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Database: UniProt
Entry: A0A2A4JIM1_HELVI
LinkDB: A0A2A4JIM1_HELVI
Original site: A0A2A4JIM1_HELVI 
ID   A0A2A4JIM1_HELVI        Unreviewed;       764 AA.
AC   A0A2A4JIM1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Prolyl endopeptidase {ECO:0000256|ARBA:ARBA00016310, ECO:0000256|RuleBase:RU368024};
DE            EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
GN   ORFNames=B5V51_1733 {ECO:0000313|EMBL:PCG71558.1};
OS   Heliothis virescens (Tobacco budworm moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC   Noctuidae; Heliothinae; Heliothis.
OX   NCBI_TaxID=7102 {ECO:0000313|EMBL:PCG71558.1, ECO:0000313|Proteomes:UP000218220};
RN   [1] {ECO:0000313|EMBL:PCG71558.1, ECO:0000313|Proteomes:UP000218220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HvINT- {ECO:0000313|EMBL:PCG71558.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:PCG71558.1};
RA   Fritz M.L., Deyonke A.M., Papanicolaou A., Micinski S., Westbrook J.,
RA   Gould F.;
RT   "Contemporary evolution of a Lepidopteran species, Heliothis virescens, in
RT   response to modern agricultural practices.";
RL   Submitted (SEP-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PCG71558.1}.
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DR   EMBL; NWSH01001356; PCG71558.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A4JIM1; -.
DR   STRING; 7102.A0A2A4JIM1; -.
DR   Proteomes; UP000218220; 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   Reference proteome {ECO:0000313|Proteomes:UP000218220};
KW   Serine protease {ECO:0000256|RuleBase:RU368024}.
FT   DOMAIN          65..472
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          538..759
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   764 AA;  86617 MW;  8D80235C4F4CBAD7 CRC64;
     MSNCMAVRRF FANHCRITTK IPVFTTKQRK IFTCARTVTN FEARKRLLCA RASTSAPEKM
     AFHYPEARRD ESVIDDYHGI KISDPYRWLE DPDSNETKEF IDAENRITRP YLDACPVKGD
     INQRLTELWN YPKYSCPFKR GNRYFFFKNT GLQNQNVLYV QDSLDGEPRV FLDPNTLSED
     GTIALSGSRF TEDGNTFAYG LSASGSDWIT IHLKDVASGE DYPEVLEKVK FASMSWTKDN
     KGLFYSRYPD QAGKTDGSET EVNRDQKLCY HRLNTPQADD VIVVEFPEEP LWRIGAEVTD
     CGKYLIVSPV KDCRDNLLFY ADLSKQPDIS GKLHLTQIVH KFEADYEYIT NEGSVCIFRT
     NKNAPNYRLI KIDLHNPAEE NWQTLIPEHP SDVLDWASAV DNDKLVIHYV RDVKSVLQLH
     DMCSGTMLQT FPLEVGSVVG FSGKKEHSEI FYHFMSFLSP GVIYHVDFTK KPYAPTVFRE
     VKVKGFDASQ YEAKQIFYTS KDGTKVPMFI VSKKGLAQDG SNPALIYGYG GFNINIQPSF
     SVTRLVFMQH FNGVVAIPNI RGGGEYGERW HNAGRLLNKQ NVFDDFQYAA QYLIQQRYTR
     PDRVTIQGGS NGGLLVAACI NQRPDLYGAA IVQVGVLDML RFQKFTIGHA WVSDYGSSDN
     KTQFEYLLKY SPLHNIQVPS NTTQYPATLV LTADHDDRVV PLHSLKFIAA LQHAARGTSQ
     QRPLLARVDT KAGHGGGKPT AKIIDEHTDI LCFMSQALGL EFIK
//
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