ID   AMPP2_TALMQ             Reviewed;         386 AA.
AC   B6QAW7;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase PMAA_074180;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase;
DE   AltName: Full=Prolidase;
GN   ORFNames=PMAA_074180;
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
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; DS995900; EEA26345.1; -; Genomic_DNA.
DR   RefSeq; XP_002146892.1; XM_002146856.1.
DR   AlphaFoldDB; B6QAW7; -.
DR   SMR; B6QAW7; -.
DR   STRING; 37727.XP_002146892.1; -.
DR   EnsemblFungi; EEA26345; EEA26345; PMAA_074180.
DR   GeneID; 7024544; -.
DR   KEGG; tmf:PMAA_074180; -.
DR   VEuPathDB; FungiDB:PMAA_074180; -.
DR   HOGENOM; CLU_017266_1_2_1; -.
DR   OrthoDB; 352329at2759; -.
DR   PhylomeDB; B6QAW7; -.
DR   Proteomes; UP000001294; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.230.10; -; 1.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   Pfam; PF00557; Peptidase_M24; 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..386
FT                   /note="Probable Xaa-Pro aminopeptidase PMAA_074180"
FT                   /id="PRO_0000411846"
FT   BINDING         160
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         311
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         350
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         350
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   386 AA;  42492 MW;  6B88B7AC5491D9DA CRC64;
     MGPTISIGEA LDRYDIDNAR YAGSLQTDIS AWLRLRNDDS QIIILHPDHR PPVKYEQDIF
     ETESLVPAMN AARGVKDSYE IELIRKANIV SGLAHTAVLE KIGQMTNESD IAGLFLETCM
     THGAPEQAYG IIAASGENGA TLHYMKNNED FGSRLSVCLD AGAEYECYAS DVTRTFPISS
     TGEWPTTEAR DIYLAVERMQ EECIRMIKPG VRFRDVHIHA SVVAVEELLK LGVFKEGNSV
     DEIMASGAVS VFFPHGLGHH VGLEVHDVSE QSVMAATDDM SPRMRARGFL MQPASMMSAA
     LLEANMIVTV EPGIYFNRLA LKNARTLPIA RFIDFDVVER YYAIGGVRIE DDILVTTDGY
     ENLTTAPKGD AALAIIRKSS VKNSRS