ID   AMPP1_ARTOC             Reviewed;         624 AA.
AC   C5FHR9;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=MCYG_01718;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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; DS995702; EEQ28899.1; -; Genomic_DNA.
DR   RefSeq; XP_002848784.1; XM_002848738.1.
DR   AlphaFoldDB; C5FHR9; -.
DR   SMR; C5FHR9; -.
DR   STRING; 63405.XP_002848784.1; -.
DR   EnsemblFungi; EEQ28899; EEQ28899; MCYG_01718.
DR   GeneID; 9227763; -.
DR   eggNOG; KOG2413; Eukaryota.
DR   HOGENOM; CLU_011781_2_2_1; -.
DR   OMA; YRPGKWG; -.
DR   OrthoDB; 417805at2759; -.
DR   Proteomes; UP000002035; 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; -; 3.
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..624
FT                   /note="Probable Xaa-Pro aminopeptidase P"
FT                   /id="PRO_0000411777"
FT   BINDING         421
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         432
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         432
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         530
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         544
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         544
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   624 AA;  69198 MW;  5169AF9E340FDAB4 CRC64;
     MTLFRSHLRF LFKPRFLYFQ SPTGQSSRPF STSQILRTAL DMPPPPVDTT QRLAKLRELM
     KQNKVDVYIV PSEDSHQSEY IAPCDGRRAF ISGFTGSAGC AIVSMSKAAL STDGRYFSQA
     AKQLDANWKL LKRGVEGVPT WEEWTAEQAE NGKVVGVDPS LITAADARKL SQTLKATGGS
     LVGIDQNLID IVWGDERPAR PVTTITVQPV ELAGKPFEEK VEALRKELAT KKRSAMVISA
     EIYVDDSRLS PEARKQLEGK VVLKPYDAIF QASKVLAESK ASASDGAASG KFLLSNKASW
     SLSLALGGEQ NVDEVRSPIT DAKAIKNDVE LEGFRKCHIR DGAALIEYFA WLENALIKEG
     AKLDEVDGAD KLYEIRKKYD LFVGNSFDTI SSTGANGAII HYKPEKSTCS VIDPKAMYLC
     DSGGQYKDGT TDTTRTLHFG EPTEFQKKAY ALVLKGHISI DNAIFPKGTT GYAIDSFARQ
     HLWREGLDYL HGTGHGVGSF LNVHEGPMGI GSRAQYAEVP LSAKNVLSNE PGYYEDGNFG
     IRLENLVICK EVETTHKFGD KPFLGFEYIT MVPFCQKLLD ASLLTEAERK WVNDYHAKVW
     EKTSPFFEKD ELTLNWLKRE TQPI