ID   MEP5_ARTGP              Reviewed;         642 AA.
AC   E4UVK2;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Extracellular metalloproteinase 5;
DE            EC=3.4.24.-;
DE   AltName: Full=Elastinolytic metalloproteinase MEP5;
DE   AltName: Full=Fungalysin MEP5;
DE   Flags: Precursor;
GN   Name=MEP5; ORFNames=MGYG_05327;
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}.
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; DS989825; EFR02329.1; -; Genomic_DNA.
DR   RefSeq; XP_003172740.1; XM_003172692.1.
DR   AlphaFoldDB; E4UVK2; -.
DR   SMR; E4UVK2; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EFR02329; EFR02329; MGYG_05327.
DR   GeneID; 10028016; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   InParanoid; E4UVK2; -.
DR   OMA; YIWTRAN; -.
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..246
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407168"
FT   CHAIN           247..642
FT                   /note="Extracellular metalloproteinase 5"
FT                   /id="PRO_0000407169"
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        595
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        624
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   642 AA;  71000 MW;  19BEF02E5EC8DD64 CRC64;
     MHGLLLAAGL LSLPLHVLAH PQPSTTTSLA GRAGTVDLNE FRMAHRSSYT GNDEMMKQPS
     IASFRQGTYL EVATELVKQT MPNMEFRLVD DHYVGDSGIG HVRFRQTMHG IDIDNSDFNV
     NIGKDGKVLS HGNSFYTGPA PSSNPMVKRD FMDPMQALHG VRKALKLPIK ADGATVQDMS
     EHKVMFKGTS GALSDPTAKL CYMAKEDGSL ALTWRVETDI GDNWLLSYMD AKESAKVHNV
     VDYVAHATFQ VYKWGLADPT EGNREILNNP WNLKTSPLTW LADGQNNFTA TRGNNAIAQY
     NPDGGNDYEN NYRPSPKNLK FEYPYSANMD PPKTYIDASV TQLFYTSNVC HDLYYMLGFT
     EKAGNFQVNN RGQGGKGGDY VILNAQDGSG TNNANFATPP DGQPGRMRAY IWTRANPPRD
     ASFEAGTVIH EYTHGLSNRL CGGPANSRCL NAIESGGMGE GWGDFYATAI RLKPKDTRKT
     NYVKGGWVNN SPKGVRMYPY STDMSVNPLV YTSNNKLNEV HAIGTVWCSM LYEVLWNLID
     KHGKNDGPVP VFENGVPKDG KYLAMKIVMD AWPCIQPCNP NFVQARDAIL DADKNLTKGA
     NKCEIWKGFA KRGLGVGAKY DPKNRTGSNE VPKEYKYSAH ME