ID   MEP20_ASPFL             Reviewed;         381 AA.
AC   P46073;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 89.
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   Aspergillus flavus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5059;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Isolate 28;
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 (By similarity).
CC       {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   -!- SIMILARITY: Belongs to the peptidase M35 family. {ECO:0000305}.
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DR   EMBL; L37524; AAA96712.1; -; Genomic_DNA.
DR   PIR; JC4378; JC4378.
DR   AlphaFoldDB; P46073; -.
DR   SMR; P46073; -.
DR   MEROPS; M35.002; -.
DR   VEuPathDB; FungiDB:AFLA_065450; -.
DR   VEuPathDB; FungiDB:F9C07_2285744; -.
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   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW   Signal; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..193
FT                   /id="PRO_0000029236"
FT   CHAIN           194..381
FT                   /note="Neutral protease 2 homolog mep20"
FT                   /id="PRO_0000029237"
FT   ACT_SITE        322
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         321
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         325
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         336
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   DISULFID        199..271
FT                   /evidence="ECO:0000250"
FT   DISULFID        278..296
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   381 AA;  40558 MW;  A09D292513FA8EC2 CRC64;
     MRFTALASAI LPLACNVLAL PAKTGEAPKL DVSLSQVDNT LIKAVVKNTG SEDITFVHLN
     FFRDKAPVKK VSLFRQRYVI PLHPHFPALT SVIQPTELPF QGIKQRFRTE GLTEDALTVL
     APGESIEDEF DIAATSDLSE GGSITISTDG FVPIATGNKI TGSVPYSSNE LSIEVDAAQA
     ASVASAVKPL DKRTKVASCS GTRSSALSTA LKNTVSLANQ AASAAQSGSS SRFQEYFKTT
     SSSVRTSVAA RFRAVASEAS STSSGSTTYY CTDTYGYCSS NVPGVHLPAY NIIANCDIYY
     TYLSALTRTC HAQDQATTTL HEFTHAPGVY SPGTDDLGYG YDAATALSSS QALNNVDTYA
     LFANGKFLLS REVDVKYLHT T