ID   MEP_ASPCL               Reviewed;         634 AA.
AC   A1C4M2;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=ACLA_060300;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS026990; EAW15362.1; -; Genomic_DNA.
DR   RefSeq; XP_001276788.1; XM_001276787.1.
DR   AlphaFoldDB; A1C4M2; -.
DR   SMR; A1C4M2; -.
DR   STRING; 344612.A1C4M2; -.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EAW15362; EAW15362; ACLA_060300.
DR   GeneID; 4708814; -.
DR   KEGG; act:ACLA_060300; -.
DR   VEuPathDB; FungiDB:ACLA_060300; -.
DR   eggNOG; ENOG502QTDC; Eukaryota.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   OMA; WALIEAH; -.
DR   OrthoDB; 1136823at2759; -.
DR   Proteomes; UP000006701; 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   Reference proteome; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..246
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407174"
FT   CHAIN           247..634
FT                   /note="Extracellular metalloproteinase mep"
FT                   /id="PRO_0000407175"
FT   REGION          282..313
FT                   /note="Disordered"
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        318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        545
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   634 AA;  69044 MW;  097714BF572C647A CRC64;
     MRGLLLAGLV ALPASVLAHP SPAGHGIQRR AVDLNAFRLK TSATYADATE TANDPALSFT
     SLEKQSYVDT ATQFVKAIAP GLTFRVVDDH YVGDNEIAHV NFRQTANGLD IDNADFNVNV
     GKDGKIFSHG NSFFKGKIPD ASSLTKRDFS DPTVALKGTM ETLKLSLGIE KASIKPTDGE
     KESYVFNGVS GTVSDPKAKL VYFAKPDGTL ALTWRVETDV DHDWLLTYVD AQSGKEVHGV
     VNYVAEADYK VYPWGLNDPT EGSRVMIKDP WDTVASEFTW NSDGTKKYPT TRGNNGIAQS
     NPSGEDDYIN NHRPRSSNLS FNYPYSPSSS PPSSYIDASI VQLFYTANMY HDLLYTLGFT
     EKTGNFEFNN NGQGGRGNDY VILNSQDGSG TNNANFATPP DGQPGRMRMY TWTKSQPYRD
     GSFEAGIVIH EYTHGVSNRL TGGPANSNCL STIEAGGMGE GWGDFMATAI RLKAADTRAK
     DYTMGAWAAN DPKGIREYPY STSLTTNPLA YSNVDGDDSV HSIGTVWATM LYELMWNLID
     KHGKNVSAKP TMKGGVPTDG KYLAMKLVVD GMALQPCNPN FVQARDAILD ADKALTKGAN
     RCEIWKAFAK RGLGYGAKYN ENKRVTSNKL PSGC