ID   MEP20_ASPFM             Reviewed;         365 AA.
AC   Q09016;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Neutral protease 2 homolog mep20;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin mep20;
DE   Flags: Precursor;
GN   Name=mep20;
OS   Neosartorya fumigata (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=746128;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7489900; DOI=10.1016/0378-1119(95)00434-8;
RA   Ramesh M.V., Sirakova T.D., Kolattukudy P.E.;
RT   "Cloning and characterization of the cDNAs and genes (mep20) encoding
RT   homologous metalloproteinases from Aspergillus flavus and A. fumigatus.";
RL   Gene 165:121-125(1995).
CC   -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC       proteinaceous substrates. Shows high activities on basic nuclear
CC       substrates such as histone and protamine. May be involved in virulence
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage of bonds with hydrophobic residues in
CC         P1'. Also 3-Asn-|-Gln-4 and 8-Gly-|-Ser-9 bonds in insulin B chain.;
CC         EC=3.4.24.39;
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 M35 family. {ECO:0000305}.
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DR   EMBL; U24146; AAB07644.1; -; Genomic_DNA.
DR   PIR; JC4379; JC4379.
DR   AlphaFoldDB; Q09016; -.
DR   SMR; Q09016; -.
DR   MEROPS; M35.002; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001384; Peptidase_M35.
DR   Pfam; PF02102; Peptidase_M35; 1.
DR   PRINTS; PR00768; DEUTEROLYSIN.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Signal;
KW   Virulence; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..172
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407064"
FT   CHAIN           173..365
FT                   /note="Neutral protease 2 homolog mep20"
FT                   /id="PRO_0000407065"
FT   ACT_SITE        300
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         299
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         303
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         314
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        351
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        178..249
FT                   /evidence="ECO:0000250"
FT   DISULFID        256..274
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   365 AA;  39031 MW;  61495EA7CF94C345 CRC64;
     MKVTILASAI LALINGALAL PANTPTLDVT LTQVDNTRIK ATVKNTGNEK VTFVHLNFFQ
     DAAPVKKVSL FRNGTEVEFT GIKRRLLTEG LSDDGLTTLA PGGTFEDEFD VASTGDLTEG
     GTVTIRTDGF VPITTDRKVS GYIPYQSNEL EIEVDPAKAA AVPQAIKLLD RRTKVASCSG
     SRASALSTAL RNAGSLANAA ASAASSGSST RFQEYFKTTS RRPENVGGRF RAVGREASSQ
     SSGKTTYYCN DPYGYCDSNT LAYTLPSSNL IANCDIYYSY LPALTSSCHA QDQATTTLHE
     FTHAPAVYSP GTDDYAYGYR ASTALSASQA LLNADTYALF ANGSPLLPLS NHSKCRNTMV
     WRTLL