ID   MEP1_PHANO              Reviewed;         626 AA.
AC   Q0UC19;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Extracellular metalloproteinase 1;
DE            EC=3.4.24.-;
DE   AltName: Full=Elastinolytic metalloproteinase MEP1;
DE   AltName: Full=Fungalysin MEP1;
DE   Flags: Precursor;
GN   Name=MEP1; ORFNames=SNOG_10695;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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; CH445341; EAT82089.2; -; Genomic_DNA.
DR   RefSeq; XP_001800956.1; XM_001800904.1.
DR   AlphaFoldDB; Q0UC19; -.
DR   SMR; Q0UC19; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; SNOT_10695; SNOT_10695; SNOG_10695.
DR   GeneID; 5977863; -.
DR   KEGG; pno:SNOG_10695; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   InParanoid; Q0UC19; -.
DR   OrthoDB; 1136823at2759; -.
DR   Proteomes; UP000001055; 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..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..241
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407156"
FT   CHAIN           242..626
FT                   /note="Extracellular metalloproteinase 1"
FT                   /id="PRO_0000407157"
FT   REGION          606..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..626
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        426
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         425
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
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   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   626 AA;  67217 MW;  2983C6A3F86082FC CRC64;
     MLSSLLAGAG LVALAASHPT SHGNALTRRA VDINAFRLTA TSEYVNATVA VSEPSLRFLK
     RADYLETATE LVKSVAKDAT FRVVEDHYVG SNGIAHVNFK QTANGLDIDN ADFNINVAKD
     GSIFSYGNSF YTGAIPANPL QKRDFSDPVD ALKAANDKLQ LAVTAEKASA ESTGAKETFT
     LKGTSGAVKD PEAKLVYLVK SDGNLALTWR VETDIMSNWL LTYVDAATNQ EIHGVVDYSA
     DATYQVYPWG LNDPTEGSRA VVTNPWDTTA SEFTWQGTGT TTYNVPRGNN AIAQSNTDGG
     SDYLSNYRPT STSQNFSYPY TLQMSPPSTY VDASVTQLFY TANVYHDLLH SLGFNERAGN
     FEVNNNGAGG SGNDMVILNT HDGSDTNNAN FATPPDGQPG RMRMFLWDLS TPNRDSSFEA
     GVVIHEYTHG LSNRLTGGPA NSNCLNALES GGMGEGWGDF MATAIRLKAG DTRAKDYTMG
     SWIANDPKGI RTYPYSTSLT TNPHKYTDVN NLRGVHPIGT VWATMLYEVM WNLIDRYGKN
     DGAKPTFGAN GAPTDGKYLA MKLVVDGMAL PNFVQARDAI LDADVALTGG ANKCDIWKGF
     AKRGLGSGAR YSSTARTGST ALPSGC