ID   AMPP1_SORMK             Reviewed;         614 AA.
AC   D1ZKF3; F7W9H7;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase P;
DE            Short=AMPP;
DE            Short=Aminopeptidase P;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase;
DE   AltName: Full=Prolidase;
GN   Name=AMPP; ORFNames=SMAC_08089;
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; CABT02000052; CCC13968.1; -; Genomic_DNA.
DR   RefSeq; XP_003347197.1; XM_003347149.1.
DR   AlphaFoldDB; D1ZKF3; -.
DR   SMR; D1ZKF3; -.
DR   STRING; 771870.D1ZKF3; -.
DR   MEROPS; M24.A10; -.
DR   EnsemblFungi; CCC13968; CCC13968; SMAC_08089.
DR   GeneID; 10804617; -.
DR   KEGG; smp:SMAC_08089; -.
DR   VEuPathDB; FungiDB:SMAC_08089; -.
DR   eggNOG; KOG2413; Eukaryota.
DR   HOGENOM; CLU_011781_2_3_1; -.
DR   InParanoid; D1ZKF3; -.
DR   OMA; YRPGKWG; -.
DR   OrthoDB; 417805at2759; -.
DR   Proteomes; UP000001881; Unassembled WGS sequence.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd01085; APP; 1.
DR   Gene3D; 3.40.350.10; -; 2.
DR   Gene3D; 3.90.230.10; -; 1.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000587; Creatinase_N.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR033740; Pept_M24B.
DR   InterPro; IPR032416; Peptidase_M24_C.
DR   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   Pfam; PF01321; Creatinase_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   Pfam; PF16188; Peptidase_M24_C; 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..614
FT                   /note="Probable Xaa-Pro aminopeptidase P"
FT                   /id="PRO_0000411810"
FT   BINDING         411
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         422
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         422
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         520
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         534
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         534
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   614 AA;  67883 MW;  719F8EB7E20C2AF8 CRC64;
     MTVNTTDRLA ALRSLMKERS VDIYVVPSED SHASEYITDC DARRTFISGF SGSAGTAVVT
     LDKAALATDG RYFNQASKQL DENWHLLKTG LQDVPTWQEW TADESAGGKT VGIDPTLISP
     AVAEKLNGDI KKHGGSGLKA VTENLVDLVW GESRPPRPSE PVFLLGAKYA GKGAAEKLTD
     LRKELEKKKA AAFVVSMLDE IAWLFNLRGN DITYNPVFFS YAIVTKDSAT LYVDESKLTD
     EVKQYLAENG TEIKPYTDLF KDTEVLANAA KSTSESEKPT KYLVSNKASW ALKLALGGEK
     HVDEVRSPIG DAKAIKNETE LEGMRKCHIR DGAALIKYFA WLEDQLVNKK AKLNEVEAAD
     QLEKFRSEQS DFVGLSFDTI SSTGPNGAII HYKPERGACS VIDPNAIYLC DSGAQFYDGT
     TDVTRTLHFG QPTAAEKKSY TLVLKGNIAL DTAVFPKGTS GFALDALARQ FLWKYGLDYR
     HGTGHGVGSF LNVHEGPIGI GTRKAYIDVP LAPGNVLSIE PGYYEDGNYG IRIENLAIVR
     EVKTEHQFGD KPYLGFEHIT MVPYCRKLID ESLLTQEEKD WLNKSNEEIR KNMAGYFDGD
     QLTTDWLLRE TSPF