ID   MEP_MAGO7               Reviewed;         635 AA.
AC   A4QWP8; G4N487;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Extracellular metalloproteinase MEP;
DE            EC=3.4.24.-;
DE   AltName: Full=Elastinolytic metalloproteinase MEP;
DE   AltName: Full=Fungalysin MEP;
DE   Flags: Precursor;
GN   Name=MEP; ORFNames=MGG_13252;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
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; CM001233; EHA51955.1; -; Genomic_DNA.
DR   RefSeq; XP_003711762.1; XM_003711714.1.
DR   AlphaFoldDB; A4QWP8; -.
DR   SMR; A4QWP8; -.
DR   STRING; 318829.MGG_13252T0; -.
DR   MEROPS; M36.001; -.
DR   PRIDE; A4QWP8; -.
DR   EnsemblFungi; MGG_13252T0; MGG_13252T0; MGG_13252.
DR   GeneID; 5049117; -.
DR   KEGG; mgr:MGG_13252; -.
DR   VEuPathDB; FungiDB:MGG_13252; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   InParanoid; A4QWP8; -.
DR   OMA; WALIEAH; -.
DR   OrthoDB; 1136823at2759; -.
DR   Proteomes; UP000009058; Chromosome 3.
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..242
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407185"
FT   CHAIN           243..635
FT                   /note="Extracellular metalloproteinase MEP"
FT                   /id="PRO_0000407186"
FT   ACT_SITE        429
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         428
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         432
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        473
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   635 AA;  68377 MW;  3F3966CA791BCFEA CRC64;
     MRYSLSLALL GVAAVTVVAH PHTPGRHGVE RRAIDLDAFR LQPTAEYVPK EEVPDQSSLA
     FISNDNYVDV ATDLVKSVAP GIEFRVVGDH YVGTNGVAHV NFKQTAHGID IDNADFNVNV
     RDGKVFSYGN SFFTGKIPEE SPLKKRDFSD PTVALTGATT VLQLPISGEA KAEAKEGTET
     YTLKGTSGAV SDPEARLVYL VRDDSLALTW RVETDIEDNW LLSYVDANNK EQVHGVVDYV
     SHASFQVYPW GTNDPLEAGA ARVTLTDPWD KASSPFGWLS DGTSTYTTTR GNNAIAQSNP
     SGGTAYLNNY RPTNANSIFS YPWTPAMSPP SSFVDFSATQ LFYTANVFHD LLYKLGFTEA
     AGNFQVNNNG KGGLGNDQVI LNTQDGSGTN NANFATPPDG QNGRMRMYIW TYTTPQRDSS
     LEAGVVIHEY THGLSNRLTG GPSNSGCLSA LEAGGMGEGW SDFFATAARI KQNDTADTDY
     PMGEWVAANP KGIRAYPYST SLTRNPQTYA TTNTLSTVHP IGNVWATVLY EVLWALVGKH
     GLQVSTFPTF DASGVPTSGN FLAQKLVLDG MALQPCNPNF VQARDAIIDA DQALTGGANK
     CELWTAFAKR GLGSGAKYAA SKRSVESKTI PAGVC