ID   A0A1D6IVD3_MAIZE        Unreviewed;       767 AA.
AC   A0A1D6IVD3;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Prolyl endopeptidase {ECO:0000256|RuleBase:RU368024};
DE            EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
GN   ORFNames=ZEAMMB73_Zm00001d023749 {ECO:0000313|EMBL:AQK39965.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:AQK39965.1};
RN   [1] {ECO:0000313|EMBL:AQK39965.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQK39965.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) 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; CM000786; AQK39965.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6IVD3; -.
DR   ExpressionAtlas; A0A1D6IVD3; baseline and differential.
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; 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.
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          55..469
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          536..762
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   767 AA;  85846 MW;  2977802FD0F771F0 CRC64;
     MLLLHKSVPL RLLLPRRPLK TFLLPPPSRP RCLSLLPRAA MGSVAGDTAA RLAYPPARRD
     DSVVDDYHGV RIPDPYRWLE DPDSEETKEF VARQAELAET VLAGCPDREN LRREVTRLFD
     HPRHAAPFRR GNKYFYFHNS GLQAQSVLYM LDDLDGKAEV LLDPNTLSKD GTVALSTYSI
     SEDGNYIAYG LSESGSDWVS IHVMSITNKQ PMPDKLSWVK FSSISWTHDG KGFFYGRYPA
     PRGGEVDAGT ETNINLNHQI YYHVLGSDQS EDILCWKDPE HPKYSFGASV TEDGKYIILG
     IYEGCDPVNK LYYCEISSLP QGIEGFRGTQ DLLPFVKLID NFDAQYQVVA NDGDEFTFLT
     NKSAPKNKLV RVNIKNPELW TDVLSEHEKD VLESADAVNN NQLLVNYMSD VKHILQIRDL
     RTGNFIHQLP LEIGSVSEIS CRREDKEVFI GFTSFLSPGI IFRCNLASTI PEMKMFREIS
     VPGFDRTSFQ VKQVFVPSKD GTKIPMFIMS KKDIDLNGSH PTLLYGYGGF NISITPSFSV
     GRVVLCKNMG FVVCVANIRG GGEYGEEWHK AGALAMKQNC FDDFAACAEF LISNGYTSSR
     RLCIEGGSNG GLLVAASINQ VMHGLQTMVV QIRKKSSSGS LSLVYWIYPD PLLQFASLMN
     INRYSPLHNV RRPWEQSSGN NCQYPATMLL TADHDDRVVP LHSLKLLATL QHVLCTSTED
     SPQTNPIIGR IDRKSGHGAG RPTQKMIDEA ADRYSFMAKM LGASWTE
//