ID   NPIIA_ASPFN             Reviewed;         404 AA.
AC   B8NJB2;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Neutral protease 2 homolog AFLA_065450;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin AFLA_065450;
DE   Flags: Precursor;
GN   ORFNames=AFLA_065450;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M35 family. {ECO:0000305}.
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DR   EMBL; EQ963479; EED49723.1; -; Genomic_DNA.
DR   RefSeq; XP_002380104.1; XM_002380063.1.
DR   AlphaFoldDB; B8NJB2; -.
DR   SMR; B8NJB2; -.
DR   MEROPS; M35.002; -.
DR   EnsemblFungi; EED49723; EED49723; AFLA_065450.
DR   VEuPathDB; FungiDB:AFLA_065450; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_1_1_1; -.
DR   OMA; DVTFVHL; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
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; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..185
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407090"
FT   CHAIN           186..404
FT                   /note="Neutral protease 2 homolog AFLA_065450"
FT                   /id="PRO_0000407091"
FT   ACT_SITE        314
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         317
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         328
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   DISULFID        191..263
FT                   /evidence="ECO:0000250"
FT   DISULFID        270..288
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   404 AA;  42823 MW;  5BCCBC745F1B99AF CRC64;
     MRFISASSLL LALAPTLNAV PVEVAGSAQG LDVTLSQVGN TRIKAVVKNT GSEDVTFVHL
     NFFKDAAPVQ KVSLFRNGML PNLNLATTEV QFQGIKQRLI TEGLSDDALT TLAPGATIED
     EFDIASTSDL SEGGTITINS NGLVPITTDN KVTGYIPFTS NELSIDVDAA EAASVTQAVK
     ILERRTKVTS CSGSRLSALQ TALRNTVSLA RAAATAAQSG SSSRFQEYFK TTSSSTRSTV
     AARLNAVANE AASTSSGSTT YYCSDVYGYC SSNVLAYTLP SYNIIANCDL YYSYLPALTS
     TCHAQDQATT TLHEFTHAPG VYSPGTDDLG YGYSAATALS ASQALLNADT YALFANGTYS
     SLLSFVNPLL TPDNSCQPQL LDARTCNRQF GRSTSCKVYW KAVE