ID   MEP1_TRIEQ              Reviewed;         615 AA.
AC   A7UKV9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Extracellular metalloproteinase 1;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP1;
DE   Flags: Precursor; Fragment;
GN   Name=MEP1;
OS   Trichophyton equinum (Horse ringworm fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=63418;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Brown J.T., Preuett B.L., Abdel-Rahman S.M.;
RT   "Comparing putative pathogenicity factors between Trichophyton tonsurans
RT   and Trichophyton equinum.";
RL   Submitted (AUG-2007) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EU076574; ABU50384.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7UKV9; -.
DR   SMR; A7UKV9; -.
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..8
FT                   /evidence="ECO:0000255"
FT   PROPEP          9..235
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000380834"
FT   CHAIN           236..>615
FT                   /note="Extracellular metalloproteinase 1"
FT                   /id="PRO_0000380835"
FT   ACT_SITE        420
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         419
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         423
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        276
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        464
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        583
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        612
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT   NON_TER         615
SQ   SEQUENCE   615 AA;  67897 MW;  5E78A7D36A769192 CRC64;
     SLPLHVLAHP QPSTSTSLAG RAGAVDLNEF RVAHRSSYAS HDEMKKLPSI ASFRQGTYLE
     VATELVKQTM PNMEFRLVDD HYVGDSGIGH VRFRQTMHGI DIDNSDFNVN VGKDGKILSH
     GNSFYTGPAP ASNPMIKRDF IDPMQALNGV RKALNLPVKA DGAHVENMSE HKVMFKGTSG
     ALSDPTAKLC YMAKEDGSLA LTWRVETDIG DNWLLSYMDA KESSKVHNVV DYVAHATFQV
     YKWGLADPTE GKRDILTNPW NLKTSPLTWL ADGKTNFTAT RGNNAIAQYN PDGGNDYENN
     YRPSPKNLKF EYPYSPDMNP PKTYIDASVT QLFYTSNVCH DLYYMLGFNE KAGNFQVNNR
     GQGGKGNDYV ILNAQDGSGT NNANFATPPD GQPGRMRAYI WTRANPPRDA SFEAGTIIHE
     YTHGLSNRLC GGPANSRCLN ALESGGMGEG WGDFYATAVR LKPNDTRKTN YVKGGWVNNS
     PKGVRMYPYS TDMNVNPLVY TSNNKLNEVH AIGTVWCTML YEVLWNLIDK HGKNDGPVPV
     FENGVPNDGK YLAMKLVMDG MAIQPCNPNF VQARDAILDA DMNLTKGANK CEIWKGFAKR
     GLGVGAKFDP KNRTG