ID   AMPP1_ARTGP             Reviewed;         635 AA.
AC   E4USI8;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 49.
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=MGYG_04346;
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893;
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; DS989824; EFR01339.1; -; Genomic_DNA.
DR   RefSeq; XP_003174169.1; XM_003174121.1.
DR   AlphaFoldDB; E4USI8; -.
DR   SMR; E4USI8; -.
DR   STRING; 63402.XP_003174169.1; -.
DR   EnsemblFungi; EFR01339; EFR01339; MGYG_04346.
DR   GeneID; 10029458; -.
DR   eggNOG; KOG2413; Eukaryota.
DR   HOGENOM; CLU_011781_2_1_1; -.
DR   InParanoid; E4USI8; -.
DR   OMA; YRPGKWG; -.
DR   OrthoDB; 417805at2759; -.
DR   Proteomes; UP000002669; 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..635
FT                   /note="Probable Xaa-Pro aminopeptidase P"
FT                   /id="PRO_0000411776"
FT   BINDING         432
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         443
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         443
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         541
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         555
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         555
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   635 AA;  70370 MW;  4AE66BD1526D5587 CRC64;
     MTILRHPLRF LFKPRFLYFQ SPSGQSSRPF STSQILRTAL DMPPPPVDTT QRLAKLRELM
     AQNKVDVYTF ISSFTGSAGC AIVSMSKAAL STDGRYFSQA AKQLDSNWTL LKRGVEGVPT
     WEEWTAEQAE NGKVVGVDPS LITAADARKL SQTLKTTGGS LIGIDQNLID AVWGDERPAR
     PSNQITVQPV ERAGKSFEEK VEDLRKELAA KKRSAMVIST LDEIAWLFNL RGSDIPYNPV
     FFSYAIVTPS VAELYVDENK LSPEARKHLE GKVVLKPYES IFQASKALAE SKASASSGSG
     GKFLLSNKAS WSVSLALGGE QNVVEVRSPI TDAKAIKNEV ELEGFRKCHI RDGAALIEYF
     AWLENALIKE GAKLDEVDGA NKLFEIRKKY DHFVGNSFDT ISSTGANGAT IHYKPEKSTC
     AVIDPKAMYL CDSGGQYLDG TTDTTRTLHF GEPTEFQKKA YALVLKGHIS IDNAIFPKGT
     TGYAIDSFAR QHLWKEGLDY LHGTGHGVGS FLNVHEGPMG IGSRAQYAEV PLSASNVLSN
     EPGYYEDGNF GIRLENLVIC KEVKTPHKFG DKPFLGFEYI TLVPFCQKLL DASLLTEAER
     KWVNDYHAKV WEKTSPFFEK DELTTNWLKR ETQPI