The domain within your query sequence starts at position 143 and ends at position 704; the E-value for the Peptidase_M49 domain shown below is 1.3e-236.



PFAM accession number:PF03571
Interpro abstract (IPR039461):

Peptidase family M49 contains exopeptidases that remove dipeptides from the N terminus of peptides and proteins and are known as dipeptidyl-peptidases (DPP). The best characterized of these is dipeptidyl-peptidase III (DPPIII; EC ; MEROPS identifier M49.001). The exopeptidases in M49 are metal-dependent, and bind a single zinc ion via the histidines in an HEXXXH motif, in which the distance between the histidines in one residue longer than in the HEXXH zinc-binding motif found in endopeptidases of clan MA. The importance of the histidines and the glutamic acid was identified by site-directed mutagenesis [ (PUBMED:10387075) ]. Some members of family M49, notably from bacteria such as Colwelia and plants possess the more usual HEXXH motif [ (PUBMED:27467751) ]. A third zinc ligand occurs within a motif that has been described as EECRAE [ (PUBMED:18550518) ]. DPPIII releases N-terminal dipeptides sequentially from peptides such as angiotensins II and III, Leu-enkephalin, prolactin and alpha-melanocyte-stimulating hormone, but tripeptides are poor substrates and polypeptides of more than ten residues are not cleaved [ (PUBMED:6749851) (PUBMED:3348886) ]. DPPIII is a soluble, cytosolic enzyme with a housekeeping role, but is elevated in retroplacental serum may participate in the increased angiotensin hydrolysis seen during pregnancy [ (PUBMED:3791505) ].

This family also includes Nudix hydrolase 3 (NUDT3) from plants, which is thought to hydrolyse nucleoside diphosphate derivatives because of the presence of a Nudix box. Isopentenyl diphosphate (IPP), a universal precursor for the biosynthesis of isoprenoid compounds, is hydrolysed; purine nucleotides such as 8-oxo-dATP are dephosphorylated; and the enzyme acts as a dipeptidyl-peptidase against dipeptidyl-2-arylamide substrates [ (PUBMED:27467751) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Peptidase_M49