ID   MEP5_TRITO              Reviewed;         608 AA.
AC   A5YCB9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Extracellular metalloproteinase 5;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP5;
DE   Flags: Precursor;
GN   Name=MEP5;
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].
RX   PubMed=17442802; DOI=10.1128/jcm.02610-06;
RA   Abdel-Rahman S.M., Preuett B.L., Gaedigk A.;
RT   "Multilocus genotyping identifies infections by multiple strains of
RT   Trichophyton tonsurans.";
RL   J. Clin. Microbiol. 45:1949-1953(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABQ96590.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; EF490686; ABQ96590.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A5YCB9; -.
DR   SMR; A5YCB9; -.
DR   MEROPS; M36.001; -.
DR   VEuPathDB; FungiDB:TESG_03496; -.
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..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..244
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380880"
FT   CHAIN           245..608
FT                   /note="Extracellular metalloproteinase 5"
FT                   /id="PRO_0000380881"
FT   ACT_SITE        428
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         427
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         431
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        285
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        591
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   608 AA;  67308 MW;  7714D05CF449494A CRC64;
     MHGLLLAAAG LLSLPLHVIA HPQPSTNLAG RGVDLDAYRM ADRSSYMNSD DMKLKQPGIA
     SLSGGNYVDT ATEVVKRMVP GMTFRMVDDH YVGESGISHV YFRQTMHGMD IDNSDFNVNI
     GKDGKVLSFG HSFYTGPAPD KAPVEKRDFS DPMKAFHGAC KALNLPINAD KATVQTMNEH
     EVMFMGTSGA MSDPQGKLCY MAKEDGTLAL TWRVETDMGD NWLLSYVDAK ETEKVHNVVD
     YVSHATYQVY RWPIPDPTEG KRETIENPWN LKTSPFTWIS DGKTNYTTTR GNNAIAQANF
     DGGEDYLNNH RPNNKNLKFE YPYAPNMSPK SYIDASVTQL FYSANMVHDL YYMLGFTEKA
     GNFQVNNHGQ GGKGNDFVIL NAQDGSGTNN ANFATPPDGK PGRMRVYIWT KAKPARDSSF
     EAGTVIHEYT HGLSNRLTGG PANAGCLNGM ESGGMGEGWG DFFATAIRLK PNDNRNANYV
     HGEWVNNSPK GNRMYPYSTS LQTNPLVYTS CNKYNEVHAI GTVWGSMLYE VLWNLIDKHG
     KNDGPTPVFE NGVPKDGKYL AMKLVMDGMA IQPCKPTFVQ ARDAIIDADM NLTKGSNRCE
     IWKAFAKR