ID   AMPP2_AJEDR             Reviewed;         506 AA.
AC   C5GKT2;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase BDCG_04966;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase;
DE   AltName: Full=Prolidase;
GN   ORFNames=BDCG_04966;
OS   Ajellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces
OS   dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=559297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ER-3 / ATCC MYA-2586;
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EQ999977; EEQ89846.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5GKT2; -.
DR   SMR; C5GKT2; -.
DR   STRING; 559297.C5GKT2; -.
DR   EnsemblFungi; EEQ89846; EEQ89846; BDCG_04966.
DR   VEuPathDB; FungiDB:BDCG_04966; -.
DR   eggNOG; KOG2737; Eukaryota.
DR   HOGENOM; CLU_017266_1_2_1; -.
DR   OMA; LHYGANN; -.
DR   Proteomes; UP000002039; Unassembled WGS sequence.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.350.10; -; 1.
DR   Gene3D; 3.90.230.10; -; 1.
DR   InterPro; IPR007865; Aminopep_P_N.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   Pfam; PF05195; AMP_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   SMART; SM01011; AMP_N; 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..506
FT                   /note="Probable Xaa-Pro aminopeptidase BDCG_04966"
FT                   /id="PRO_0000411818"
FT   BINDING         285
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         296
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         433
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         471
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         471
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   506 AA;  56861 MW;  E0CCEE9619BBB78B CRC64;
     MISAIEPKNL LRPHSQPVVT TSTLQPDDEC NIELRIEDTT VDKYPAKQHA RRVAAEIHRD
     RGLVYLMGQK STLYEDSDQE RTFRQRRYFF YMSGVDEPDC DLTYDINADK LTLYVPDFDL
     KRTIWMGPTL GREEALQRFD IDEVKYQSSL DEDVKQWAQN QGRGSTLYLL HESQKPAEKV
     PNVFIDSKTL KHAMDTSRAI KDEHEIGLIR RANEVSAAAH IDVLRGIRKM SNERDIEASF
     LNTSVSLGAH KQAYHIIAAS GSNAATLHYS KNNEPLKGRQ FVCLDAGAEW NCYASDVTRT
     FPMTSQWPSA EAKHIYKLVE HMQESCIVRV KEGVRYLDLH ILAHRSLIRG FLTLGIFKGG
     TLEEIQNSGA SNLFFPHGLG HHIGLEVHDV SPESIMAQDN GDYSDNVLIS PNNLSPCTTS
     SPTLKSGMVV TIEPGIYFSQ IALDNAKPEQ LKYVDLELVK TYMPVGGVRI EDDILVTKTG
     YENLTTAPKG DGMLEIIRQG DGSCNI