ID   A0A1I8HCW0_9PLAT        Unreviewed;       715 AA.
AC   A0A1I8HCW0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Prolyl endopeptidase {ECO:0000256|ARBA:ARBA00016310, ECO:0000256|RuleBase:RU368024};
DE            EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
OS   Macrostomum lignano.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC   Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX   NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0005473-snap-gene-0.11-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:maker-uti_cns_0005473-snap-gene-0.11-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-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; A0A1I8HCW0; -.
DR   WBParaSite; maker-uti_cns_0005473-snap-gene-0.11-mRNA-1; maker-uti_cns_0005473-snap-gene-0.11-mRNA-1; maker-uti_cns_0005473-snap-gene-0.11.
DR   Proteomes; UP000095280; 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          9..415
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          485..709
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   715 AA;  80144 MW;  1BB2271152706862 CRC64;
     LQANLPKYPD APRDESIVDE FFGVKVSDPY RALEDSDSPG TKSFVEAQNK ISSEYLAGCP
     DREKLRQCLT DLKDYPRYSV DFREGDRYFY WYNSGLQAQS VLKVRDTYDG ESRTLLDPNT
     MSEEGTVSIG QLSMTRDGSV MAYCQSSCGL DWKTIRFKRV ADGSDLPDQL DKVKFSGLAW
     TEDGAGVFYS CYPHGRMSEG GATGDLDLNH KLMYHKLGEP QSRDRLCAEF PDAPKWLVTA
     SVSDCGQYAL IFLTDGCKPA NQLHVCQLAK DCPNGVAAGS GPLPYTVVSD SFDCSYHYIT
     NDGPLFYLMT NGEAPRNRIV TFCLDTMRWL ELVPQHETDV LSTAAVVNRS LILSYRRNVQ
     DVLLVTDLLN RQAWKQIEFG LGTVGSITCE RWHNELFFSY SSFLTPSNQY RVEFSPEGDF
     TTTLVRKSSP KGFDASEYTE KQVFYTSKDG TRVPMFIVRH RDLEGPAPCL LYGYGGFNIS
     IMPYFSTDRL PLLRNYRCAF AVANIRGGDE FGEDWHLGGC LMNKQNCFDD FIAAAEYLVK
     EGVALPDKLV IEGASNGGLL VAACALQRPD LYAGVVCSMG VLDMLRFHKF TIGHGWVSDY
     GTPDGSKSEF RNVFAYSPLH NVARVADRSD WGSDFPALLV LTASHDDRVM ALHSLKFVAE
     VQYRLGSRPG QTRPLLARIE TKDGHGFGRP LNKTIEERAD VYCFMQRSLA LVWRD
//