ID   MEP6_TRIVH              Reviewed;         271 AA.
AC   D4DI84;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 2.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Extracellular metalloprotease TRV_06892;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   ORFNames=TRV_06892;
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   -!- SEQUENCE CAUTION:
CC       Sequence=EFE38422.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; ACYE01000399; EFE38422.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003019067.1; XM_003019021.1.
DR   AlphaFoldDB; D4DI84; -.
DR   SMR; D4DI84; -.
DR   EnsemblFungi; EFE38422; EFE38422; TRV_06892.
DR   GeneID; 9582552; -.
DR   KEGG; tve:TRV_06892; -.
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..271
FT                   /note="Extracellular metalloprotease TRV_06892"
FT                   /id="PRO_0000407213"
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        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        222..248
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   271 AA;  28970 MW;  B858DADB5D93DB4E CRC64;
     MRFSVLLTGL AAAGSIATAE RTCGAVPPRA YEKEFTEALN SLSPEAASAD LTAGITIDTY
     LHVLTSGQTG NIPDSQLQAQ INAMNQHYSQ AGVQFRLVKA TRTDNANWAS GRDEAGMKKA
     LHMGTYSSLN IYFIPNLSSG LLGICYFPRA NPSQTTIIMD GCMVRSGTVP GGETTNYNQG
     KTATHEVGHF LGLYHVFSEN GSCVDADMVA DTPAQSKKTS GCPSSQDSCP GGGVDSIHNY
     MDYSYDVCMN QFTPGQANRI AQSWRAFRAG H