ID   MEP1_SORMK              Reviewed;         285 AA.
AC   D1ZSU8; F7W7A4;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Extracellular metalloprotease SMAC_06893;
DE            EC=3.4.24.-;
DE   Flags: Precursor;
GN   ORFNames=SMAC_06893;
OS   Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX   NCBI_TaxID=771870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX   PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA   Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K.,
RA   Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S.,
RA   Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.;
RT   "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT   Sordaria macrospora, a model organism for fungal morphogenesis.";
RL   PLoS Genet. 6:E1000891-E1000891(2010).
CC   -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC       proteinaceous substrates. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M43B family. {ECO:0000305}.
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DR   EMBL; CABT02000038; CCC13395.1; -; Genomic_DNA.
DR   RefSeq; XP_003344584.1; XM_003344536.1.
DR   AlphaFoldDB; D1ZSU8; -.
DR   SMR; D1ZSU8; -.
DR   MEROPS; M43.008; -.
DR   EnsemblFungi; CCC13395; CCC13395; SMAC_06893.
DR   GeneID; 10801885; -.
DR   KEGG; smp:SMAC_06893; -.
DR   VEuPathDB; FungiDB:SMAC_06893; -.
DR   eggNOG; ENOG502RYKG; Eukaryota.
DR   HOGENOM; CLU_048726_0_0_1; -.
DR   InParanoid; D1ZSU8; -.
DR   OMA; QITRMAN; -.
DR   OrthoDB; 1569419at2759; -.
DR   Proteomes; UP000001881; 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; Zinc.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..285
FT                   /note="Extracellular metalloprotease SMAC_06893"
FT                   /id="PRO_0000407205"
FT   ACT_SITE        198
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         201
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        233..260
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   285 AA;  30543 MW;  A86740E9AB8B96CD CRC64;
     MQIKSLLLAA AAAPAALGAA VGTVKPFNCG TDAPSRQHIQ MTKEIAEKEA AFTAAGGVSA
     QAAINVNVYF HVVASSTSLS GGYVTSTMIN NQVSVLNTAY APHGIQFTLK GTDYTVNSNW
     AVDGSELAMK KALRKGTYKD LNLYILKDLG DALGYCYFPT SVTSKSNDWY YDGCSILYNT
     LPGGDLTNYN LGHTSTHEVG HWFGLYHTFQ GGCTGNGDYV ADTPAQASAS SGCPTGRDSC
     PSQTGLDPIH NYMDYSYDTC YEEFTAGQKT RMTSYFNQYR ANASV