ID   MEP2_TRITO              Reviewed;         632 AA.
AC   B6V873;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Extracellular metalloproteinase 2;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP2;
DE   Flags: Precursor;
GN   Name=MEP2;
OS   Trichophyton tonsurans (Scalp ringworm fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=34387;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Preuett B.L., Abdel-Rahman S.M.;
RT   "Comparing putative pathogenicity factors between Trichophyton tonsurans
RT   and Trichophyton equinum.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; FJ267696; ACJ06664.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6V873; -.
DR   SMR; B6V873; -.
DR   MEROPS; M36.001; -.
DR   VEuPathDB; FungiDB:TESG_06485; -.
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   Secreted; Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..244
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380846"
FT   CHAIN           245..632
FT                   /note="Extracellular metalloproteinase 2"
FT                   /id="PRO_0000380847"
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;  69760 MW;  815455284559320E CRC64;
     MHGLLLAGLA AALPLGVAGL PARQQSGLSP RGIDINPYRF ASMAKYSEHK ATSQMVHSFS
     YSKDDDYVAT ATKLVKSTFP NMTFRTVKDH YIGTNGIGHV HFKQTAHGID IDNADFNVNI
     GRDGKVFTFG NSFYEGEMPK TNPLTKRDFA DPVKALHGAI KTLKLPVKPQ SAKAMPMKEA
     ETFMFEGTSG ALSEPMAKLV YIQKDGKLHL TWRVETDVGD NWLLSYVDSK ETETVHNVVD
     YVASADYKVF AWGLNDPTEG QPTMIKDPWN TTGSGSPFTW HGDGEMDYTV TRGNNIAAQD
     NPSGGGQWEN NYRPESPELS FVYEYNEQME PEQYKDFAIT QLFYTTNTFH DLLYSFGFTE
     EAGNFQMNNN GKGGEGNDFA ICNAQDGSGT NNANFATPPD GQNGRMRMYT WTTAQPSRDG
     DLEAGIVIHE YAHGLSNRLC GGPANSNCLS ELEAGGMGEG WGDFYATAIR LKQDDTRETD
     YTMGEWAANM EGGIREYPYS TNMQTNPYTY ADVEGMSEVH GIGTVWATIL YDVLWNLIDE
     HGMSKNIMPK FVNGAPSDGR NLAMKLVLDG MTLMPCNPNF VQARDAIIDA DQALTNGQNK
     CALMKAFSKR GLGSNYKHGK NRVNNFDMPA DC