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IPR011356 is a Peptidase M17, leucine aminopeptidase/peptidase B.
<p>The majority of members of this family are zinc-dependent exopeptidases belonging to MEROPS peptidase family M17 (leucyl aminopeptidase, clan MF).</p> <p>Leucyl aminopeptidase (LAP; [ec:3.4.11.1]) selectively release N-terminal amino acid residues from polypeptides and proteins; in general they are involved in the processing, catabolism and degradation of intracellular proteins [[cite:PUB00011211], [cite:PUB00001416], [cite:PUB00004713]]. Leucyl aminopeptidase forms a homohexamer containing two trimers stacked on top of one another [[cite:PUB00004713]]. Each monomer binds two zinc ions. The zinc-binding and catalytic sites are located within the C-terminal catalytic domain [[cite:PUB00004713]]. Leucine aminopeptidase has been shown to be identical with prolyl aminopeptidase ([ec:3.4.11.5]) in mammals [[cite:PUB00000202]].</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 | Aminopeptidase activity | Catalysis of the hydrolysis of N-terminal amino acid residues from in a polypeptide chain. | ||
| Cellular component | Cytoplasm | All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. | ||
| Molecular function | Metalloexopeptidase activity | Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. | ||
| Biological process | Protein metabolic process | The chemical reactions and pathways involving a protein. Includes protein modification. | ||
| Molecular function | Manganese ion binding | Interacting selectively and non-covalently with manganese (Mn) ions. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | PREDICTED: leucine aminopeptidase 3, chloroplastic-like [Cicer arietinum] gi|502149990|ref|XP_004507738.1| | 10 | ||
| – | PREDICTED: leucine aminopeptidase 2, chloroplastic-like [Cicer arietinum] gi|502169702|ref|XP_004514667.1| | 23 | ||
| – | Leucine aminopeptidase, putative; TAIR: AT4G30910.1 Cytosol aminopeptidase family protein; Swiss-Prot: sp|Q6K669|AMPL2_ORYSJ Leucine aminopeptidase 2, chloroplastic; TrEMBL-Plants: tr|A0A0B2SEX9|A0A0B2SEX9_GLYSO Leucine aminopeptidase 3, chloroplastic; Found in the gene: LotjaGi3g1v0327400_LC | 8 | ||
| – | Leucine aminopeptidase; TAIR: AT4G30920.1 Cytosol aminopeptidase family protein; Swiss-Prot: sp|Q6K669|AMPL2_ORYSJ Leucine aminopeptidase 2, chloroplastic; TrEMBL-Plants: tr|A0A0B2SEX9|A0A0B2SEX9_GLYSO Leucine aminopeptidase 3, chloroplastic; Found in the gene: LotjaGi3g1v0327400_LC | 8 | ||
| – | Leucine aminopeptidase, putative; TAIR: AT4G30910.1 Cytosol aminopeptidase family protein; Swiss-Prot: sp|Q6K669|AMPL2_ORYSJ Leucine aminopeptidase 2, chloroplastic; TrEMBL-Plants: tr|A0A0B2SEX9|A0A0B2SEX9_GLYSO Leucine aminopeptidase 3, chloroplastic; Found in the gene: LotjaGi3g1v0327400_LC | 8 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| SSF52949 | SUPERFAMILY | 1 | 20.00 |