ID   MEP2_PHANO              Reviewed;         637 AA.
AC   Q0V671;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Extracellular metalloproteinase 2;
DE            EC=3.4.24.-;
DE   AltName: Full=Elastinolytic metalloproteinase MEP2;
DE   AltName: Full=Fungalysin MEP2;
DE   Flags: Precursor;
GN   Name=MEP2; ORFNames=SNOG_00493;
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; CH445325; EAT91988.1; -; Genomic_DNA.
DR   RefSeq; XP_001791178.1; XM_001791126.1.
DR   AlphaFoldDB; Q0V671; -.
DR   SMR; Q0V671; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; SNOT_00493; SNOT_00493; SNOG_00493.
DR   GeneID; 5968027; -.
DR   KEGG; pno:SNOG_00493; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   InParanoid; Q0V671; -.
DR   OMA; IRKDSYT; -.
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..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..244
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407162"
FT   CHAIN           245..637
FT                   /note="Extracellular metalloproteinase 2"
FT                   /id="PRO_0000407163"
FT   ACT_SITE        431
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         430
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         434
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        328
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        337
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        413
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   637 AA;  69501 MW;  7A66E34804B282D3 CRC64;
     MRSFLLASLA SVATLKSAQA HPAHSTRGLS KRGIDLDSYR LKQPVSYTNA NDVGSDASIS
     SLTRRATAEE TASELVKKVV PGATFRVADN YVGSNGVAHV YFKQTANGLD VDNGDFNVNV
     GRDGTVFSFG NSFYTGDIPT APSKSKRDTI EPAAAFKSAV SVLDLPVSAG SATSEPKEAE
     NTFAIKQSEG TVSEPEARLV YVQTNGKLAL TWRVETDVLS NWLLTYVDAI DGSQVHAVVD
     YSADASYQVY PWGINDPTEG ERTIVVDPFD KQASEFGWHS DGSKTYDTTR GNNGVAQNNW
     ANKSASEYLN LPRPVSTDLK FHYPYSLNET DFQKYSNASV TQLFYTSNVY HDLLHKLGFN
     EQAGNFEINN NGAGGAGNDF VFLNAQDGSD FNNANFATPP DGQAARMRMY MWNGTTPFRD
     CSFDASVIIH EYTHGLSNRL TGGPANSNCL NVLESGGMGE GWSDFYAIAT HLKAGDTRET
     DYPMAPWVSG KPNGIRNYLY STDINVNPQT YIYVDPQTRV HPIGNIWAGM LYEVLWNLID
     KHGKNDAGTP DFDSNGLPTD GKYLAMKIVM EGMALQPCNP NFVSARDAIV DADKILTGGD
     NKCEIWKGFA KRGLGKDAKY DRVARTESYD LPEGVCA