ID   NPIIA_ASPTN             Reviewed;         352 AA.
AC   Q0CMZ3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Neutral protease 2 homolog ATEG_04941;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin ATEG_04941;
DE   Flags: Precursor;
GN   ORFNames=ATEG_04941;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476600; EAU34010.1; -; Genomic_DNA.
DR   RefSeq; XP_001214119.1; XM_001214119.1.
DR   AlphaFoldDB; Q0CMZ3; -.
DR   SMR; Q0CMZ3; -.
DR   MEROPS; M35.002; -.
DR   EnsemblFungi; EAU34010; EAU34010; ATEG_04941.
DR   GeneID; 4321206; -.
DR   VEuPathDB; FungiDB:ATEG_04941; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_1_1_1; -.
DR   OMA; DVTFVHL; -.
DR   OrthoDB; 1038868at2759; -.
DR   Proteomes; UP000007963; 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..175
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407096"
FT   CHAIN           176..352
FT                   /note="Neutral protease 2 homolog ATEG_04941"
FT                   /id="PRO_0000407097"
FT   ACT_SITE        304
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         303
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         307
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         318
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   DISULFID        181..253
FT                   /evidence="ECO:0000250"
FT   DISULFID        260..278
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   352 AA;  37061 MW;  4CC8825D185B825B CRC64;
     MRFTALATAI LPLACNVLAL PAKTGEAPKL DVSLSQVDNT LIKAVVKNTG SEDITFVHLN
     FFRDKAPVKK VSLFRNATEL PFQGIKQRFR TEGLTEDALT VLAPGESIED EFDIAATSDL
     SEGGSITIST DGFVPIATGN KITGSVPYSS NELSIEVDAA QAASVASAVK PLDKRTKVAS
     CSGTRSSALS TALKNTVSLA NAAASAAQSG SSSRFQEYFK TTSSSVRSTV AARFRAVASE
     ASSTSSGSTT YYCTDTYGYC SSNVLAYTLP AYNIIANCDI YYTYLSALTR TCHAQDQATT
     TLHEFTHAPG VYSPGTDDLG YGYDAATALS SSQALNNADT YALFANAVNL NC