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Database: UniProt
Entry: N6T232_DENPD
LinkDB: N6T232_DENPD
Original site: N6T232_DENPD 
ID   N6T232_DENPD            Unreviewed;       706 AA.
AC   N6T232;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Prolyl endopeptidase {ECO:0000256|ARBA:ARBA00016310, ECO:0000256|RuleBase:RU368024};
DE            EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
DE   Flags: Fragment;
GN   Name=109540986 {ECO:0000313|EnsemblMetazoa:ENN74169};
GN   ORFNames=YQE_09142 {ECO:0000313|EMBL:ENN74169.1};
OS   Dendroctonus ponderosae (Mountain pine beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Curculionidae; Scolytinae; Dendroctonus.
OX   NCBI_TaxID=77166 {ECO:0000313|EMBL:ENN74169.1};
RN   [1] {ECO:0000313|EMBL:ENN74169.1, ECO:0000313|Proteomes:UP000019118}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23537049; DOI=10.1186/gb-2013-14-3-r27;
RA   Keeling C.I., Yuen M.M., Liao N.Y., Roderick Docking T., Chan S.K.,
RA   Taylor G.A., Palmquist D.L., Jackman S.D., Nguyen A., Li M., Henderson H.,
RA   Janes J.K., Zhao Y., Pandoh P., Moore R., Sperling F.A., W Huber D.P.,
RA   Birol I., Jones S.J., Bohlmann J.;
RT   "Draft genome of the mountain pine beetle, Dendroctonus ponderosae Hopkins,
RT   a major forest pest.";
RL   Genome Biol. 14:R27-R27(2013).
RN   [2] {ECO:0000313|EnsemblMetazoa:ENN74169}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JAN-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   EMBL; APGK01047157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KB741077; ENN74169.1; -; Genomic_DNA.
DR   RefSeq; XP_019765155.1; XM_019909596.1.
DR   RefSeq; XP_019765156.1; XM_019909597.1.
DR   RefSeq; XP_019765157.1; XM_019909598.1.
DR   AlphaFoldDB; N6T232; -.
DR   MEROPS; S09.001; -.
DR   EnsemblMetazoa; ENN74169; ENN74169; YQE_09142.
DR   GeneID; 109540986; -.
DR   HOGENOM; CLU_011290_1_1_1; -.
DR   OMA; LDPWFSH; -.
DR   OrthoDB; 7264at2759; -.
DR   Proteomes; UP000019118; Unassembled WGS sequence.
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          6..413
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          479..700
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ENN74169.1"
SQ   SEQUENCE   706 AA;  80410 MW;  768D54AE4A48B465 CRC64;
     MSFTYPKPRR DETVKDDFFG TQVSDPYRWL EDPDSEETRS FVNAQNEISR PYLENCPYKD
     SIRSRITQLW DFMRFSVPFK HGNKYFQYRN TGLQNQSVLY VQDSLKGKER VFLDLNGFSE
     DGTVALSGNC FSDDGSTFAY GLSSSGSDWI EIRFRDVETG EDHPETLKKV KYSPMTWMHD
     NKGFFYGGYL NQTGKADGSE TTSSENQKLY YHELGTDQSQ DVVVVEFEDK ELRMGACVSH
     CGTYLVITPI KGCKNNLLYF ARIDPTNRIN KPLELTPVVT TFEADYKYIT NVGSKFYFRT
     NKDAMNYRII IINFNNPSES EWTNLIAEHP KDVLHDVKVI NKTMLVICYL KDVKHTMHIF
     DINTGNKIYN FKLDVGTVSE ISGKRHHSEM FYSVCSFLTP SIIYRVQFNG DQITEERYYE
     TKVADFDPSL YETKQVFYKS KDGTNIPMFI INKIGFVNDG SQPCLLYGYG GFNVNLTPSF
     AISRLVFVGN FNGVYALANI RGGGEYGDNW HNGGRFANKQ NCFDDFQHAA KYLIEENYTS
     ASKLTIQGGS NGGLLVAACI NQAPELFGAA ICQVGVLDML RYHKFTIGYA WKSDYGCSDE
     EDEFKYLYKY SPLHNITVPK NGAQYPATLL LTADHDDRVV PLHSLKFCAE LQEKIGNLPQ
     QENPLLIRIE TKAGHGAGKP TAKMIEEMTE IFCFISKALG LPFSEQ
//
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