AMPP3_PYRTR
ID AMPP3_PYRTR Reviewed; 463 AA.
AC B2WMQ2;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Probable Xaa-Pro aminopeptidase pepP;
DE EC=3.4.11.9;
DE AltName: Full=Aminoacylproline aminopeptidase;
DE AltName: Full=Prolidase;
GN Name=pepP; ORFNames=PTRG_11262;
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; DS231630; EDU44312.1; -; Genomic_DNA.
DR RefSeq; XP_001941593.1; XM_001941558.1.
DR AlphaFoldDB; B2WMQ2; -.
DR SMR; B2WMQ2; -.
DR STRING; 45151.EDU44312; -.
DR MEROPS; M24.A09; -.
DR EnsemblFungi; EDU44312; EDU44312; PTRG_11262.
DR GeneID; 6349575; -.
DR eggNOG; KOG2737; Eukaryota.
DR HOGENOM; CLU_017266_1_2_1; -.
DR InParanoid; B2WMQ2; -.
DR OMA; DQKFIYN; -.
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 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..463
FT /note="Probable Xaa-Pro aminopeptidase pepP"
FT /id="PRO_0000411886"
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 393
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 433
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 433
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 463 AA; 52110 MW; F74145C5533E74B4 CRC64;
MAIAENYEDV LKGKYPAKAH AKKVAEWIIA KGGDKNGTIY LEAQKQKLNE DNDGEAPFRQ
RRYFFYLSGC ELPDSYLTYE IATEKLTLFI PPVEPDEVIW SGLPMSPEEA KEKYDIDQCL
TTKDVNAHLT STSESAQSTI YAIPEQVSDH ITFISYKEKE FKQLKPAIEY CRVIKSDYEI
ALIRKANIIS TAAHEAVMKA ASTAKNECEL EAVFLKACVE RNAKNQAYHS IVAAGEHAAT
LHYVHNAAPI SDQNLLLLDA GCEVDCYASD ITRTFPLKGK FTTESLAIYK IVLDMQHQCI
NALKEGVVWD SVHELAHKVA IKGLLELGIL KGDAEEIFTK RISVAFFPHG LGHYLGMDTH
DTGGNPNYAD KDVMFRYLRT RGSLPERSVI TVEPGVYFCR FIIEPYLKDE EKKKYIDESV
LEKYWSVGGV RIEDNVLVTK NGFENLTPTP KEIDDITKLI LST