ID   AMPP1_TRIVH             Reviewed;         698 AA.
AC   D4D891;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
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=TRV_03327;
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFE41910.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; ACYE01000172; EFE41910.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003022528.1; XM_003022482.1.
DR   AlphaFoldDB; D4D891; -.
DR   SMR; D4D891; -.
DR   EnsemblFungi; EFE41910; EFE41910; TRV_03327.
DR   GeneID; 9581105; -.
DR   KEGG; tve:TRV_03327; -.
DR   HOGENOM; CLU_011781_2_1_1; -.
DR   Proteomes; UP000008383; 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   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.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW   Protease.
FT   CHAIN           1..698
FT                   /note="Probable Xaa-Pro aminopeptidase P"
FT                   /id="PRO_0000411812"
FT   BINDING         509
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         520
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         604
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         618
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         618
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   698 AA;  77470 MW;  C74FC33E0CBA2CBD CRC64;
     MTIFRPHLRF LFKPHFLYFQ SPAGQSSRPF STSQILRTAL DMPPPPVDTT QRLAKLRELM
     AQNKVDVYSM QFRYTIKAPL IITVVYSFFF FLLLALKLCL RKTAISQSTL LHVMGVETLI
     RITAAFISSF TGSAGCAIVS MSKAALSTDG RYFSQAAKQL DSNWTLLKRG VEGVPTWEEW
     TAEQAENGKV VGVDPSLITA GENLHYTPLT SVVVTNCSYV IADARKLSQT LKTTGGSLVG
     IDQNLIDAVW GNERPARPAN QITVQPVERA GKPFEEKVED LRKELAAKKR SAMVISTLDE
     IAWLFNLRGS DIPYNPVFFS YAIVTPSVAE LYVDESKLSP EARKHLEGKV VLKPYDSIFQ
     ASKVLAESKA SASSGSSGKF LLSNKASWSL SLALGGEQNV VEVRSPITDA KAIKNEVELE
     GFRKCHIRDG AALIEYFAWL ENALIKEGAQ LDEVDGADKL FEIRKKYDLF VGNSFDTISS
     TGANGATIHY KPEKSTCAVI DPKAMYLCDS GGQYLDGTTD TTRTLHFGEP TEFQKKAYAL
     VLKGHISIDN AIFPKGTTGY AIDSFARQHL WKEGLDYLHG TGHGVGSFLY AEVPLSASNV
     LSNEPGYYED GNFGIRLENL VICKEVQTAH KFGDKPFLGF ESITLVPFCQ KLLDASLLTE
     AERKWVNDYH ARVWEKTSPF FEKDELTTAW LKRETQPI