ID   AMPP2_PYRTR             Reviewed;         660 AA.
AC   B2WKR4;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Probable Xaa-Pro aminopeptidase PTRG_10574;
DE            EC=3.4.11.9;
DE   AltName: Full=Aminoacylproline aminopeptidase;
DE   AltName: Full=Prolidase;
GN   ORFNames=PTRG_10574;
OS   Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS   (Drechslera tritici-repentis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=426418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pt-1C-BFP;
RX   PubMed=23316438; DOI=10.1534/g3.112.004044;
RA   Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA   Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA   Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA   Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA   Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT   "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT   repentis, reveals transduplication and the impact of repeat elements on
RT   pathogenicity and population divergence.";
RL   G3 (Bethesda) 3:41-63(2013).
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; DS231628; EDU43624.1; -; Genomic_DNA.
DR   RefSeq; XP_001940905.1; XM_001940870.1.
DR   AlphaFoldDB; B2WKR4; -.
DR   SMR; B2WKR4; -.
DR   STRING; 45151.EDU43624; -.
DR   EnsemblFungi; EDU43624; EDU43624; PTRG_10574.
DR   GeneID; 6348881; -.
DR   eggNOG; KOG2737; Eukaryota.
DR   HOGENOM; CLU_017266_1_2_1; -.
DR   InParanoid; B2WKR4; -.
DR   OMA; SLQPAMN; -.
DR   OrthoDB; 352329at2759; -.
DR   Proteomes; UP000001471; 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..660
FT                   /note="Probable Xaa-Pro aminopeptidase PTRG_10574"
FT                   /id="PRO_0000411849"
FT   REGION          641..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         274
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         285
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         285
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
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         476
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         476
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   660 AA;  74551 MW;  58CEEF14C5FAF623 CRC64;
     MEVLDATGLA ERLRWEDNDY LLHLKAETSF DKYPAKQHAR RVQAELGVED GLIYLPGQPA
     RNNEDSDMPA PFRQRRYFYY MSGCDEPDCH LMYDIRRDVL TLFIPRIKPE RVIWNGRGST
     PAEALAKYDI DQVHHSQDLA YIIQNWAFKH QNTGIYILHP SSRIPGCDNL MPRIDSHSLQ
     PAMNLCRMIK DDHEIKRIRK ANDISSQAHR EVLANIQKYK NEAQVEGLFM DVCISRQAKQ
     QAYDPIAASG PNAGTLHYDA NNEDLAGRQL MCLDAGCEFE LYASDITRTF PLSASWPSKE
     AENIYNLVQR MQETCIERLE PGVRYLDLHI MAHQVAIDGL LRLGILCNGT REEIYKAGTS
     RAFFPHGLGH HIGLEVHDVG QAELMSVRRG KPVYQQAPSL YPENFHDPVY DSETCHAPTD
     PQSSHLEEGM VVTVEPGIYF SVYALQHFYL PSPIHSKFIN LEVLERYLPV GGVRIEDDIL
     ITANGHENLT TAPKGEAMLD MIRQGKPGTT DVLIPSPTYS RRMRSENNTP RLCAPGISKN
     TLRPLLTPLA RAATLPTEFR QQDDFDFEPT VGPSLFSGFS RAMTTEEKIQ QWKQKRDSVP
     VALNRPTKAK SLSPVCGENT PNVQHVYMST ASDLASFSQL SAGSGSTPLW KPHNKQDKKN