ID   A0A183AD90_9TREM        Unreviewed;       424 AA.
AC   A0A183AD90;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Prolyl endopeptidase {ECO:0000256|ARBA:ARBA00016310, ECO:0000256|RuleBase:RU368024};
DE            EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
OS   Echinostoma caproni.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Echinostomatidae;
OC   Echinostoma.
OX   NCBI_TaxID=27848 {ECO:0000313|Proteomes:UP000050740, ECO:0000313|WBParaSite:ECPE_0000493701-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ECPE_0000493701-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.;
CC         EC=3.4.21.26; Evidence={ECO:0000256|ARBA:ARBA00001070};
CC   -!- SIMILARITY: Belongs to the peptidase S9A family.
CC       {ECO:0000256|ARBA:ARBA00005228, ECO:0000256|RuleBase:RU368024}.
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DR   AlphaFoldDB; A0A183AD90; -.
DR   WBParaSite; ECPE_0000493701-mRNA-1; ECPE_0000493701-mRNA-1; ECPE_0000493701.
DR   Proteomes; UP000050740; Unplaced.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR023302; Pept_S9A_N.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002470; Peptidase_S9A.
DR   PANTHER; PTHR42881; PROLYL ENDOPEPTIDASE; 1.
DR   PANTHER; PTHR42881:SF2; PROLYL ENDOPEPTIDASE; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   Pfam; PF02897; Peptidase_S9_N; 1.
DR   PRINTS; PR00862; PROLIGOPTASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368024};
KW   Protease {ECO:0000256|RuleBase:RU368024};
KW   Serine protease {ECO:0000256|RuleBase:RU368024}.
FT   DOMAIN          2..55
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          188..396
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   424 AA;  47072 MW;  B2094562B8CB6362 CRC64;
     LSVHDLSTGA KVADLDLPLG SVSGLTGRKR DSLAFVQFTS FLTPGTVFKC DLTEQPPKLE
     VCEYGRGWVS YVVVSQPPCA PCVMHAMYEE ASQTICLGRG SPTQRIDLTL FPHQDAFASG
     SSHTIQVFRE AKLNDVDLSG FTVRQVFYES KDKTRIPMFI VGPKELKLDG TYPCQLYGYG
     GFDIAITPSF SVSRLLLLMN FGGIVAIANI RGGGEYGKRW HDAGRRKLKQ NCFDDFQAAA
     EYLIAGQYTC RDKLYIVGGS NGGLLVCTCC NQRPDLFGAA IAQVPVCDLL RFHKFTIGHA
     WVSDYGDPDT EEDFRVLLKY SPLHNVRVPN DPKTRYPALM ILTADHDDRV VPLHAFKFIS
     TLQASMGERN NPNDRPLLAR IETKAGHGAG KPTSKMVRTC VCVSHRLAFD KDIRDKLIVK
     QIHW
//