MEP8_ARTGP
ID MEP8_ARTGP Reviewed; 275 AA.
AC E4USP0;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Extracellular metalloprotease MGYG_03559;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN ORFNames=MGYG_03559;
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. Plays a pivotal role as a pathogenicity
CC determinant during infections and contributes to the ability of the
CC pathogen to persist within the mammalian host (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M43B family. {ECO:0000305}.
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DR EMBL; DS989824; EFR00555.1; -; Genomic_DNA.
DR RefSeq; XP_003173385.1; XM_003173337.1.
DR AlphaFoldDB; E4USP0; -.
DR SMR; E4USP0; -.
DR EnsemblFungi; EFR00555; EFR00555; MGYG_03559.
DR GeneID; 10028664; -.
DR eggNOG; ENOG502RYKG; Eukaryota.
DR HOGENOM; CLU_048726_0_0_1; -.
DR InParanoid; E4USP0; -.
DR OMA; HTINTTW; -.
DR OrthoDB; 1569419at2759; -.
DR Proteomes; UP000002669; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04275; ZnMc_pappalysin_like; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR008754; Peptidase_M43.
DR Pfam; PF05572; Peptidase_M43; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Secreted; Signal; Virulence; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..275
FT /note="Extracellular metalloprotease MGYG_03559"
FT /id="PRO_0000407218"
FT ACT_SITE 189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 225..252
FT /evidence="ECO:0000250"
SQ SEQUENCE 275 AA; 29729 MW; 7C5762678476F22D CRC64;
MRFSLSLIGL VASGSLAAAH PSHCGAEPSE DFDILSKDIT DKLAAEASEI HAPIEVTTFF
HVVASSKSVA DGYISDKMLQ DQLAVMNKAY APHGFSFKHG NTTRTINPTW ATGGDELNMK
YALHMGKYAD LNLYFVKKLA DNSHGSCPYP SNPYPGTPGY IKDGCTILSS TVPGGSQSNA
NRGLTTVHEI GHYMGLYHTF QGGCSTELGD RVADTPAQKN GTVGCPSSRD SCPDQAGLDP
IHNYMDTSDD VCRTEFTPKQ AMRMQEMYKE FRAGK