ID   R9AKR4_WALI9            Unreviewed;       726 AA.
AC   R9AKR4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Prolyl endopeptidase {ECO:0000256|RuleBase:RU368024};
DE            EC=3.4.21.- {ECO:0000256|RuleBase:RU368024};
GN   ORFNames=J056_003252 {ECO:0000313|EMBL:EOR02690.1};
OS   Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC   Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX   NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOR02690.1, ECO:0000313|Proteomes:UP000014064};
RN   [1] {ECO:0000313|Proteomes:UP000014064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX   PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA   Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT   "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT   ichthyophaga: haloadaptations present and absent.";
RL   BMC Genomics 14:617-617(2013).
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   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the peptidase S9A family.
CC       {ECO:0000256|ARBA:ARBA00005228, ECO:0000256|RuleBase:RU368024}.
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DR   EMBL; KE007227; EOR02690.1; -; Genomic_DNA.
DR   RefSeq; XP_009266750.1; XM_009268475.1.
DR   AlphaFoldDB; R9AKR4; -.
DR   STRING; 1299270.R9AKR4; -.
DR   GeneID; 20376204; -.
DR   KEGG; wic:J056_003252; -.
DR   eggNOG; KOG2237; Eukaryota.
DR   HOGENOM; CLU_011290_1_1_1; -.
DR   OMA; LDPWFSH; -.
DR   OrthoDB; 7264at2759; -.
DR   Proteomes; UP000014064; 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:UP000014064};
KW   Serine protease {ECO:0000256|RuleBase:RU368024}.
FT   DOMAIN          4..446
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          521..721
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   726 AA;  81000 MW;  7CFD48A6097225AF CRC64;
     MNYPRVRRDE GNVLEFKSKK NGFVSVKDPY AWLETPPSQS KESADFVDAQ NKLFGNYMED
     VSYRDEFKAA LTDNMSYPKF SAPSIKKNKI AYWSENSGLM PHAVIRSSKN LDSRDSDVFF
     DPNQLSEDKS ASLATAAFSK TAKYFAYGIS RSGSDWVTLY VRSASSPFNE HSGSHETDQS
     RFSDEVRYVK FSSIGWLGDE GFFYQRYDVA EGAHGAANED KAGLETDANE NAKLYFHKVN
     TPQSEDVLVL SDSQNPTHMW SAGTTDDSRY VVLTVSKDTS RRNLLKVADL KDPQNAKISA
     NMKWIDVVGE FKHEYSVIDN DGSKLYLQTN EMADNFKIVT ADVYDSSSIE WKDFIAEDNA
     AVLTDASVVN NDKLVLVYLR DVKSELIVHS LSDGRYLYRL FDDFTGTINQ VTGESDQSKL
     FISTTSYTTP GTVLSFDFDK HASSTFRSTE VHGLSPTEFM TEQQFYTSKD GTKVPIFITR
     HKDTPKNAPF FLFGYGGFSI SVLPFFSPSA LTFVKHFRAG LAVANIRGGS EYGEKWHKDG
     ILDLKQNGFS DFLSASDFLV DTGYAGKGSI IVNGGSNGGL LAAVAAQQDL SNNIAVSIVD
     VGVLDMLKFH KWTIGRAWTS DYGNPDDPSD FDHLHAYSPL HRSQEIKDKI YPAMLLTSAA
     HDDRVVSCHT TKMIAELQHS HIEQVKLARI ETKAGHGAGK STQMRILEAT DKYTFAANEL
     GLKWFK
//