ID   AMPP3_MAGO7             Reviewed;         465 AA.
AC   A4RAE9; G4N2Y5;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase PEPP;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase;
GN   Name=PEPP; ORFNames=MGG_13438;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EHA51744.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CM001233; EHA51744.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_003711551.1; XM_003711503.1.
DR   AlphaFoldDB; A4RAE9; -.
DR   SMR; A4RAE9; -.
DR   STRING; 318829.MGG_13438T0; -.
DR   MEROPS; M24.A09; -.
DR   GeneID; 5050362; -.
DR   KEGG; mgr:MGG_13438; -.
DR   eggNOG; KOG2737; Eukaryota.
DR   InParanoid; A4RAE9; -.
DR   OrthoDB; 352329at2759; -.
DR   Proteomes; UP000009058; Chromosome 3.
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..465
FT                   /note="Probable Xaa-Pro aminopeptidase PEPP"
FT                   /id="PRO_0000411874"
FT   BINDING         259
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         270
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         270
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         395
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         435
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         435
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   465 AA;  51824 MW;  9F9A8FC38B5B44E9 CRC64;
     MASKNYDDVL KGKYPAKEHA RRVVEVIRSS QPDVSGVLYL EGQKTKMIED NDSEEHFRQR
     RYFYYLTGCE LPDCYLTYDI ATSRSTLYIP PVDPESVIWS GLPMSALEAL QKYDVDEVRY
     THEVNAALTS LAEAAPSSTV YAIPNQVSDS ITFLGFGAKN FDVLKPAIER ARVVKSDYEI
     ALIAKANDIS GAAHLAVLKR VRHVSNEREL YATFLAECIS RGAPHMAYHS IVAAGRAAAT
     LHYVKNDEPT AGKLNLLLDA ACELNCYASD ITRTFPISGS FTPESRAIYD TVLRMQLETL
     AMLKEGVRWD DVHIHAHRVA IEGLLAAGIF KKGFSVDEIL ESRTSVAFFP HGLGHYLGMD
     THDTGGNANY QDKDSMFRYL RVRGTLPAGS VITVEPGIYF CNFIIEPYLK DEKHSKYIDA
     AVLDKYWDVG GVRIEDNVVI TKDGYDNLTT AVKDAKEMEK IISSS