ID   MEP3_ARTOC              Reviewed;         633 AA.
AC   C5FNU8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Extracellular metalloproteinase 3;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP3;
DE   Flags: Precursor;
GN   Name=MEP3; ORFNames=MCYG_04620;
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 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.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR   EMBL; DS995704; EEQ31801.1; -; Genomic_DNA.
DR   RefSeq; XP_002846883.1; XM_002846837.1.
DR   AlphaFoldDB; C5FNU8; -.
DR   SMR; C5FNU8; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EEQ31801; EEQ31801; MCYG_04620.
DR   GeneID; 9229998; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   OMA; IRKDSYT; -.
DR   OrthoDB; 1136823at2759; -.
DR   Proteomes; UP000002035; 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   Reference proteome; Secreted; Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..246
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000384081"
FT   CHAIN           247..633
FT                   /note="Extracellular metalloproteinase 3"
FT                   /id="PRO_0000384082"
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"
SQ   SEQUENCE   633 AA;  69377 MW;  DB61E74102A5030C CRC64;
     MHGLLLAGLL ALPMNVLAHP AEQQTSSVLS RRGVDIDSFR LPLKAKYMDS DATAQKIQAL
     SFSKEDDYVS TATKLVKSTF PKSTFRVVDD HYIGTNGIGH VHFKQTAHGL DIDNSDFNVN
     IDRDGKVFSF GNSFFTGEIP KESPMVKREF SDPVKALKGA VKALNLPVKS ENAKAKTVEG
     KESFEFQGTS GALSAPKAKL VYLQKEDGSL ALTWKVETDV GDNWLLSYVD AHDSETVHNV
     VDYVASAEFK VFAWGLNDPT EGNPTSFRDP WTASSPFTWH SDGTNKYPTT RGNNAIAQDN
     PTGGSTYLNN YRPQSANLIF NYPWTAAMTP PSSYKDFSIT QLFYTTNRYH DLLYSFGFNE
     AAGNFQVNNN NKGGKGNDFA IVNAQDGSGT NNANFATPPD GSPGRMRMYN WTTARPNRDG
     CLEAGIVIHE YTHGLSNRLC GGPANSACLN ALESGGMGEG WGDFYATAIR LKPRDTKNTN
     YSMGAWAAND PKGIRAYLYS TNLQTNPYMY TSVNNLREVH GIGTVWATML YELMWGLIEA
     HGGTYSADPV FRNGVPQDGR HLAMKIVMDG MALQPCNPNF VQARDAIIDA DRALTNGANK
     CTIWKAFAKR GLGYGAKYDP RTRTGSNQLP PGC