ID   MEP5_TRIVH              Reviewed;         633 AA.
AC   D4DIT1;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Probable extracellular metalloproteinase 5;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP5;
DE   Flags: Precursor;
GN   Name=MEP5; ORFNames=TRV_07092;
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}.
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DR   EMBL; ACYE01000412; EFE38255.1; -; Genomic_DNA.
DR   RefSeq; XP_003018900.1; XM_003018854.1.
DR   AlphaFoldDB; D4DIT1; -.
DR   SMR; D4DIT1; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EFE38255; EFE38255; TRV_07092.
DR   GeneID; 9580072; -.
DR   KEGG; tve:TRV_07092; -.
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..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..244
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397740"
FT   CHAIN           245..633
FT                   /note="Probable extracellular metalloproteinase 5"
FT                   /id="PRO_0000397741"
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        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        592
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        621
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   633 AA;  69756 MW;  4E7DDF2002687C1E CRC64;
     MHGLLLAAAG LLSLPLHVLA HPQPSTNLAG RGVDLDAYRM ADRSSYMSSD DMKLKQPAIA
     SLSGGNYVDT ATEVVKRMMP GMTFRMVDDH YVGESGISHV YFRQTMHGMD IDNADFNVNI
     GKDGKVLSVG HSFYTGPAPD KAPVEKRDFS DPMQAFHGAC KALNLSINSD KATIQTMNEH
     EVMFMGTSGA MSDPQGKLCY MAKEDGTLAL TWRVETDMGD NWLLSYVDAK ETDKVHNVVD
     YVSHATYQVY KWPIPDPTEG KREIVENPWN LKTSPFTWIS DGKTNYTTTR GNNAIAQANF
     DGGEDYLNNY RPDSKNLKFE YPYAPNMSPP KSYIDASVTQ LFYSANMVHD LYYMLGFTEK
     AGNFQVNNHG QGGKGNDFVI LNAQDGSGTN NANFATPPDG KPGRMRVYIW TKAKPSRGSS
     FEAGTVIHEY THGLSNRLCG GPANAGCLNG MESGGMGEGW GDFFATAIRL KPNDNRNSNY
     VHGEWVNNSP KGNRLYPYST NLQTNPLVYT SCNKYNEVHA IGTVWCSILY EVLWNLIDKH
     GKNDGPTPVF ENGVPNDGKY LALKLVLDGM AIQPCKPTFV QARDAIIDAD MNLTKGSNKC
     ELWKAFAKRG LGVGAKYDPK NRTGSKAVPK ECQ