ID   MEP5_ARTOT              Reviewed;         632 AA.
AC   Q6WIH7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Extracellular metalloproteinase 5;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP5;
DE   Flags: Precursor;
GN   Name=MEP5;
OS   Arthroderma otae (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=63405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LAU709-03;
RX   PubMed=14766908; DOI=10.1099/mic.0.26690-0;
RA   Jousson O., Lechenne B., Bontems O., Capoccia S., Mignon B., Barblan J.,
RA   Quadroni M., Monod M.;
RT   "Multiplication of an ancestral gene encoding secreted fungalysin preceded
RT   species differentiation in the dermatophytes Trichophyton and
RT   Microsporum.";
RL   Microbiology 150:301-310(2004).
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; AY283570; AAQ21095.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6WIH7; -.
DR   SMR; Q6WIH7; -.
DR   MEROPS; M36.001; -.
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_0000380876"
FT   CHAIN           245..632
FT                   /note="Extracellular metalloproteinase 5"
FT                   /id="PRO_0000380877"
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        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        591
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        620
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   632 AA;  69546 MW;  E39A4963B743DEDB CRC64;
     MHGLLLAAGL LSLPLHVLAH PQPGTSLAGR AVDLNAYRMA DRASYMSSDE MQAQQPHIAS
     VSAGGYVETA TEVVKRVMPG MTFRLVDDHY VGVSGISHVY FRQTMHGMDI DNSDFNVNIG
     KDGKVLSYGN SFYTGPAPDK APMVKRDFSD PMQALHGVRK ALNLPITADK ATVKTVNEHE
     VTFMGTTGAL SDPSAKLCYM AKEDGSLALT WRVETDMGDN WLLSYVDAKS TDQVHNVVDY
     VSHATYQVYR WPIPDPTEGK REILENPWNL RTSPFTWISD GKNNYTTTRG NNAIAQANPD
     GGNEYLNNYR PNNKNLKFEY PYSPNMSPPK TYIDASITQL FYSANMVHDL YYMLGFTEKA
     GNFQVNNRGQ GGKGNDFVIL NAQDGSGTNN ANFATPPDGQ PGRMRVYIWT KAQPARDSSF
     EAGTVIHEYT HGLSNRLCGG PANSACLNGL ESGGMGEGWG DFFATAIRLK PNDNRNANYV
     HGEWVNNSPK GNRLFPYSTS LKTNPLVYTS CNKYNEVHAI GTVWASILYE VLWNLIDKHG
     KNDGPTPVFE NGVPKDGKYL SLKLVLDGMA IQPCKPNFVQ ARNAIIDADK NLTKGANKCE
     LWKAFAKRGL GTGAKYDPKN RTGSTAVPKE CQ