ID   A0A183LSC6_9TREM        Unreviewed;       362 AA.
AC   A0A183LSC6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-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   Schistosoma margrebowiei.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=48269 {ECO:0000313|WBParaSite:SMRZ_0000670201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMRZ_0000670201-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; A0A183LSC6; -.
DR   STRING; 48269.A0A183LSC6; -.
DR   WBParaSite; SMRZ_0000670201-mRNA-1; SMRZ_0000670201-mRNA-1; SMRZ_0000670201.
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; 2.
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; 2.
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          3..137
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          205..269
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   DOMAIN          280..355
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   REGION          343..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   362 AA;  40963 MW;  3EECD90C4D95AC66 CRC64;
     LIPIVDRFEA VYEYVTNEGD SFVFRTNLDA PMYKIIKINL SNCDRQHWED LIDHNAESLL
     ESAVCVNEDK LIICHLKNVK SCLSVHKLLT GEKISDIDIS LGCVANVTGR KRDDEAFIHF
     TSFLTPGIIY SYNFSHSHPK LEVIRESKIR NVDLNQFEVK QVFYESKDKT VVPMFLVLPK
     NFQQNNSAPC QLYGYGGFNI SVTPSFSVGR LFFLMHFGGI IAVANIRGGG EYGKSWHDAG
     RLQNKQNSFD DFQAAAEYLL NHGYTNNQKR VFFLFTVFGI SPLHNVKIPS NPDVQYPALL
     ILTADHDDRV VPLHSFKFIA TLQEKLCHNC HQTNPILIRI EPKAGHGQGK PTSKSVSLQA
     NK
//