ID   MEP4_TRIVH              Reviewed;         643 AA.
AC   D4CZ44;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Probable extracellular metalloproteinase 4;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP4;
DE   Flags: Precursor;
GN   Name=MEP4; ORFNames=TRV_00081;
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; ACYE01000003; EFE45143.1; -; Genomic_DNA.
DR   RefSeq; XP_003025754.1; XM_003025708.1.
DR   AlphaFoldDB; D4CZ44; -.
DR   SMR; D4CZ44; -.
DR   MEROPS; M36.001; -.
DR   PRIDE; D4CZ44; -.
DR   EnsemblFungi; EFE45143; EFE45143; TRV_00081.
DR   GeneID; 9581985; -.
DR   KEGG; tve:TRV_00081; -.
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..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..254
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397736"
FT   CHAIN           255..643
FT                   /note="Probable extracellular metalloproteinase 4"
FT                   /id="PRO_0000397737"
FT   REGION          49..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        438
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         437
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         441
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        420
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        603
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        629
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   643 AA;  70693 MW;  FD4E9E5E8EAC0F91 CRC64;
     MHGLLLAGLL ALPLNVFAHP TESHSSGVSR RAIDITSYRL PQISKYTKSD AVPKQDGESF
     TTSSTGDDNV SSGDYVTTAT NWLKKTLPKA TYRLVNDHYI GDSGIGHVHF RQTAHGIDID
     NTDFNVNIGR DGKVFSFGNS FYDGEIPKAN PMVKRDFSDP VNALHGAIQT LNLPVTAKPE
     NVKAKPVEGK ENFKFEGTSG ALSDPKAQLV YLQKDGGLVL SWKVETDVGD NWLLTYVDAN
     KNDQVHSVVD YVSAAEYQVY PWGINDPTEG NRTTIHLPWL KTLSTDWHID GKGWYPTTRG
     NNAIAQENPT GHPEYENNYR PKSPLFIFKY PYSPAMTPPS SYRDASITQL FYTTNVYHDV
     LYILGFNEKA GNFQINNWNK GGVGGDFAIL NSQDGSGVNN ANFATPPDGQ PGRMRMYTWN
     ASTPERDGCF EAGIVIHEYT HGVSNRLTGG PENSRCLAAL ESGGMGEGWS DFFATAIRLK
     AGDTRATDYT MGEWASNRPN GIRKYRYSTS LTTNPHMYVD ADGLTSVHAI GTIWASMLYE
     LLWNLIDKHG KGDVTKIRPV LKNGVPTDGR HLAMKIVLDG MALQPCLPNF VQARDAILDA
     DKNLTQGSNK CEIWKAFAKR GLGVGAAFNQ TKRTGSNELP AGC