ID   AMPP2_MAGO7             Reviewed;         526 AA.
AC   A4RQ11; G4MP22;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase MGG_05684;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase;
DE   AltName: Full=Prolidase;
GN   ORFNames=MGG_05684;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
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; CM001231; EHA57971.1; -; Genomic_DNA.
DR   RefSeq; XP_003710583.1; XM_003710535.1.
DR   AlphaFoldDB; A4RQ11; -.
DR   SMR; A4RQ11; -.
DR   STRING; 318829.MGG_05684T0; -.
DR   EnsemblFungi; MGG_05684T0; MGG_05684T0; MGG_05684.
DR   GeneID; 2675942; -.
DR   KEGG; mgr:MGG_05684; -.
DR   VEuPathDB; FungiDB:MGG_05684; -.
DR   eggNOG; KOG2737; Eukaryota.
DR   HOGENOM; CLU_017266_1_2_1; -.
DR   InParanoid; A4RQ11; -.
DR   OMA; LHYGANN; -.
DR   OrthoDB; 352329at2759; -.
DR   Proteomes; UP000009058; Chromosome 1.
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; Reference proteome.
FT   CHAIN           1..526
FT                   /note="Probable Xaa-Pro aminopeptidase MGG_05684"
FT                   /id="PRO_0000411836"
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         447
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         488
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         488
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   526 AA;  58488 MW;  829B0ECC1E2D0B46 CRC64;
     MGVEHELVVV DEFDALSIEL KRPNGSSSSS PSRAVSVEKY PAKTHARKVA DKLGVDKGLI
     YLQGKPTTTY EDSDMEPPFR QRRYFYYMSG ADFPNAHLTY DVATDQLLLW IPTRQPREEL
     YLGRIPSRED CMSRLDVDDC RDVVQMTRFI AAHLKHHPGT TLFLLHSDQA PGLDDLPVQY
     AGRRLDIGRL RLAVDAARVI KTPFEIRQIR RANQVSSEAH RAVLRQIRHL RTEADVEAVF
     VAACRVRGAR SQAYNPIAGA GANAATLHYV DNAAPLKGKQ TLVLDAGCEW DCYASDITRT
     MPAAGRKFSP EAQTIYRIVE KMQNACIDLV RPGVSYLFIQ ATAQLVAIEE FLKIGLLVGD
     KAKIAASRVV SAFFPHGLGH HVGLETHDVR SERLLGYDKS SAALWRGKRL VMSVEQCDRV
     AELMVTARQQ GADARDALAE GMVITIEPGI YFNRQYIEAF CSDVPERGSF INKSVLDRYY
     PVGGVRIEDD ILVTADGYEN LTTAPKGEEA LRIINGDDVE ADAVLV