ID   MEP_PYRTR               Reviewed;         653 AA.
AC   B2WKX9;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Extracellular metalloproteinase;
DE            EC=3.4.24.-;
DE   AltName: Full=Elastinolytic metalloproteinase MEP;
DE   AltName: Full=Fungalysin MEP;
DE   Flags: Precursor;
GN   Name=MEP; ORFNames=PTRG_10639;
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: Secreted metalloproteinase that allows assimilation of
CC       proteinaceous substrates. {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- INDUCTION: Expression is controlled by the prtT transcription factor.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR   EMBL; DS231628; EDU43689.1; -; Genomic_DNA.
DR   RefSeq; XP_001940970.1; XM_001940935.1.
DR   AlphaFoldDB; B2WKX9; -.
DR   SMR; B2WKX9; -.
DR   STRING; 426418.B2WKX9; -.
DR   MEROPS; M36.001; -.
DR   PRIDE; B2WKX9; -.
DR   EnsemblFungi; EDU43689; EDU43689; PTRG_10639.
DR   GeneID; 6348947; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   InParanoid; B2WKX9; -.
DR   OMA; IRKDSYT; -.
DR   OrthoDB; 1136823at2759; -.
DR   Proteomes; UP000001471; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.390.10; -; 1.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR001842; Peptidase_M36.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   Pfam; PF07504; FTP; 1.
DR   Pfam; PF02128; Peptidase_M36; 1.
DR   PRINTS; PR00999; FUNGALYSIN.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..244
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407191"
FT   CHAIN           245..653
FT                   /note="Extracellular metalloproteinase"
FT                   /id="PRO_0000407192"
FT   ACT_SITE        430
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         429
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         433
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        327
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        412
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        636
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        637
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   653 AA;  71711 MW;  FB5013718D392CDD CRC64;
     MRSFLLASLA SLSVISVYGH PHARSTLTRR GVDLDSYRMK HAATYKNVAE VVADHNINTL
     AKRASAQDIA TDLVKATIPN ATFRLVSDSY VSDNGVAHFY FKQTANGLDI DTADFNVNIG
     RDGNVFSFGN SFYKGDVPAP PSLTKRDGSE PVAALKSAVD VLALPVSAQS ATAEPKDATE
     TYAIKKTTGT VSEPEARLVY LVDDEGKLAL TWRVETDIMS NWLLSYVDVK DGSKVHAVVD
     YSADATYNVY PWGINDPTEG ERQLVTDGFY PPASEFGWHN DGKMAFKTTR GNNGIAHTNW
     DNKMSGFLDL PRPTSEDLNF DYPFSLNQTD FHDYGNASIT QLFYTSNKYH DLLYTLGFNE
     KAGNFEINNN GAGGVGQDFV YLNAQDGERF NNANFATPPD GSPARMRMYI WNQTTPFRDC
     SFEAGVVIHE YTHGLSNRLT GGPANSGCLS MLESGGMGEG WSDFFATAIR LKPSDTRAKD
     YTMGEWISGS EFGIRNYKYS TNLEVNPQVY TDVDQYTRVH PIGNIWASML YEVLWNLIDK
     YGKNDDWLPE FNSAGVPKDG KYLAMKLALD GMALQPCNPT FVSARDAIID ADKALTGGAN
     LCEIWSGFAK RGLGEKAVYS TGGRTNSFDV PAGVCNNSTV SSQARRVKLP LSV