PepX_N

X-Prolyl dipeptidyl aminopeptidase PepX, N-terminal
PepX_N
SMART accession number:SM00940
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 abstract (IPR015251):

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)].

GO process:proteolysis (GO:0006508)
GO function:dipeptidyl-peptidase activity (GO:0008239)
Family alignment:
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There are 89 PepX_N domains in 89 proteins in SMART's nrdb database.

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