ID   NPIIB_ASPFN             Reviewed;         284 AA.
AC   B8NWE1;
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_119780;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin AFLA_119780;
DE   Flags: Precursor;
GN   ORFNames=AFLA_119780;
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; EQ963485; EED45749.1; -; Genomic_DNA.
DR   RefSeq; XP_002384685.1; XM_002384644.1.
DR   AlphaFoldDB; B8NWE1; -.
DR   SMR; B8NWE1; -.
DR   MEROPS; M35.001; -.
DR   EnsemblFungi; EED45749; EED45749; AFLA_119780.
DR   VEuPathDB; FungiDB:AFLA_119780; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_2_0_1; -.
DR   OMA; NTIMDEH; -.
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..?
FT                   /evidence="ECO:0000255"
FT   PROPEP          ?..110
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407124"
FT   CHAIN           111..284
FT                   /note="Neutral protease 2 homolog AFLA_119780"
FT                   /id="PRO_0000407125"
FT   ACT_SITE        236
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         235
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         239
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         250
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   DISULFID        113..185
FT                   /evidence="ECO:0000250"
FT   DISULFID        192..210
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   284 AA;  30301 MW;  B6310970F3CE6943 CRC64;
     MAFINSAAED EVQFEGIKRR LRSSGITKEA VTSLGAGETL EDEFDIASTS DLASGGPVSI
     RSHGFVPIVV DGKITGYIPY KSNDLTVNVD GGKAAKVTKA LSQLTRRTEV TDCKGDAESS
     LTTALSNAAK LANQAAEAAE SGDESKFEEY FKTTDQQTRT TVAERLRAVA KEAGSTSGGS
     TTYHCSDPYG YCEPNVLAYT LPSKNEIANC DIYYSELPPL AQKCHAQDQA TTTLHEFTHA
     PGVYQPGTED LGYGYDAATQ LSAQDALNNA DSYALYANAI ELKC