ID   AMPP2_METAQ             Reviewed;         509 AA.
AC   E9E2J4;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase MAC_04092;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase;
DE   AltName: Full=Prolidase;
GN   ORFNames=MAC_04092;
OS   Metarhizium acridum (strain CQMa 102).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655827;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQMa 102;
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.-H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.-Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.-J., St Leger R.J., Zhao G.-P., Pei Y., Feng M.-G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
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; GL698495; EFY89883.1; -; Genomic_DNA.
DR   RefSeq; XP_007810432.1; XM_007812241.1.
DR   AlphaFoldDB; E9E2J4; -.
DR   SMR; E9E2J4; -.
DR   STRING; 92637.XP_007810432.1; -.
DR   PRIDE; E9E2J4; -.
DR   EnsemblFungi; EFY89883; EFY89883; MAC_04092.
DR   GeneID; 19248403; -.
DR   KEGG; maw:MAC_04092; -.
DR   eggNOG; KOG2737; Eukaryota.
DR   HOGENOM; CLU_017266_1_2_1; -.
DR   InParanoid; E9E2J4; -.
DR   OMA; LHYGANN; -.
DR   OrthoDB; 352329at2759; -.
DR   Proteomes; UP000002499; 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..509
FT                   /note="Probable Xaa-Pro aminopeptidase MAC_04092"
FT                   /id="PRO_0000411837"
FT   BINDING         273
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         284
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         284
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         437
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         478
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         478
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   509 AA;  56347 MW;  CC7342C4E68AD841 CRC64;
     MDYDLVMEDE FDALCLDVRR DHDSASKTKY PAKLHARKVV KELGVDDGLI YLPGQPDISL
     ENSDQPRLFR QRRYFFYITG ADFEDCAATY EVKHDKLTLW VPYVEPRQVL WFGSKPSAAE
     CKRRYDVDEV RYTTQLSSFL RRFAAQPEPP VVYILHPDQA PDLGHGSQSQ LRLDSSLLLP
     AMDRARVVKS DYEVAMVRRA NDISSAAHRR VAERILRLTN EREIEAIIQA VCIANGSRSQ
     AYPIIAGSGA NGATLHYGAN NAPLGGKQCV VIDAGCEWNC YASDITRTLP LSGSWTPKAA
     AIHAIVQRMQ QECIAKVGPG TAWRDIHLHA ASLGMEGLLG LGILKGRRED VARAGTVAAF
     FPHGLGHHVG LEVHDVSGTL ALSAAEGHGT QLDFGKRAMV TPSMLADMTR SASSPDAAGV
     QERKTQLLLP NMIVTVEPGI YFCREYLEGY FRSDPAHADF IDWDLLEEYY DVGGVRIEDC
     ILVTEDGYEN LTVAPKGDEL LDVINKGEK