ID   MEP_ASPTN               Reviewed;         633 AA.
AC   Q0CFJ0;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=ATEG_07544;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- INDUCTION: Expression is controlled by the prtT transcription factor.
CC   -!- SIMILARITY: Belongs to the peptidase M36 family. {ECO:0000305}.
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DR   EMBL; CH476604; EAU31806.1; -; Genomic_DNA.
DR   RefSeq; XP_001216165.1; XM_001216165.1.
DR   AlphaFoldDB; Q0CFJ0; -.
DR   SMR; Q0CFJ0; -.
DR   STRING; 341663.Q0CFJ0; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EAU31806; EAU31806; ATEG_07544.
DR   GeneID; 4322867; -.
DR   VEuPathDB; FungiDB:ATEG_07544; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   OMA; IRKDSYT; -.
DR   OrthoDB; 1136823at2759; -.
DR   Proteomes; UP000007963; 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   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..244
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407179"
FT   CHAIN           245..633
FT                   /note="Extracellular metalloproteinase mep"
FT                   /id="PRO_0000407180"
FT   ACT_SITE        429
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         428
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         432
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        326
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        514
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   633 AA;  68841 MW;  F9BF3ECBDE12509E CRC64;
     MRLLSLAGAM ALPLCVLAHP THRTRGIARR GIDLTPYRLP GNAEYTSSRT SAMRSLLFER
     ADGEDYVETA KKVLQSVHPD ATFRVIDDHY VGDNGVAHVH LLQTAHGIDI DNANFNVNID
     KNGKVLSYGN SFFSGKIPDS DPLTKRSFSD PVEALKAAAT GLGIPLTADD VTSEGLDGTT
     SYTFKGTKGA LSDPTADLVY LAKPDNTLAL TWRVETDMNS NWLLTYVDAE TAETIHGVVD
     YISDATYQVY PWGLNDPTEG SRQILEDPWD SKASEFTWIG DGKAKYKTTR GNNGIAQSNP
     DGGDDYLNNH RPESSSLKFV YPYSPNATSP SSYIDASITQ LFYTANTYHD LLYTLGFNEK
     AGNFEANNNG AGGKGNDFVI LNAQDGSGTN NAMFGSPPDG RPGRMYMFIW TESNPPRDGS
     MEAGIVIHEY THGLSSRLTG GPANARCVDG EESGGMGEGW GDFMATAVRL KSGDTRQTDY
     TMGAWAANDP KGIRDYPYST SMTKNPLTYA HLNNVTEVHE GGTIWASMLY EVMWNLIDKH
     GKNDAPKPDL KDGVPTDGKY LSMKLVMDGM ALQPCNPSFI QARDAILDAD VALTKSGNQC
     EIWKGFAKRG LGERAALKNG IRVDSFDVPK GVC