ID   AMPP1_ARTBC             Reviewed;         698 AA.
AC   D4ARJ9;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 56.
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=ARB_06742;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
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}.
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DR   EMBL; ABSU01000006; EFE34342.1; -; Genomic_DNA.
DR   RefSeq; XP_003014982.1; XM_003014936.1.
DR   AlphaFoldDB; D4ARJ9; -.
DR   SMR; D4ARJ9; -.
DR   STRING; 663331.D4ARJ9; -.
DR   EnsemblFungi; EFE34342; EFE34342; ARB_06742.
DR   GeneID; 9520705; -.
DR   KEGG; abe:ARB_06742; -.
DR   eggNOG; KOG2413; Eukaryota.
DR   HOGENOM; CLU_011781_2_1_1; -.
DR   OMA; YRPGKWG; -.
DR   Proteomes; UP000008866; 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; Reference proteome.
FT   CHAIN           1..698
FT                   /note="Probable Xaa-Pro aminopeptidase P"
FT                   /id="PRO_0000411775"
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;  77502 MW;  D2C6D429300476DD CRC64;
     MTIFRPHLRF LFKPHFLYFQ SPIGKSSRPF STSQILRTAL DMPPPPVDTT QRLAKLRELM
     AQNKVDVYSM QFRYTIKAPL IITVVYSFFF FLLLALKLCL RKTAISQSTL LHVTGVETLI
     RITAAFISSF TGSAGCAIVS MSKAALSTDG RYFSQAAKQL DANWTLLKRG VEGVPTWEEW
     TAEQAENGKV VGVDPSLITA GENLQYSPLT SVIVVNCSYV IADARKLSQT LKTTGGSLIG
     IDQNLIDAVW GDERPARPAN QITVQPVERA GKSFEEKVED LRKELAAKKR SAMVISTLDE
     IAWLFNLRGS DIPYNPVFFS YAIVTPSVAE LYVDESKLSP EARKHLEGKV ILKPYDSIFQ
     ASKVLAESKA SASSGSSGKF LLSNKASWSL SLALGGEQNV VEVRSPITDA KAIKNEVELE
     GFRKCHIRDG AALIEYFAWL ENALIKEGAQ LDEVDGADKL FEIRKKYDLF VGNSFDTISS
     TGANGATIHY KPEKSTCAVI DPEAMYLCDS GGQYLDGTTD TTRTLHFGEP TEFQKKAYAL
     VLKGHISIDN AIFPKGTTGY AIDSFARQHL WKEGLDYLHG TGHGVGSFLY AEVPLSANNV
     LSNEPGYYED GNFGIRLENL VICKEVQTAH KFGDKPFLGF ESITLVPFCQ KLLDASLLTE
     AERKWVNDYH ARVWEKTSPF FEKDELTTAW LKRETQPI