ID   MEP1_ARTGP              Reviewed;         632 AA.
AC   E4UYA3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Extracellular metalloproteinase 1;
DE            EC=3.4.24.-;
DE   AltName: Full=Elastinolytic metalloproteinase MEP1;
DE   AltName: Full=Fungalysin MEP1;
DE   Flags: Precursor;
GN   Name=MEP1; ORFNames=MGYG_05070;
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893;
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 that allows assimilation of
CC       proteinaceous substrates and probably acts as a virulence factor.
CC       {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; DS989825; EFR02066.1; -; Genomic_DNA.
DR   RefSeq; XP_003172477.1; XM_003172429.1.
DR   AlphaFoldDB; E4UYA3; -.
DR   SMR; E4UYA3; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EFR02066; EFR02066; MGYG_05070.
DR   GeneID; 10027747; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   InParanoid; E4UYA3; -.
DR   OMA; FMAIAIN; -.
DR   OrthoDB; 1136823at2759; -.
DR   Proteomes; UP000002669; 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; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..243
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407152"
FT   CHAIN           244..632
FT                   /note="Extracellular metalloproteinase 1"
FT                   /id="PRO_0000407153"
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;  69777 MW;  397C2CB30081AE18 CRC64;
     MHGLLLAAGL LSLPLRVLAH PQPSTSLTSQ GVDLNAYRMA DRSSYMSSDE MKLEQPSISS
     LSGGNYVETA TEVVKRMMPG VTFRMVDDHY VGESGISHVY FRQTMHGMDI DNSDFNVNIG
     KDGKVLSFGN SFYTNPTPDK APVEKRDFSD PMKALHGARK ALNLPINADK ATIKSMNEHE
     VMFMGTSGAL SDPQGKLCYM AKEDGTLALT WRVETDMGDN WLLSYVDAKD TDKVHNVVDY
     VSHATYQVYP WPVPDPTEGK RAVLQNPWNL KASPFTWISD GKNNYSTTRG NNAIAQANFD
     GGSDYLNNYR PNNKNLKFEY PYAPNMSPPK SYIDASVTQL FYSANMVHDL YYMLGFTEKA
     GNFQVNNRNQ GGKGGDFVIL NAQDGSGTNN ANFATPPDGQ PGRMRVYIWT KAKPARDSSF
     EAGTVIHEYT HGLSNRLCGG PANSACLNGM ESGGMGEGWG DFFATAIRLK PNDNRNANYV
     HGEWVNNSPR GNRMFPYSTS LQTNPLVYTS CNKYNEVHAI GTVWCSILYE VLWNLIDKHG
     KNDGPTPVFE NGVPKDGKYL AMKLVLDGMA IQPCKPTFVQ ARNAILDADM NLTKGANKCE
     LWKAFAKRGL GTGAKYDPKN RTGSKAVPKE CQ