The domain within your query sequence starts at position 168 and ends at position 589; the E-value for the DPPIV_N domain shown below is 3.3e-102.

GSGTFLFQAGSGIYHIKDGGPHGFTQQPLRPNLVETSCPNIRMDPKLCPADPDWIAFIHS
NDIWISNLVTREERRITYVHNELANMEEDPRSAGVATFVLQEEFDRYSGYWWCPQAERTP
SGGKILRILYEENDESEVEIIHVTSPMLETRRADSFRYPKTGTANPKVTFKMSEIVVDAA
GGIIDVIDKELVQPFEILFEGVEYIARAGWTPEGKHAWSILLDRSQTHLQIVLISPELFI
PVEDDAMDRQRLIESVPDSVTPLIIYEETTDIWINIHDIFHVFPQTHEDEIEFIFASECK
TGFRHLYKITSILKESKYKRSSGGLPAPSDFKCPIKEEITITSGEWEVLGRHGSNIWVDE
ARKLVYFEGTKDSPLEHHLYVTSYANPGEVVRLTDRGYSHSCCLSRHCDFFISKYSNQKN
PH

DPPIV_N

DPPIV_N
PFAM accession number:PF00930
Interpro abstract (IPR002469):

This domain defines serine peptidases belonging to MEROPS peptidase family S9 (clan SC), subfamily S9B (dipeptidyl-peptidase IV). The protein fold of the peptidase domain for members of this family resembles that of serine carboxypeptidase D, the type example of clan SC. This domain is an alignment of the region to the N-terminal side of the active site, which is found in IPR001375.

Dipeptidyl-peptidase IV (EC 3.4.14.5) is also called adenosine deaminase-binding protein (ADA-binding protein) or CD26. The exopeptidase cleaves off N-terminal X-Pro or X-Ala dipeptides from polypeptides (dipeptidyl peptidase IV activity). It serves as the costimulatory molecule in T cell activation and is an associated marker of autoimmune diseases, adenosine deaminase-deficiency and HIV pathogenesis [(PUBMED:1352530), (PUBMED:20959412), (PUBMED:21856036)].

GO process:proteolysis (GO:0006508)

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