ID   AMPP2_SORMK             Reviewed;         467 AA.
AC   D1ZQL9; F7W1S6;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase SMAC_04549;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase;
DE   AltName: Full=Prolidase;
GN   ORFNames=SMAC_04549;
OS   Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX   NCBI_TaxID=771870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX   PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA   Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K.,
RA   Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S.,
RA   Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.;
RT   "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT   Sordaria macrospora, a model organism for fungal morphogenesis.";
RL   PLoS Genet. 6:E1000891-E1000891(2010).
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; CABT02000020; CCC11561.1; -; Genomic_DNA.
DR   RefSeq; XP_003345316.1; XM_003345268.1.
DR   AlphaFoldDB; D1ZQL9; -.
DR   SMR; D1ZQL9; -.
DR   STRING; 771870.D1ZQL9; -.
DR   MEROPS; M24.A09; -.
DR   PRIDE; D1ZQL9; -.
DR   EnsemblFungi; CCC11561; CCC11561; SMAC_04549.
DR   GeneID; 10802654; -.
DR   KEGG; smp:SMAC_04549; -.
DR   VEuPathDB; FungiDB:SMAC_04549; -.
DR   eggNOG; KOG2737; Eukaryota.
DR   HOGENOM; CLU_017266_1_2_1; -.
DR   InParanoid; D1ZQL9; -.
DR   OMA; DQKFIYN; -.
DR   OrthoDB; 352329at2759; -.
DR   Proteomes; UP000001881; 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; Reference proteome.
FT   CHAIN           1..467
FT                   /note="Probable Xaa-Pro aminopeptidase SMAC_04549"
FT                   /id="PRO_0000411852"
FT   BINDING         263
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         274
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         274
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         397
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
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         437
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   467 AA;  52430 MW;  5F2E27CB515952D7 CRC64;
     MTTTTRMDYE TTLKGKYPAK RHAQRVADYI RNKVPGASGV LYLEGRATKL LEDNDEAEPF
     RQRRYFYYLT GCPLADCHYM YDIDADKSTL FIPPIDPESV IWSGLPVSAD EAKQNWDVDE
     VKYTSDVNAT LAHVGSEKPK GASVFAIPNQ VSDKITFLEF DNKNFSILKE AIEVTRVVKD
     EYELAIMAKA NEISSDGHKA VMQKVKHVQN ERELEAVFLG HCIAKGSRNQ AYHSIVASGR
     AAATLHYVPN NADMAGKLNL LLDAGGEWDC YASDITRTFP INGKFTKESR EVYDIVLKMQ
     NDCIAALKEG VLWDDVHLLA HKIAIDGLLQ IGILQGDKDE ILESRTSVAF FPHGLGHYLG
     MDTHDTGGNP NYADKDTMFR YLRVRGRLPA GSVITVEPGI YFCNFIIEPF LKDPKHSKYI
     NADVLEKYWD VGGVRIEDNL VITKDGTYNL TTAPKDPEEM EKIIQQS