ID   MEP_LEPMJ               Reviewed;         635 AA.
AC   E4ZJL4;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 40.
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=Lema_P068070.1;
OS   Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS   (Blackleg fungus) (Phoma lingam).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC   Leptosphaeria; Leptosphaeria maculans species complex.
OX   NCBI_TaxID=985895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8;
RX   PubMed=21326234; DOI=10.1038/ncomms1189;
RA   Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA   Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA   Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA   Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA   Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA   Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA   Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA   Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT   "Effector diversification within compartments of the Leptosphaeria maculans
RT   genome affected by Repeat-Induced Point mutations.";
RL   Nat. Commun. 2:202-202(2011).
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; FP929072; CBX91299.1; -; Genomic_DNA.
DR   RefSeq; XP_003834664.1; XM_003834616.1.
DR   AlphaFoldDB; E4ZJL4; -.
DR   SMR; E4ZJL4; -.
DR   STRING; 985895.E4ZJL4; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; CBX91299; CBX91299; LEMA_P068070.1.
DR   GeneID; 13287951; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   InParanoid; E4ZJL4; -.
DR   OMA; IRKDSYT; -.
DR   OrthoDB; 1136823at2759; -.
DR   Proteomes; UP000002668; Genome.
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_0000407183"
FT   CHAIN           245..635
FT                   /note="Extracellular metalloproteinase MEP"
FT                   /id="PRO_0000407184"
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        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   635 AA;  69222 MW;  FF40CD3D652A4480 CRC64;
     MRAFLLASLA SLPAVNVYAH PTHNSRGLTR RAVDLDAFRP KVPTSYTNAT AVQADPEIPT
     LARRADPEQV ASELVAKILP DAQFRLVSDH YVGTNGVAHF YYKQTVHGLD VDSGDFNVNI
     GKDGNVFSFG NSFYKGKLPA APTLKRDTEA AANALRSAVN VLSLPMSAES ATAVPKEGSD
     AFTITQTSGA VKEPEARLVY VQDASGNLKL AWRVETDIQS NWLLTYVDAE DGSQVHAVVD
     YAAEATYEVY PWGISDPTEG ERVVLTDPFD RQASEFGWHS DGTTEFNTTR GNNGLAHTNW
     ENLSSGYLNF PRPSSADLKF EYPYSLEETD YKAYANASIT QLYYTSNAYH DLLHTLGFNE
     RAGNFEINNN GAGGRGGDLV YLNTQDGGGV NNANFLTPPD GQPPRMRMFI WTKTSPSRDS
     SFDAGVVIHE YTHGLSSRLT GGPANAGCLS SIESGGMGEG WSDFYATAIR LKPADTRATD
     YPMGAWIEGD SRGIRNFLYS TSMETNPQVY TNVDQYIRVH PIGNIWASML YEVLWNLIDK
     HGKNDAAKPD FDANGVPTDG KYLTMKLVLD GMALQPCNPT FVSARDAIID ADKALTGGSN
     ACEIWRGFAK RGLGAGARYD PTTRTDSFEL PEGVC