ID   MEP_ASPFC               Reviewed;         634 AA.
AC   B0Y9E2;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, 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=AFUB_080720;
OS   Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS   fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
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 and probably acts as a virulence factor.
CC       {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; DS499600; EDP48635.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y9E2; -.
DR   SMR; B0Y9E2; -.
DR   Allergome; 75; Asp f 5.
DR   MEROPS; M36.001; -.
DR   EnsemblFungi; EDP48635; EDP48635; AFUB_080720.
DR   VEuPathDB; FungiDB:AFUB_080720; -.
DR   HOGENOM; CLU_012703_3_0_1; -.
DR   PhylomeDB; B0Y9E2; -.
DR   Proteomes; UP000001699; 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..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..245
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407176"
FT   CHAIN           246..634
FT                   /note="Extracellular metalloproteinase mep"
FT                   /id="PRO_0000407177"
FT   ACT_SITE        430
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         429
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         433
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        286
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   634 AA;  68708 MW;  B9F9A8D83E1FEBBF CRC64;
     MRGLLLAGAL ALPASVFAHP AHQSYGLNRR TVDLNAFRLK SLAKYVNATE TVIEAPSSFA
     PFKPQSYVEV ATQHVKMIAP DATFRVVDDH YVGDNGVAHV HFRQTANGLD IDNADFNVNV
     GKDGKVFSYG NSFYTGQIPS SAALTKRDFS DPVTALKGTT NTLQLPITVD SASSESTEEK
     ESYVFKGVSG TVSDPKAKLV YFVKDDGTLA LAWRVETDID SNWLLTYIDA KSGEEIHGVV
     DYVAEADYQV YAWGINDPTE GERTVIKDPW DSVASEFTWI SDGSTNYTTS RGNNGIAQSN
     PSGGSSYLNN YRPSSSSLSF KYPYSVSSSP PSSYIDASII QLFYTANIYH DLLYTLGFTE
     KAGNFEYNTN GQGGLGNDYV ILNAQDGSGT NNANFATPPD GQPGRMRMYV WTESTPYRDG
     SFEAGIVIHE YTHGLSNRLT GGPANSNCLN ALESGGMGEG WSDFMATAIR LKPGDKRSTD
     YTMGEWASNR AGGIRQYPYS TSLSTNPLTY TSVNSLNAVH AIGTVWASML YEVLWNLIDK
     HGKNDAPKPT LRDGVPTDGK YLAMKLVMDG MALQPCNPNF VQARDAILDA DTALTGGENQ
     CEIWTAFAKR GLGAGAKYSS RNRVGSTEVP SGVC