ID   MEP7_TRIVH              Reviewed;         294 AA.
AC   D4DIV0;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Extracellular metalloprotease TRV_07111;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   ORFNames=TRV_07111;
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 that allows assimilation of
CC       proteinaceous substrates. Plays a pivotal role as a pathogenicity
CC       determinant during infections and contributes to the ability of the
CC       pathogen to persist within the mammalian host (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M43B family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ACYE01000414; EFE38240.1; -; Genomic_DNA.
DR   RefSeq; XP_003018885.1; XM_003018839.1.
DR   AlphaFoldDB; D4DIV0; -.
DR   SMR; D4DIV0; -.
DR   MEROPS; M43.008; -.
DR   EnsemblFungi; EFE38240; EFE38240; TRV_07111.
DR   GeneID; 9580057; -.
DR   KEGG; tve:TRV_07111; -.
DR   HOGENOM; CLU_048726_0_0_1; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04275; ZnMc_pappalysin_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR008754; Peptidase_M43.
DR   Pfam; PF05572; Peptidase_M43; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Secreted; Signal; Virulence; Zinc.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..294
FT                   /note="Extracellular metalloprotease TRV_07111"
FT                   /id="PRO_0000407217"
FT   ACT_SITE        186
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         185
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         189
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        224..250
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   294 AA;  32042 MW;  2D1E2346FC80438D CRC64;
     MRFSVVFAAI AALSSVVTAE RGCGAIPHKG FATELMEAMD NARASSFSNT TAANVTINTY
     FHVITDGNKG QINNDTLQKQ IEVLNKDYSG TGFSFKLVGS ERTNNAGWAS GNDDFGMKSS
     LRKGGYDSLN VYFVPMLREG LLGFCHFPTK NPGKRQLIMD GCVINSNTVP GGSAQNYDEG
     RTTTHEVGHF MGLYHVFNDN GGGCQQDGDM VDDTPVQSKP SSGCPKGKDS CPQQGVDSIH
     NYMDYSYDSC LNEFSPGQIQ RMQMLWKQFR AGNSNRSPKA MKPIIPSYVS DPVM