ID   AMPP1_COCP7             Reviewed;         651 AA.
AC   C5P7J2;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-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=CPC735_027280;
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; ACFW01000025; EER27392.1; -; Genomic_DNA.
DR   RefSeq; XP_003069537.1; XM_003069491.1.
DR   AlphaFoldDB; C5P7J2; -.
DR   SMR; C5P7J2; -.
DR   MEROPS; M24.009; -.
DR   PRIDE; C5P7J2; -.
DR   EnsemblFungi; EER27392; EER27392; CPC735_027280.
DR   GeneID; 9695032; -.
DR   KEGG; cpw:CPC735_027280; -.
DR   VEuPathDB; FungiDB:CPC735_027280; -.
DR   HOGENOM; CLU_011781_2_3_1; -.
DR   Proteomes; UP000009084; 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   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
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.
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Manganese; Metal-binding; Metalloprotease;
KW   Protease.
FT   CHAIN           1..651
FT                   /note="Probable Xaa-Pro aminopeptidase P"
FT                   /id="PRO_0000411787"
FT   BINDING         448
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         459
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         459
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         557
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         571
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         571
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   651 AA;  72466 MW;  AEBFA0DB692CD098 CRC64;
     MTLFRSSLRL RLPVTLLSPP PIHKHSRLFS ASHRLFTAAE MPVDTSQRLA KLRELMKERH
     VDVYLIPSED SHQSEYIAPC DARRAFISGF TGSAGCAIVS MSKAALSTDG RYFNQAAKQL
     DENWLLLKRG MENVPTWQEW TAEQAEGGKV VGVDPSLITA AEARKLSDTI KNTGGSLVGV
     PDNLVDLVWG GDRPARPREK VMVHPIEFAG QSFEEKITDL RKELTKKKRA GMVISMLDEI
     AWLYNLRGAD IPFNPVFFAY AIVTHSTAEL FVDEAKLTQA VKEHLGDKVA LRPYESIFES
     LKLLSQAAAS NGDEGHQKFL LSDKASWSLN LALGGEEKVE EVRSPIADAK AVKNAVELEG
     TRACHIRDGA ALTEYFAWLE NELINKKTVL NEVDASDKLA QIRSKHKDFV GLSFDTISST
     GPNAAIIHYR AERGNCPNID PNAVYLCDSG AQYLDGTTDT TRTLHFGKPT EMEKKAYTLV
     LKGLISIDTA VFPKGTTGYA IDAFARQHLW RNGLDYLHGT GHGVGSYLNV HEGPMGIGTR
     VQYAETPITA GNVLSDEPGY YEDGNFGIRI ENIVVAKEVK TPHKFGDKPW IGFEHVTMTP
     LCQNLMDTSL LTAEEKKWVN DYHTEVWEKT KGFFNNDELT RNWLKRETQP I