MEP7_ARTBC
ID MEP7_ARTBC Reviewed; 294 AA.
AC D4ATD1;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Extracellular metalloprotease ARB_07495;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN ORFNames=ARB_07495;
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 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; ABSU01000009; EFE33550.1; -; Genomic_DNA.
DR RefSeq; XP_003014190.1; XM_003014144.1.
DR AlphaFoldDB; D4ATD1; -.
DR SMR; D4ATD1; -.
DR MEROPS; M43.008; -.
DR EnsemblFungi; EFE33550; EFE33550; ARB_07495.
DR GeneID; 9521608; -.
DR KEGG; abe:ARB_07495; -.
DR eggNOG; ENOG502S6EM; Eukaryota.
DR HOGENOM; CLU_048726_0_0_1; -.
DR OMA; LYFQTDL; -.
DR Proteomes; UP000008866; 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..294
FT /note="Extracellular metalloprotease ARB_07495"
FT /id="PRO_0000407214"
FT ACT_SITE 186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 224..250
FT /evidence="ECO:0000250"
SQ SEQUENCE 294 AA; 32042 MW; 2D1E2346FC80438D CRC64;
MRFSVVFAAI AALSSVVTAE RGCGAIPHKG FATELMEAMD NARASSFSNT TAANVTINTY
FHVITDGNKG QINNDTLQKQ IEVLNKDYSG TGFSFKLVGS ERTNNAGWAS GNDDFGMKSS
LRKGGYDSLN VYFVPMLREG LLGFCHFPTK NPGKRQLIMD GCVINSNTVP GGSAQNYDEG
RTTTHEVGHF MGLYHVFNDN GGGCQQDGDM VDDTPVQSKP SSGCPKGKDS CPQQGVDSIH
NYMDYSYDSC LNEFSPGQIQ RMQMLWKQFR AGNSNRSPKA MKPIIPSYVS DPVM