ID   NPIIA_ASPCL             Reviewed;         349 AA.
AC   A1CIU4;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Neutral protease 2 homolog ACLA_052720;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin ACLA_052720;
DE   Flags: Precursor;
GN   ORFNames=ACLA_052720;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027054; EAW10799.1; -; Genomic_DNA.
DR   RefSeq; XP_001272225.1; XM_001272224.1.
DR   AlphaFoldDB; A1CIU4; -.
DR   SMR; A1CIU4; -.
DR   MEROPS; M35.002; -.
DR   EnsemblFungi; EAW10799; EAW10799; ACLA_052720.
DR   GeneID; 4703879; -.
DR   KEGG; act:ACLA_052720; -.
DR   VEuPathDB; FungiDB:ACLA_052720; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_1_1_1; -.
DR   OMA; DVTFVHL; -.
DR   OrthoDB; 1038868at2759; -.
DR   Proteomes; UP000006701; 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_0000407086"
FT   CHAIN           173..349
FT                   /note="Neutral protease 2 homolog ACLA_052720"
FT                   /id="PRO_0000407087"
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        178..250
FT                   /evidence="ECO:0000250"
FT   DISULFID        257..275
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   349 AA;  36695 MW;  F5D5CF0D9C710CC6 CRC64;
     MQLTVLASAI LALAQGALAI PAKAPALDVT LSQIDNTRVK AVVKNTGAEE VTFVHLNFFR
     DAAPVKKVSL FRNATEVPFN GIKLRFRNKG LTDDVLTTLA AGATFEDEFD IASTADLTEG
     GVVTVRSQGV VPLTKDNKVS GYIPFTSNEI ELEVDGAKAA AVPAAINLLD RRTKVASCSG
     SRATALQTAL RNTVSLANAA ASAAESGSSS RFSEYFKTTS SATRSTVAAR LRAVAREAGS
     TSSGKTTYYC GDPYGYCDPN VLAYTLPSKN IVANCDIYYS DLPALARSCH AQDQATTTLH
     EFTHAPGVYS PGTDDLGYGY QAATALSTSD ALNNADTYAL FANAVNLNC