ID   MEP4_ARTBC              Reviewed;         643 AA.
AC   D4AX35;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Probable extracellular metalloproteinase 4;
DE            EC=3.4.24.-;
DE   AltName: Full=Fungalysin MEP4;
DE   Flags: Precursor;
GN   Name=MEP4; ORFNames=ARB_00762;
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; ABSU01000016; EFE32240.1; -; Genomic_DNA.
DR   RefSeq; XP_003012880.1; XM_003012834.1.
DR   AlphaFoldDB; D4AX35; -.
DR   SMR; D4AX35; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EFE32240; EFE32240; ARB_00762.
DR   GeneID; 9522958; -.
DR   KEGG; abe:ARB_00762; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   OMA; STDWHID; -.
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..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..254
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397734"
FT   CHAIN           255..643
FT                   /note="Probable extracellular metalloproteinase 4"
FT                   /id="PRO_0000397735"
FT   REGION          47..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        438
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         437
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         441
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        420
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        603
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        629
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   643 AA;  70687 MW;  2641F0074F1FA681 CRC64;
     MHGLLLAGLL ALPLNVLAHP TESHSSGVSR RAIDITSYRL PQISKYTKSD AVPKQDGESF
     TTSSTGDDNV SSGDYVTTAT NWLKKTLPKA TYRLVNDHYI GDSGIGHVHF RQTAHGIDID
     NTDFNVNIGR DGKVFSFGNS FYDGEIPKAN PMVKRDFSDP VNALHGAIQT LNLPVTAKPE
     NVKAKPVEGK ENFKFEGTSG ALSDPKAQLV YLQKDGGLVL SWKVETDVGD NWLLTYVDAN
     KNDQVHSVVD YVSAAEYQVY PWGINDPTEG NRTSIHLPWL KTLSTDWHID GKGWYPTTRG
     NNAIAQENPT GHPEYENNYR PKSPLFIFKY PYSLAMTPPS SYRDASITQL FYTTNVYHDV
     LYILGFNEKA GNFQINNWNK GGVGGDFAIL NSQDGSGVNN ANFATPPDGQ PGRMRMYTWN
     ASTPERDGCF EAGIVIHEYT HGVSNRLTGG PENSRCLAAL ESGGMGEGWS DFFATAIRLK
     PGDTRATDYT MGEWASNRPN GIRKYRYSTS LTTNPHMYVD ADGLTSVHAI GTIWASMLYE
     LLWNLIDKHG KGDVTKIRPV LKNGVPTDGR HLAMKIVLDG MALQPCLPNF VQARDAILDA
     DKNLTQGSNK CEIWKAFAKR GLGVGAAFNQ TKRTGSNELP AGC