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 27-MAR-2024, entry version 63.
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 STRING; 332952.B8NJB2; -.
DR MEROPS; M35.002; -.
DR EnsemblFungi; EED49723; EED49723; AFLA_065450.
DR VEuPathDB; FungiDB:AFLA_008474; -.
DR eggNOG; ENOG502SGF5; Eukaryota.
DR HOGENOM; CLU_039313_1_1_1; -.
DR OMA; ANCDLYY; -.
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 CDD; cd11008; M35_deuterolysin_like; 1.
DR Gene3D; 2.60.40.2970; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001384; Peptidase_M35.
DR PANTHER; PTHR37016; -; 1.
DR PANTHER; PTHR37016:SF3; NEUTRAL PROTEASE 2 HOMOLOG AN3393-RELATED; 1.
DR Pfam; PF02102; Peptidase_M35; 1.
DR PRINTS; PR00768; DEUTEROLYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
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
//
