ID   AMPP1_METAQ             Reviewed;         618 AA.
AC   E9E9B2;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   03-AUG-2022, entry version 47.
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=MAC_06460;
OS   Metarhizium acridum (strain CQMa 102).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655827;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQMa 102;
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., Pei Y., Feng M.-G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
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; GL698526; EFY87483.1; -; Genomic_DNA.
DR   RefSeq; XP_007812800.1; XM_007814609.1.
DR   AlphaFoldDB; E9E9B2; -.
DR   SMR; E9E9B2; -.
DR   STRING; 92637.XP_007812800.1; -.
DR   EnsemblFungi; EFY87483; EFY87483; MAC_06460.
DR   GeneID; 19250771; -.
DR   KEGG; maw:MAC_06460; -.
DR   eggNOG; KOG2413; Eukaryota.
DR   HOGENOM; CLU_011781_2_3_1; -.
DR   InParanoid; E9E9B2; -.
DR   OMA; YRPGKWG; -.
DR   OrthoDB; 417805at2759; -.
DR   Proteomes; UP000002499; 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..618
FT                   /note="Probable Xaa-Pro aminopeptidase P"
FT                   /id="PRO_0000411795"
FT   BINDING         414
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         425
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         425
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         523
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         537
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         537
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   618 AA;  67902 MW;  FA55CD49E35CD9EA CRC64;
     MADSSPQLAK LRSLMKERKV HVYVIPSEDS HSSEYIAACD ARREFISGFT GSAGCAIVTL
     EAAALATDGR YFNQAAKQLD GNWTLLKQGL QDVPTWQEWA ASQSAGGKIV AVDPSLLPGS
     AAKKLNDQVR KAGGADLVPL DENIVDIAWG DSRPERPCQP VSVLPDELAG KPVATKIEEL
     RQELAKKNCP GFFVSMLDEV AWLFNLRGSD IPYNPVFFSY ATITPETAIL YVDESKLDDS
     CRAHLRENNV QVKPYDSFLP DARHLHTEVK TKRQAGGDGV VIGNFLISNK ASWAMSRALG
     GDGSVEEMRS PVGDAKAVKN ETEMNGMRAC HVRDGAALIE FFAWLEDQLV DKKIMIDEVQ
     AADKLEQLRS KQQHFVGLSF PTISSTGANA AIIHYGPEKG SCATIDAGSV YLCDSGAQYR
     DGTTDTTRTL HFGKPSDAEK KAYTLVLKGL IGLDTAVFPK GTTGFALDCL ARQHLWKNGL
     DYRHGTGHGV GSYLNVHEGP IGIGTRVQYT EVPLAPGNVL SNEPGYYEDG NFGIRIENIM
     MVREVQTEHC FGDKSYLGFE HVTMVPYCQS LIERDMLTAD EKAWLNAYND EVLKNTRGFF
     EGDDLTMSWL TRETRPVE