ID   A0A0N4ZM74_PARTI        Unreviewed;       687 AA.
AC   A0A0N4ZM74;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Prolyl endopeptidase {ECO:0000256|ARBA:ARBA00016310, ECO:0000256|RuleBase:RU368024};
DE            EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
OS   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0000963200.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0000963200.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) 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; A0A0N4ZM74; -.
DR   WBParaSite; PTRK_0000963200.1; PTRK_0000963200.1; PTRK_0000963200.
DR   Proteomes; UP000038045; 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};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..687
FT                   /note="Prolyl endopeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005891945"
FT   DOMAIN          57..257
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          459..681
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   687 AA;  79545 MW;  F0817DB9AD65A3E9 CRC64;
     MYSNFLFILI LLLILFPNFS TERKYRRHYQ LVEQGKSTHD CSKVKINVNR YPYVKPNYTI
     VDESFGQRIP DFYRDLENTT SKKSITFIKS LNLLSERTLS KSKFRKRIKK TLTRYLDHEK
     FDIYSKDGNY YYFYHNSGLQ EQRVLKRVKN IGDTPETFLD VNTLSKEGTI SLNEIKFSND
     GSIMAYSLSV NGSDWMTIKF KHSNGEDLPD VINNVIFSEM QFVFGNKGFL YGTYDKHSNN
     SIKHVLYYHK MGTDQTDAKY DILDNDRDII YVFTNKNTPL GEIIKMNLKE ISKGGEKWQV
     IVKEKDNAKI DAILSVGSQY FIINRLKDVV SHLYVYDKMN GTLLRELKLP KGVVTKLTGR
     KDSNEFFVAF TNQATPGTVY RGNIDNLKLK RAFKFEKVVQ NVPKGFKGDN LQVTQIFYKS
     TNSTKIPLFM LHRKNLKFNS KNPVLLEVHG GYGIVSKPYF STSRYLFVKK FNGIWCIANI
     RGGGEYGDEW HKAGVKHNKQ NSIDDVIHAA KYLIKHRYTR PSKLSIYGSS NGGFVVTAAS
     QQRPDLFGAV ISKAGVYDML RYPKFSIGKA WIPEYGDPSV EKDFKHLFKI SPLHNIRRPK
     KHRQWPSTLM LSDLHDDRVN IGHTLKYAAS LYHFFKLELD HQKNPVIVEI DKGSGHGIEM
     GLSKLIEEIS DEYAFLHLTL NLRWRNN
//