gene: LotjaGi1g1v0158000 | 22 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd05475 | CDD | 1 | 25.00 |