ID   MEP3_TRIVH              Reviewed;         633 AA.
AC   D4DHN5;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Probable extracellular metalloproteinase 3;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP3;
DE   Flags: Precursor;
GN   Name=MEP3; ORFNames=TRV_06691;
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; ACYE01000382; EFE38642.1; -; Genomic_DNA.
DR   RefSeq; XP_003019287.1; XM_003019241.1.
DR   AlphaFoldDB; D4DHN5; -.
DR   SMR; D4DHN5; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EFE38642; EFE38642; TRV_06691.
DR   GeneID; 9577609; -.
DR   KEGG; tve:TRV_06691; -.
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..246
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397732"
FT   CHAIN           247..633
FT                   /note="Probable extracellular metalloproteinase 3"
FT                   /id="PRO_0000397733"
FT   ACT_SITE        430
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   BINDING         433
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        410
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        480
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        622
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   633 AA;  69246 MW;  E327FD3F1BD6287D CRC64;
     MHGLLLAGLL ALPMNVLAHP AEQHASNVLS RRGVDIESFR LPLKAKYMDS DATAQKIQAM
     SFSKDDDYVS TATKLVKSTF PKSTFRVVDD HYIGTNGIGH VHFKQTAHGL DIDNSDFNVN
     IGRDGKVFSF GNSFFTGEIP KENPMVKRAF SDPVKALKGA VKALNLPVKS DNAKAKTAAG
     KEAFEFMGTT GALSAPKANL VYLQKEDGSL ALTWKVETDV GDNWLLTYVD AHNSETVHNV
     VDYVASAEYK VFAWGLNDPT EGNPTSIRDP WTDASPYTWN SDGMTKYPTT RGNNAIAQDN
     PTGGSTYINN YRPQSPNLIF SYPWSPTATP PSSYKDFSIT QLFYTTNRYH DLLYSFGFNE
     AAGNFQVNNG NKGGRGNDFA IVNAQDGSGT NNANFATPPD GSPGRMRMYN WTTARPNRDG
     CLEAGIVIHE YTHGLSNRLC GGPANSACLN ALESGGMGEG WGDFYATAIR LKPRDTKDTN
     YSMGAWAANN PKGIRAYLYS TNLQTNPYMY TSVNSLREVH QIGTVWASML YDLMWALIEA
     HGGTYSADPV FRNGVPQDGR HLSMKLVMDG MALQPCNPNF VQARDAILDA DRALTNSANK
     CTIWKAFAKR GLGYGAKYDA RNRTGSNKLP PGC