ID   NPIIA_NEOFI             Reviewed;         467 AA.
AC   A1DA48;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Neutral protease 2 homolog NFIA_031120;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin NFIA_031120;
DE   Flags: Precursor;
GN   ORFNames=NFIA_031120;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027693; EAW20679.1; -; Genomic_DNA.
DR   RefSeq; XP_001262576.1; XM_001262575.1.
DR   AlphaFoldDB; A1DA48; -.
DR   SMR; A1DA48; -.
DR   MEROPS; M35.002; -.
DR   EnsemblFungi; EAW20679; EAW20679; NFIA_031120.
DR   GeneID; 4589113; -.
DR   KEGG; nfi:NFIA_031120; -.
DR   VEuPathDB; FungiDB:NFIA_031120; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_1_1_1; -.
DR   OMA; GTQTMWD; -.
DR   OrthoDB; 1038868at2759; -.
DR   Proteomes; UP000006702; 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; IPR029463; Lys_MEP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001384; Peptidase_M35.
DR   Pfam; PF02102; Peptidase_M35; 1.
DR   PRINTS; PR00768; DEUTEROLYSIN.
DR   SMART; SM01351; Aspzincin_M35; 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; Reference proteome; Secreted;
KW   Signal; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..172
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407106"
FT   CHAIN           173..467
FT                   /note="Neutral protease 2 homolog NFIA_031120"
FT                   /id="PRO_0000407107"
FT   REGION          359..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        301
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         300
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
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         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   DISULFID        179..251
FT                   /evidence="ECO:0000250"
FT   DISULFID        258..276
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   467 AA;  49367 MW;  8711BC6A16F0E61F CRC64;
     MKITALASAI LAVVHGALAL PARAPALDIT LSQVNNTRIK AVVKNSGSEK ITFVHLNFFN
     DPSPVKKVSL YRNATEVEFT GIKQRLRSDG LSNEALTTLA PGATYEDEFD IASTANLTQG
     GPVTVRTQGF VPIAMNNKIA GYIPYSSNEL ELEVDAVKAV AVPASIKPLD RRTKITSSCT
     GDRAAVLNTA LRNAASIAGK AANAASSGSS ALFAEYFKST SGNIRSAVAA RLKAVASEAS
     LNGGGSTTYY CSDPYGYCDS NVLAYTLPST NEVVNCELFY TLQEVTNDCH GQDQATTIIH
     EFTHAPGVYP PGTEDLGYGY SAATALSANN ALNNADSYAL FANAVYLNCQ GQTGGQTMWD
     GNSQPGQTAP GTQTMWDGNS QPGQTEPGTQ TMWDGNSQPG QTEPGTQTMW DGNSQPGQTE
     PGTQTMWDGN SQPGQTEPCT QTMWDGSSEP GQTEPDAHTT WGNFYQA