ID   AMPP3_COCP7             Reviewed;         469 AA.
AC   C5PHM7;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase PEPP;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase;
DE   AltName: Full=Prolidase;
GN   Name=PEPP; ORFNames=CPC735_054000;
OS   Coccidioides posadasii (strain C735) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=222929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C735;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; ACFW01000049; EER24030.1; -; Genomic_DNA.
DR   RefSeq; XP_003066175.1; XM_003066129.1.
DR   AlphaFoldDB; C5PHM7; -.
DR   SMR; C5PHM7; -.
DR   EnsemblFungi; EER24030; EER24030; CPC735_054000.
DR   GeneID; 9691645; -.
DR   KEGG; cpw:CPC735_054000; -.
DR   VEuPathDB; FungiDB:CPC735_054000; -.
DR   HOGENOM; CLU_017266_1_2_1; -.
DR   Proteomes; UP000009084; 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   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.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW   Protease.
FT   CHAIN           1..469
FT                   /note="Probable Xaa-Pro aminopeptidase PEPP"
FT                   /id="PRO_0000411869"
FT   BINDING         265
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         276
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         276
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         399
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         439
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         439
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   469 AA;  52198 MW;  3382417B65392FBE CRC64;
     MDSAVTAVLA GKYPAKQHAR RVAEALKASG HDGSGVIYLE GTKTRMAEDS DEAVPFRQRR
     NFYYLSGCEL ADSYVTYNID QDELVLYIPA ADPDEVMWTG LPLSPEEALK KYDVDKVLAS
     SEINAHLAHY CTNKETAPKR VYAIPDRVCA ETTFLPFDDT NWDALSNALN QCRKVKDDYE
     IALLKRSNEI SALAHLAVMK AAKLAKNERE LEAVFRSTCL SHGSRGQSYG PIVAAGVNGA
     TLHYQTNDMD LEDPVTGERP SLLVDAGGEY RLYCSDITRA YPLSGKFSVE ARQIYDIVLD
     MQTQCMDMIK PGVAWDDIHA RAHKVAISGL LRLGILRGSE EELFEKRISV AFFPHGLGHY
     MGMDTHDVGG NPNHADPNPM FRYLRLRGTL SPSEVVTVEP GVYFCRFIIE PYLSSPELGK
     YIDSAVLDKY WKVGGVRIED NLVITQDGYL NLTTAPKDPE EVERIVQQG