ID   AMPP1_TALSN             Reviewed;         657 AA.
AC   B8M9W2;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=TSTA_118800;
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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; EQ962655; EED18114.1; -; Genomic_DNA.
DR   RefSeq; XP_002482106.1; XM_002482061.1.
DR   AlphaFoldDB; B8M9W2; -.
DR   SMR; B8M9W2; -.
DR   STRING; 441959.B8M9W2; -.
DR   MEROPS; M24.009; -.
DR   EnsemblFungi; EED18114; EED18114; TSTA_118800.
DR   GeneID; 8108554; -.
DR   VEuPathDB; FungiDB:TSTA_118800; -.
DR   eggNOG; KOG2413; Eukaryota.
DR   HOGENOM; CLU_011781_2_2_1; -.
DR   InParanoid; B8M9W2; -.
DR   OMA; YRPGKWG; -.
DR   OrthoDB; 417805at2759; -.
DR   PhylomeDB; B8M9W2; -.
DR   Proteomes; UP000001745; 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..657
FT                   /note="Probable Xaa-Pro aminopeptidase P"
FT                   /id="PRO_0000411811"
FT   BINDING         453
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         464
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         464
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         562
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         576
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         576
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   657 AA;  73137 MW;  6E3EA0AED3557264 CRC64;
     MLFSCRAPSL LQRTALSSPL RLFAPCRPSF SRTFVTTTVR FSVEMETVNT SERLAQLREL
     MKQNNLDVYI VPSEDSHQSE YIAHCDARRE FISGFTGSAG TAVISTTAAA LSTDGRYFNQ
     AAKQLDSNWK LLKRGLEGVL TWQEWTAEQA EGGKIVGVDP SVITAASARK LSETLEKGGS
     KLVGIEQNLV DQIWGTHRPQ RPSEKVKIHP IEYAGKPFQE KIADLRKELK TKKRAGFIVS
     VLDEIAWLFN LRGNDIPYNP VFFSYAVITP DTVDLYIDDE KLSPEVKVHL GSDVVIKPYE
     SIFADAKALS AKAPLTESGA PMKYLTSNKA SWALSLSFGG EKKLDEARSP ISDAKAIKNE
     VELKGMRDCH IRDGAALTEY FAWLENELIN KKSTLDEVDG ADKLEQIRSK HDKFVGLSFD
     TISSTGPNAA VIHYKPEKGV CSVIDPNAIY LCDSGAQYLD GTTDTTRTFH FSTPTEMEKK
     AFTLVLKGLI ALDTAVFPKG TSGFALDALA RQHLWRQGLD YLHGTGHGVG AYLNVHEGPI
     GVGTRIQYSE VSLSPGNVIS DEPGYYEDGK FGIRIENIIM AREVETPYKF GDKPWLGFEH
     VTMTPIGQNL IETSLLSKEE RQWVDNYHAE VWEKTSGFFK QDELTLNWLK KETQPLK