ID   NPIIA_PHANO             Reviewed;         350 AA.
AC   Q0UCJ2;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Neutral protease 2 homolog SNOG_10522;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin SNOG_10522;
DE   Flags: Precursor;
GN   ORFNames=SNOG_10522;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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; CH445341; EAT81916.1; -; Genomic_DNA.
DR   RefSeq; XP_001800791.1; XM_001800739.1.
DR   AlphaFoldDB; Q0UCJ2; -.
DR   SMR; Q0UCJ2; -.
DR   MEROPS; M35.001; -.
DR   EnsemblFungi; SNOT_10522; SNOT_10522; SNOG_10522.
DR   GeneID; 5977698; -.
DR   KEGG; pno:SNOG_10522; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_0_0_1; -.
DR   InParanoid; Q0UCJ2; -.
DR   OMA; GTQTMWD; -.
DR   OrthoDB; 1038868at2759; -.
DR   BRENDA; 3.4.24.39; 7864.
DR   Proteomes; UP000001055; 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; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001384; Peptidase_M35.
DR   Pfam; PF02102; Peptidase_M35; 1.
DR   PRINTS; PR00768; DEUTEROLYSIN.
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..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..180
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407112"
FT   CHAIN           181..350
FT                   /note="Neutral protease 2 homolog SNOG_10522"
FT                   /id="PRO_0000407113"
FT   ACT_SITE        302
FT                   /evidence="ECO:0000250"
FT   BINDING         301
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         305
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         316
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   DISULFID        184..251
FT                   /evidence="ECO:0000250"
FT   DISULFID        258..276
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   350 AA;  35981 MW;  56041855C351FA88 CRC64;
     MKVSSQLAVA ALASFATAAS VDVHKRETPL SVKLAASGNS EVKVTLTNNG EKTLNLLSKG
     TFLDEQLPVE KVQMYAAGGS DKVAFEGMKV RLLTSGLKAD DFVTLAAGET KEITVETAAL
     HSLHEGGDFD VFAKGALPFA EGASTELAGA LDYESNKLSM TIDGAQAASV AKALNKRTAI
     GSSCTGTKLS TVRTALSNCA RLANAAASAA TSGTKLTTYF KTTSSASTVA ARLRAVASDC
     GSTSSRTTTN CNDPYSGCSS NVLAYTVPSA NFITYCPIFF SALPALASTC HGQDQATTAL
     HEETHAPGVY SPGTQDNGYG YAAATALSAN QALNNADSYA LYANAINLNC