ID   A0A0N4Z5N4_PARTI        Unreviewed;       583 AA.
AC   A0A0N4Z5N4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 22.
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_0000242800.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0000242800.1}
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; A0A0N4Z5N4; -.
DR   WBParaSite; PTRK_0000242800.1; PTRK_0000242800.1; PTRK_0000242800.
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; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU368024};
KW   Protease {ECO:0000256|RuleBase:RU368024};
KW   Serine protease {ECO:0000256|RuleBase:RU368024}.
FT   DOMAIN          29..436
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          510..583
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   583 AA;  66427 MW;  7EFD8AD4885B4F60 CRC64;
     MCNEERVDTE SSKIIVIHPG GLLNNSVYPD IYRNESEGET FSNNITVQDP YRYLNDNNNT
     NRTKFIEKLN NISLTYFTNV SSYNDIKNKV EKYMHYERYD VLGKHGNYYY YLYNNGSQET
     DILIQTDNYT NIRNATKFVD LNNTTKKGYL LTKAAFSSDG DIIAYAVSAN GSDFNTIHFI
     YQNETKLNDT IEHVIYSEIT FVLNGTGFIY SKYPDTKEED GEIKTEYQNH TMYFHKMGTN
     QTKDVPIANS TGEWDIIDGS TSLDGKYLFS TFWIEGSDSN YIKYYDISNC TADNFTEILN
     MTSLFTEENG VNYEIIYSND THALVKTNNN ATYGRVIKVA FSNKNNETLI NEKNDSKLQS
     TWAVGNQFLI LNYLENVTSR LYVYSRLNGS LIQKLDILNL NGTVKQHSAS VESNETFFEF
     ENELTPKTIF RVNLTNVTPN TSLNVEEVAR PKIEGFNSSE FVVKQVFYPS VDSEVNISMF
     ILSRKDVVLN KSNPVLLEVY GAFGVPVTPH FSAPKMMFVK HFNGVSCYAN VRGGGEFGEK
     WHEDGMLLNK QNTFNDTAQA IHYLIENNYT SPTKVALLGG AHG
//