ID   AMPP3_SORMK             Reviewed;         591 AA.
AC   D1ZBF6; F7W336;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase PEPP;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase;
DE   AltName: Full=Prolidase;
GN   Name=PEPP; ORFNames=SMAC_02260;
OS   Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX   NCBI_TaxID=771870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX   PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA   Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K.,
RA   Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S.,
RA   Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.;
RT   "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT   Sordaria macrospora, a model organism for fungal morphogenesis.";
RL   PLoS Genet. 6:E1000891-E1000891(2010).
CC   -!- FUNCTION: Catalyzes the removal of a penultimate prolyl residue from
CC       the N-termini of peptides. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of any N-terminal amino acid, including proline, that
CC         is linked to proline, even from a dipeptide or tripeptide.;
CC         EC=3.4.11.9;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR   EMBL; CABT02000023; CCC12038.1; -; Genomic_DNA.
DR   RefSeq; XP_003350547.1; XM_003350499.1.
DR   AlphaFoldDB; D1ZBF6; -.
DR   SMR; D1ZBF6; -.
DR   STRING; 771870.D1ZBF6; -.
DR   PRIDE; D1ZBF6; -.
DR   EnsemblFungi; CCC12038; CCC12038; SMAC_02260.
DR   GeneID; 10808095; -.
DR   KEGG; smp:SMAC_02260; -.
DR   VEuPathDB; FungiDB:SMAC_02260; -.
DR   eggNOG; KOG2737; Eukaryota.
DR   HOGENOM; CLU_017266_1_2_1; -.
DR   InParanoid; D1ZBF6; -.
DR   OMA; LHYGANN; -.
DR   OrthoDB; 352329at2759; -.
DR   Proteomes; UP000001881; Unassembled WGS sequence.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.350.10; -; 1.
DR   Gene3D; 3.90.230.10; -; 1.
DR   InterPro; IPR007865; Aminopep_P_N.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   Pfam; PF05195; AMP_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   SMART; SM01011; AMP_N; 1.
DR   SUPFAM; SSF53092; SSF53092; 1.
DR   SUPFAM; SSF55920; SSF55920; 1.
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome.
FT   CHAIN           1..591
FT                   /note="Probable Xaa-Pro aminopeptidase PEPP"
FT                   /id="PRO_0000411889"
FT   REGION          31..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          441..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         322
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         333
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         333
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         511
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         552
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         552
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   591 AA;  66317 MW;  3E0D85D67C9EFA35 CRC64;
     MANSDEIHYD LVEDDEFDIV NIVVEGLDET SIHSPPPSVS AATHGGVKNP SFSQRRTSGR
     HDFQKWLHEE LGKYPAKTHA QKVVEELDAP KSGLIYLRGF NEPLYPYSDQ GPPFRQQRHF
     FYLSGADFPG CAVTYDIPRQ HLIVWIRRND PRLSLWYGTT PSIEEVKSKS DVSDVRYIDD
     VTKYLHANLT PDTTLFLLHP DQTPKLEPPS LNLRHRFKGP KIDTTSLLPA IEAARVIKTP
     HEISLIRRAV ALTSLAHRMV LQRIKHLSNE REAHAVFEGF CISQGAPRQS YAVIAASGAN
     ASTLHYEAND QPLEGKQTML LDAGCEWGCY ASDVTRTFPL KGKWTKEGEE IYKVVERMQR
     ETIDAIRPGR LYYKLHLVAC LVAVEELMKL GILHNGTRTE ILAKGTVAAF FPHGLGHHVG
     LEVHDVSGRE RLLLSSSSSS GLSRQAISGS RRLPPPRNMK REQVTPEDLA AMYREAMMDT
     AGDEVEQSAV APPPPYRGRQ RLKENMVVTV EPGIYFHRPY IQSFFLSNPD HAKYINTKVL
     DRYWDVGGVR IEDCILVTKD GYENLTTAPK GKEALKIINA GIPGFPCDGK A