ID   MEP1_TRIVH              Reviewed;         635 AA.
AC   D4D4Z2;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Probable extracellular metalloproteinase 1;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP1;
DE   Flags: Precursor;
GN   Name=MEP1; ORFNames=TRV_02160;
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
CC   -!- FUNCTION: Secreted metalloproteinase probably acting as a virulence
CC       factor. {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   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFE43079.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; ACYE01000116; EFE43079.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003023697.1; XM_003023651.1.
DR   AlphaFoldDB; D4D4Z2; -.
DR   SMR; D4D4Z2; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EFE43079; EFE43079; TRV_02160.
DR   GeneID; 9582244; -.
DR   KEGG; tve:TRV_02160; -.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   Proteomes; UP000008383; 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   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Secreted; Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..246
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397724"
FT   CHAIN           247..635
FT                   /note="Probable extracellular metalloproteinase 1"
FT                   /id="PRO_0000397725"
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        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        475
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        594
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        623
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   635 AA;  70069 MW;  8339BFA134DBBE74 CRC64;
     MHGLLLAAGL LSLPLHVLAH PQPSTSTSLA GRAGAVDLNE FRIAHRSSYT SHDEMKKLPS
     IASFRQGTYL EVATELVKQT IPNMEFRLVD DHYVGDSGIG HVRFRQTMHG IDIDNSDFNV
     NVGKDGKVLS HGNSFYTGPA PSSNPMVKRD FIDPMQALHG VRKALNLPIK ADGAHVEDMS
     EHKVMFKGTS GALSDPTAKL CYMAKEDGSL ALTWRVETDI GDNWLLSYMD AKESSKVHNV
     VDYVAHATFQ VYKWGLADPT EGKREILTNP WNLKTSPLTW LSDGQNNFTA TRGNNAIAQY
     NPDGGNDYEN NYRPSPKNLK FEYPYSPDMN PPKTYIDASV TELFYTSNVC HDLYYMLGFN
     EKAGNFQVNN RGQGGKGNDF VILNAQDGSG TNNANFATPP DGQPGRMRAY IWTRANPPRD
     ASFEAGTIIH EYTHGLSNRL CGGPANSRCL NAIESGGMGE GWGDFYATAV RLKPNDTRKT
     NYVKGGWVNN SPKGVRMYPY STDMNVNPLV YTSNNKLNEV HAIGTVWCTM LYEVLWNLID
     KHGKNDGPVP IFENGVPNDG KYLAMKIVMD GMAIQPCNPN FVQARDAILD ADMNLTKGAN
     KCEIWKGFAK RGLGVGAKFD PKNRTGSTQV PNECK