ID   NPIIA_ASPOR             Reviewed;         353 AA.
AC   Q2UP30;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Neutral protease 2 homolog AO090001000135;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin AO090001000135;
DE   Flags: Precursor;
GN   ORFNames=AO090001000135;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007154; BAE56685.1; -; Genomic_DNA.
DR   RefSeq; XP_001818687.1; XM_001818635.2.
DR   AlphaFoldDB; Q2UP30; -.
DR   SMR; Q2UP30; -.
DR   MEROPS; M35.001; -.
DR   EnsemblFungi; BAE56685; BAE56685; AO090001000135.
DR   GeneID; 5990658; -.
DR   KEGG; aor:AO090001000135; -.
DR   VEuPathDB; FungiDB:AO090001000135; -.
DR   HOGENOM; CLU_039313_1_1_1; -.
DR   OMA; DVTFVHL; -.
DR   BRENDA; 3.4.24.39; 522.
DR   Proteomes; UP000006564; Chromosome 2.
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; Reference proteome; Secreted;
KW   Signal; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..176
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407094"
FT   CHAIN           177..353
FT                   /note="Neutral protease 2 homolog AO090001000135"
FT                   /id="PRO_0000407095"
FT   ACT_SITE        305
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         304
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         319
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   DISULFID        182..254
FT                   /evidence="ECO:0000250"
FT   DISULFID        261..279
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   353 AA;  37103 MW;  747D31A9AC64AA0F CRC64;
     MRFISVSSLL LALAPALNAV PVEVAGSAQG LDVTLSQVGN TRIKAVVKNT GSEDVTFVHL
     NFFKDAAPVQ KVSLFRNATE VQFQGIKQRL ITEGLSDDAL TTLAPGATIE DEFDIASTSD
     LSEGGTITIN SNGLVPITTD NKVTGYIPFT SNELSIDVDA AEAASVTQAV KILERRTKVT
     SCSGSRLSAL QTALRNTVSL ARAAATAAQS GSSSRFQEYF KTTSSSTRST VAARLNAVAN
     EAASTSSGST TYYCSDVYGY CSSNVLAYTL PSYNIIANCD LYYSYLPALT STCHAQDQAT
     TTLHEFTHAP GVYSPGTDDL GYGYSAATAL SASQALLNAD TYALFANAVN LNC