ID   MEP1_ARTBC              Reviewed;         635 AA.
AC   D4B1S5;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Probable extracellular metalloproteinase 1;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP1;
DE   Flags: Precursor;
GN   Name=MEP1; ORFNames=ARB_02406;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
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:0000269|PubMed:21247460}.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR   EMBL; ABSU01000027; EFE30707.1; -; Genomic_DNA.
DR   RefSeq; XP_003011347.1; XM_003011301.1.
DR   AlphaFoldDB; D4B1S5; -.
DR   SMR; D4B1S5; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EFE30707; EFE30707; ARB_02406.
DR   GeneID; 9524248; -.
DR   KEGG; abe:ARB_02406; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   OMA; YIWTRAN; -.
DR   Proteomes; UP000008866; 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   1: Evidence at protein level;
KW   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Secreted; Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..246
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397722"
FT   CHAIN           247..635
FT                   /note="Probable extracellular metalloproteinase 1"
FT                   /id="PRO_0000397723"
FT   ACT_SITE        431
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         430
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         434
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        475
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        594
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        623
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   635 AA;  70062 MW;  A1EB896ADF5C780C CRC64;
     MHGLLLAAGL LSLPLHVLAH PQPSTSTSLA GRAGAVDLNE FRVAHRSSYT SHDEMKKLPS
     IASFRQGTYL EVATELVKQT MPNMEFRLVD DHYVGDSGIG HVRFRQTMHG IDIDNSDFNV
     NVGKDGKVLS HGNSFYTGPA PSSNPMVKRD FIDPMQALHG VRKALNLPIK ADGAHVEDMS
     EHKVMFKGTS GALSDPTAKL CYMAKEDGSL ALTWRVETDI GDNWLLSYMD AKESSKVHNV
     VDYVAHATFQ VYKWGLADPT EGKREILTNP WNLKTSPLTW LSDGQNNYTA TRGNNAIAQY
     NPDGGSDYEN NYRPSPKNLK FEYPYSPDMN PPKTYIDASV TELFYTSNVC HDLYYMLGFN
     EKAGNFQVNN RGQGGKGNDF VILNAQDGSG TNNANFATPP DGQPGRMRAY IWTRANPPRD
     ASFEAGTIIH EYTHGLSNRL CGGPANSRCL NAIESGGMGE GWGDFYATAV RLKPNDTRKT
     NYVKGGWVNN SPKGVRMYPY STDMNVNPLV YTSNNKLNEV HAIGTVWCTM LYEVLWNLID
     KHGKNDGPVP IFENGVPNDG KYLAMKIVMD GMAIQPCNPN FVQARDAILD ADMNLTKGAN
     KCEIWKGFAK RGLGVGAKFD PKNRTGSTQV PNECK