ID   POPA_GALM3              Reviewed;         738 AA.
AC   H2E7Q7; A0A067SWU5;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   22-JAN-2014, sequence version 2.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Prolyl oligopeptidase A {ECO:0000303|PubMed:22202811};
DE            EC=3.4.21.26 {ECO:0000305|PubMed:22202811};
GN   Name=POPA {ECO:0000303|PubMed:22202811}; ORFNames=GALMADRAFT_70906;
OS   Galerina marginata (strain CBS 339.88).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Strophariaceae; Galerina.
OX   NCBI_TaxID=685588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=CBS 339.88;
RX   PubMed=22202811; DOI=10.1016/j.fgb.2011.12.005;
RA   Luo H., Hallen-Adams H.E., Scott-Craig J.S., Walton J.D.;
RT   "Ribosomal biosynthesis of alpha-amanitin in Galerina marginata.";
RL   Fungal Genet. Biol. 49:123-129(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 339.88;
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA   LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA   Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA   Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT   white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC   -!- FUNCTION: Housekeeping prolyl oligopeptidase (POP) that behaves like a
CC       conventional POP by cleaving peptide bonds on the C-terminal side of
CC       prolyl residues within peptides that are up to approximately 30 amino
CC       acids long (PubMed:22202811). {ECO:0000305|PubMed:22202811}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.;
CC         EC=3.4.21.26; Evidence={ECO:0000305};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P48147}.
CC   -!- SIMILARITY: Belongs to the peptidase S9A family. {ECO:0000305}.
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DR   EMBL; JN827313; AEX26937.2; -; mRNA.
DR   EMBL; KL142383; KDR74502.1; -; Genomic_DNA.
DR   AlphaFoldDB; H2E7Q7; -.
DR   SMR; H2E7Q7; -.
DR   EnsemblFungi; KDR74502; KDR74502; GALMADRAFT_70906.
DR   OrthoDB; 225446at2759; -.
DR   Proteomes; UP000027222; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 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   Pfam; PF00326; Peptidase_S9; 1.
DR   Pfam; PF02897; Peptidase_S9_N; 1.
DR   PRINTS; PR00862; PROLIGOPTASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Protease; Reference proteome; Serine protease.
FT   CHAIN           1..738
FT                   /note="Prolyl oligopeptidase A"
FT                   /id="PRO_0000443715"
FT   ACT_SITE        581
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        665
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
FT   ACT_SITE        701
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10084"
SQ   SEQUENCE   738 AA;  83321 MW;  1B48FFAAC44AFA61 CRC64;
     MARTPWLPNA YPPARRSDHV DIYKSALRGD VRVQDPYQWL EEYTDETDKW TTAQEVFTRT
     YLDKNPDLPR LEKAFQACND YPKSYAPYLH DDNRWYWYYN SGLEPQTALY RSKDSSLPDL
     STADGSGGDL FFDPNALSND GTAALSTYAF SDCGKYFAYG ISFSGSDFVT IYVRLTDSPL
     TKDVDAKNDK GRLPEEIKFV KFSSIGWTPD SKGFFYQRYP DTSTVTQENG PIATEGDLDA
     MVYYHRLGTP QSEDTLIYQD KEHRDWMFSI DVTDDGNYLL LYILKDSSRQ NLLWIAAFDP
     ANLGPNIKWQ KVFDEYHSEY EIITNKGSLF YVRTNESAPQ YRVITVDIAK GNEINELIPE
     TDAYLSSITS VNKGYFALVY KRNVKDEVYV YSHAGNQLAR LAEDFVGAAH VSGREKHSSF
     FVELNGFTSP GTIGRYKFTD PEEQRWSIYR TTKLNGLNTE DFEASQVWYE SKDGTSIPMF
     IVRHKSTKFD GTAPVIQYGY GGFSISIDPF FSATILTFLQ KYGVVFALPN IRGGGEFGED
     WHLAGCREKK GNCFDDFIAA TQYLVKNKYA APDKVTINGG SNGGLLVSAC VNRAPEGTFG
     CAVADVGVHD LLKFHKFTIG KAWTSDYGNP DDPNDFDFIF PISPLQNIPK DKVFPPMLLL
     TADHDDRVVP MHSFKLAAEL QYSLPHNPNP LLIRIDKKAG HGAGKSTQQK IKESADKWGF
     VAQSLGLVWK DSTEQPNL