ID   MEP6_ARTBC              Reviewed;         271 AA.
AC   D4ALW9;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Extracellular metalloprotease ARB_05317;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   ORFNames=ARB_05317;
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 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:0000269|PubMed:21247460}.
CC   -!- SIMILARITY: Belongs to the peptidase M43B family. {ECO:0000305}.
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DR   EMBL; ABSU01000002; EFE36378.1; -; Genomic_DNA.
DR   RefSeq; XP_003017023.1; XM_003016977.1.
DR   AlphaFoldDB; D4ALW9; -.
DR   SMR; D4ALW9; -.
DR   STRING; 663331.D4ALW9; -.
DR   EnsemblFungi; EFE36378; EFE36378; ARB_05317.
DR   GeneID; 9526744; -.
DR   KEGG; abe:ARB_05317; -.
DR   eggNOG; ENOG502RYKG; Eukaryota.
DR   HOGENOM; CLU_048726_0_0_1; -.
DR   OMA; MTMNYMD; -.
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   1: Evidence at protein level;
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..271
FT                   /note="Extracellular metalloprotease ARB_05317"
FT                   /id="PRO_0000407210"
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        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        222..248
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   271 AA;  28942 MW;  75E49684957046F5 CRC64;
     MRFSVLLTGL AAAGSIATAE RTCGAVPPRA YEKEFTEALN SLSPEAASAD LTAGITIDTY
     LHVLTSGQTG NIPDSQLQAQ INAMNQHYSQ AGVQFKLVKA TRTDNANWAS GRDEAGMKKA
     LHMGTYSSLN IYFIPNLSSG LLGICYFPRA NPSQTTIIMD GCMVRSGTVP GGETTNYNQG
     KTATHEVGHF LGLYHVFSEN GSCVDADMVA DTPAQSKKTS GCPSSQDSCP GGGVDSIHNY
     MDYSYDVCMN QFTPGQANRI AQSWRAFRAG H