ID   MEP7_ARTGP              Reviewed;         293 AA.
AC   E5QZI4;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Extracellular metalloprotease MGYG_00389;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   ORFNames=MGYG_00389;
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893;
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; DS989822; EFQ97350.1; -; Genomic_DNA.
DR   RefSeq; XP_003176302.1; XM_003176254.1.
DR   AlphaFoldDB; E5QZI4; -.
DR   SMR; E5QZI4; -.
DR   MEROPS; M43.008; -.
DR   EnsemblFungi; EFQ97350; EFQ97350; MGYG_00389.
DR   GeneID; 10031619; -.
DR   eggNOG; ENOG502S6EM; Eukaryota.
DR   HOGENOM; CLU_048726_0_0_1; -.
DR   InParanoid; E5QZI4; -.
DR   OMA; LYHVFNE; -.
DR   OrthoDB; 1569419at2759; -.
DR   Proteomes; UP000002669; 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..293
FT                   /note="Extracellular metalloprotease MGYG_00389"
FT                   /id="PRO_0000407215"
FT   REGION          270..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        185
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         188
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        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        223..249
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   293 AA;  32021 MW;  62ED919251A8E3FF CRC64;
     MRFSVFLPAI AALSSAVAAQ RSCGSIPHKA FSNELKEAME NSRTSSFSNV TSNVTINTYF
     HVITDGNTGK ISDETLQKQI AVLNSDYKAS GFSFKLVASD SVDNPTWAAG EDDMGMKSAL
     RKGGYDTLNV YFVPMLREGL LGFCYFPMKN PSEGQKIKDG CVINSNSVPG GSAQNYNEGK
     TTTHEVGHFM GLYHVFNEQE GNCQQDGDMI EDTPVQGSAS SGCPTGKDSC PQQGVDSIHN
     YMDYSYDSCL TEFSPGQIKR MQMLWQFRAG SGSGSVTRPR PKPPVLMDYE HRL