ID   MEP2_ARTOC              Reviewed;         632 AA.
AC   C5FJ19;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Extracellular metalloproteinase 2;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP2;
DE   Flags: Precursor;
GN   Name=MEP2; ORFNames=MCYG_02168;
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR   EMBL; DS995702; EEQ29349.1; -; Genomic_DNA.
DR   RefSeq; XP_002849234.1; XM_002849188.1.
DR   AlphaFoldDB; C5FJ19; -.
DR   SMR; C5FJ19; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EEQ29349; EEQ29349; MCYG_02168.
DR   GeneID; 9223171; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   OMA; NDFAICN; -.
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..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..244
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000384079"
FT   CHAIN           245..632
FT                   /note="Extracellular metalloproteinase 2"
FT                   /id="PRO_0000384080"
FT   REGION          294..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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        270
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   632 AA;  69468 MW;  F2FFC2FF8683D33E CRC64;
     MHGLLLAGLA VALPLGVAGH PARPQTALSP RGIDVNAYRF TSTAKYNEHK TTSQMVQSFA
     YSKDDDYVAT ATKLVKSTFP NMTFRTVKDH YIGTNGIGHV HFKQTAHDID IDNADFNVNI
     GRDGKVFTFG NSFYQGEMPK TNPMVKRDYS DPVKALHGAI KTLKIPVKPE SAKAMPMDEV
     ETFKFEGTSG ALSEPKAKLV YIQKDGNLHL TWRVETDVGD NWLLSYVDSK ESETVHNVVD
     YVASADYKVF AFGLNDPTEG QPSMIKDPWN TTGSGSPFTW HGDGKTDYTV TRGNNVAAQD
     NPSGGSQWEN NYRPDSPQLS FVYDYSDQME PEDYKDFAIT QLFYTTNTFH DVLYSLGFTE
     EAGNFQVNNG NKGGKGNDFA ICNAQDGSGT NNANFATPPD GQPGRMRMYT WTTSKPKRDG
     DLEAGIVIHE YTHGLSNRLC GGPANSNCLN DLEAGGMGEG WGDFYATAIR LKQGDTHDTD
     YTMGEWAANQ KGGIREYPYS TNMQTNPYTY ADVKGMREVH GIGTVWATIL YDVLWNLIDD
     HGMGKNVMPK MVDGVPTDGR TLAMKLVLDG MTLMPCNPNF MQARDAIIDA DMALTKGANK
     CSLMKAFAKR GLGSNTKPGK GYTNNFDMPS GC