ID   MEP5_ARTBC              Reviewed;         633 AA.
AC   D4AQG5;
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 5;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP5;
DE   Flags: Precursor;
GN   Name=MEP5; ORFNames=ARB_06472;
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].
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:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR   EMBL; ABSU01000005; EFE34709.1; -; Genomic_DNA.
DR   RefSeq; XP_003015349.1; XM_003015303.1.
DR   AlphaFoldDB; D4AQG5; -.
DR   SMR; D4AQG5; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EFE34709; EFE34709; ARB_06472.
DR   GeneID; 9521073; -.
DR   KEGG; abe:ARB_06472; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   OMA; TSPFTWI; -.
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   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Secreted; Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..244
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397738"
FT   CHAIN           245..633
FT                   /note="Probable extracellular metalloproteinase 5"
FT                   /id="PRO_0000397739"
FT   ACT_SITE        429
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         428
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         432
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        592
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        621
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   633 AA;  69841 MW;  099BCE9E8F452F5D CRC64;
     MHGLLLAAAG LLSLPLHVLA HPQPSTNLAG RGVDLDAYRM ADRSSYMSSD DMKLKQPAIA
     SLSGGNYVDT ATEVVKRMMP GMTFRMVDDH YVGESGISHV YFRQTMHGMD IDNADFNVNI
     GKDGKVLSLG HSFYTGPAPD KAPVEKRDFS DPMQAFHGAC KALNLPINAD KATIQTMNEH
     EVMFMGTSGA MSDPQGKLCY MAKEDGTLAL TWRVETDMGD NWLLSYVDAK ETDKVHNVVD
     YVSHATYQVY KWPIPDPTEG KREIVQNPWN LKTSPFTWIS DGKTNYTTTR GNNAIAQANF
     DGGEDYLNNY RPDSKNLKFE YPYAPNMSPP KSYIDASVTQ LFYSANMVHD LYYMLGFTEK
     AGNFQVNNRG QGGKGNDFVI LNAQDGSGTN NANFATPPDG KPGRMRVYIW TKAKPSRDSS
     FEAGTVIHEY THGLSNRLCG GPANAGCLNG MESGGMGEGW GDFFATAIRL KPNDNRNSNY
     VHGEWVNNSP KGNRLYPYST NLQTNPLVYT SCNKYNEVHA IGTVWCSILY EVLWNLIDKH
     GKNDGPTPVF ENGVPNDGKY LALKLVLDGM AIQPCKPTFV QARDAIIDAD MNLTKGSNKC
     ELWKAFAKRG LGVGAKYDPK NRTGSKAVPK ECQ