ID   E1U339_9HEMI            Unreviewed;       711 AA.
AC   E1U339;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 2.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Prolyl endopeptidase {ECO:0000256|ARBA:ARBA00016310, ECO:0000256|RuleBase:RU368024};
DE            EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
OS   Eurygaster integriceps.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC   Pentatomomorpha; Pentatomoidea; Scutelleridae; Eurygastrinae; Eurygaster.
OX   NCBI_TaxID=555972 {ECO:0000313|EMBL:ACI03586.2};
RN   [1] {ECO:0000313|EMBL:ACI03586.2}
RP   NUCLEOTIDE SEQUENCE.
RA   Darkoh C., El-Bouhssini M., Baum M., Clack B.;
RT   "Isolation, purification, and characterization of prolyl-endopeptidase from
RT   Eurygaster integriceps.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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   EMBL; EU934738; ACI03586.2; -; mRNA.
DR   AlphaFoldDB; E1U339; -.
DR   SMR; E1U339; -.
DR   ESTHER; 9hemi-e1u339; S9N_PPCE_Peptidase_S9.
DR   MEROPS; S09.001; -.
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   2: Evidence at transcript level;
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          7..412
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          486..706
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   711 AA;  80779 MW;  3A1780DF4984F546 CRC64;
     MKKFQYPEAR RDETIKETFF GIEVADPYRW LEDPDSEETK NFVDAQNSIS EPYLKGCPAR
     DKIKARLTQM LDYPKYSPPE KEGNHYFYFK NTGLQNHSVL YMQDSLDGPS KVFLDPNTFS
     SDGTVALTST SFSEDGSIMG YTVSKSGSDW CTIHFRRVDT GEDYPEELKF VKFGHAAWTH
     DNLGVFYTRF PEVEGKSDGS ETSQNRNQKI YYHKVGTPQS EDILVVELDD PEYIYTVCVS
     DCGRGVVILP SKFCHNNLVY FSDLSTLKDG IKGKLDVTCI VDKFEADYEF VANTGSKFVF
     RTNKNAHNYK LVVIDFENHS EENWVTLVPE HPTDVLEQAV SVAQDKLVLC YIRDVKNTLD
     IHSLVDGSLI RKIPVPIGTV SSISGSKKHS EVFYTFISFT SPGTIYRCDL SQSPIPDPEV
     FRQITIPGYD PSMFEEKQVF YLSKDGTRIP MFLVHKKVLE QNGKNPCLVY GYGGFNISLL
     PMFSTIRLVF VQYFNAVFAS ANIRGGGEYG EKWHDGGRLL NKQNSFDDFI AAGEYLIAEK
     YTNKSCLAIQ GASNGGLLIG ASVKPPYWLL EDPEYIYTVC VSDCGRWAVI LPSKFCYNNL
     VYFSVLFQEE HFKNVLKYSP LHNIRVPEDQ YPALLLLTAS HDDRVVPLHS LKYIAQLQHV
     MRDNPKQENP LLIQVETKAG HGAGKPTNKR IEEQVDILCF LMNSMNLKFI E
//