PepX_NX-Prolyl dipeptidyl aminopeptidase PepX, N-terminal | |
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| SMART ACC: | SM000940 |
| Description: | This N-terminal domain adopts a secondary structure consisting of a helical bundle of eight alpha helices and three beta strands, with the last alpha helix connecting to the first strand of the catalytic domain. The first strand of the N-terminus also forms a small parallel beta sheet with strand five of the catalytic domain. This domain mediates dimerisation of the protein, with two proline residues present in the domain being critical for interaction (PUBMED:12377124). |
| InterPro ACC: | IPR015251 |
| InterPro abstract: | This N-terminal domain adopts a secondary structure consisting of a helical bundle of eight α helices and three β strands, with the last α helix connecting to the first strand of the catalytic domain. The first strand of the N terminus also forms a small parallel β sheet with strand five of the catalytic domain. This domain mediates dimerisation of the protein, with two proline residues present … expand |
| GO process: | proteolysis (GO:0006508) |
| GO function: | dipeptidyl-peptidase activity (GO:0008239) |
| Family alignment: | View the Family alignment or the Alignment consensus sequence |
| There are 558 PepX_N domains in 558 proteins in SMART's NRDB database. | |
Taxonomic distribution of proteins containing PepX_N domains
The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing PepX_N domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.
Predicted cellular role
| Cellular role: | Metabolic |
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Relevant references for this domain
Primary literature for the PepX_N domain is listed below. Automatically-derived, secondary literature is also available.
KEGG pathways involving proteins which contain this domain
This information is based on the mapping of SMART genomic protein database to KEGG orthologous groups. Percentages are related to the number of proteins containing a PepX_N domain which could be assigned to a KEGG orthologous group, and not all proteins containing PepX_N domains. Please note that proteins can be included in multiple pathways, ie. the numbers below will not add to 100%.