ID   MEP7_ARTOC              Reviewed;         278 AA.
AC   C5FL47;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Extracellular metalloprotease MCYG_03238;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   ORFNames=MCYG_03238;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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}.
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DR   EMBL; DS995703; EEQ30419.1; -; Genomic_DNA.
DR   RefSeq; XP_002847732.1; XM_002847686.1.
DR   AlphaFoldDB; C5FL47; -.
DR   SMR; C5FL47; -.
DR   EnsemblFungi; EEQ30419; EEQ30419; MCYG_03238.
DR   GeneID; 9230494; -.
DR   eggNOG; ENOG502S6EM; Eukaryota.
DR   HOGENOM; CLU_048726_0_0_1; -.
DR   OMA; LYHVFNE; -.
DR   OrthoDB; 1569419at2759; -.
DR   Proteomes; UP000002035; 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; Reference proteome; Secreted; Signal; Virulence; Zinc.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..278
FT                   /note="Extracellular metalloprotease MCYG_03238"
FT                   /id="PRO_0000407216"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         170
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        209..255
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   278 AA;  29932 MW;  51A3245541DAC023 CRC64;
     MRFSIVLSSI AALSSVAAAE RVCGAIPHRT FAKESKAAIE AATAAGLTTK ANITVETYFH
     VITAGSKGEI NNYGPAGIGF KLMDVSRTDN AKWASGGDET GMKKSLRKGG YSALNVYFAP
     NLEGGLLGFC YFPKANPSAN DKLVDGCVIL SGSVPGGEAA PYNEGKTTTH EVGHYMGLYH
     VFNEEQGNCQ KDGDMVADTP VQGTKTSGCP QGKDSCPGQG VDSIHNYMDY SDEYVLLSPV
     YDSWHQTNHR HFSPCMNQFT PGQISRMQMM WQQFRAGK