ID   MEP1_ASPFN              Reviewed;         635 AA.
AC   B8NC58;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Extracellular metalloproteinase mep;
DE            EC=3.4.24.-;
DE   AltName: Full=Elastinolytic metalloproteinase mep;
DE   AltName: Full=Fungalysin mep;
DE   Flags: Precursor;
GN   Name=mep; ORFNames=AFLA_038530;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
CC   -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC       proteinaceous substrates. {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}.
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DR   EMBL; EQ963476; EED52152.1; -; Genomic_DNA.
DR   RefSeq; XP_002377316.1; XM_002377275.1.
DR   AlphaFoldDB; B8NC58; -.
DR   SMR; B8NC58; -.
DR   MEROPS; M36.001; -.
DR   PRIDE; B8NC58; -.
DR   EnsemblFungi; EED52152; EED52152; AFLA_038530.
DR   VEuPathDB; FungiDB:AFLA_038530; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   OMA; WALIEAH; -.
DR   Proteomes; UP000001875; 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   Secreted; Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..246
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407154"
FT   CHAIN           247..635
FT                   /note="Extracellular metalloproteinase mep"
FT                   /id="PRO_0000407155"
FT   REGION          290..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..310
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ   SEQUENCE   635 AA;  69302 MW;  7AACCD32E8409C2C CRC64;
     MMRGLLLAGA LGLPLAVLAH PTHHAHGLQR RTVDLNSFRL HQAAKYINAT ESSSDVSSSF
     SPFTEQSYVE TATQLVKNIL PDATFRVVKD HYIGSNGVAH VNFRQTAHGL DIDNADFNVN
     VGKNGKIFSY GHSFYTGKIP DANPLTKRDY TDPVAALRGT NEALQLSITL DQVSTEATED
     KESFNFKGVS GTVSDPKAQL VYLVKEDGSL ALTWKVETDI DSNWLLTYID ANTGKDVHGV
     VDYVAEADYQ VYAWGINDPT EGPRTVISDP WDSSASAFTW ISDGENNYTT TRGNNGIAQS
     NPTGGSQYLK NYRPDSPDLK FQYPYSLNAT PPESYIDASI TQLFYTANTY HDLLYTLGFN
     EEAGNFQYDN NGKGGAGNDY VILNAQDGSG TNNANFATPP DGQPGRMRMY IWTESQPYRD
     GSFEAGIVIH EYTHGLSNRL TGGPANSRCL NALESGGMGE GWGDFMATAI RLKAGDTHST
     DYTMGEWAAN KKGGIRAYPF STSLETNPLT YTSLNELDEV HAIGAVWANV LYELLWNLID
     KHGKNDGPKP EFKDGVPTDG KYLAMKLVID GMALQPCNPN CVQARDAILD ADKALTDGAN
     KCEIWKAFAK RGLGEGAEYH ASRRVGSDKV PSDAC