ID   NPIIB_PHANO             Reviewed;         354 AA.
AC   Q0V1D7;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Neutral protease 2 homolog SNOG_02177;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin SNOG_02177;
DE   Flags: Precursor;
GN   ORFNames=SNOG_02177;
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; CH445327; EAT90389.1; -; Genomic_DNA.
DR   RefSeq; XP_001792793.1; XM_001792741.1.
DR   AlphaFoldDB; Q0V1D7; -.
DR   SMR; Q0V1D7; -.
DR   EnsemblFungi; SNOT_02177; SNOT_02177; SNOG_02177.
DR   GeneID; 5969643; -.
DR   KEGG; pno:SNOG_02177; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_0_0_1; -.
DR   InParanoid; Q0V1D7; -.
DR   OMA; ESNELHM; -.
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; Glycoprotein;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..182
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407130"
FT   CHAIN           183..354
FT                   /note="Neutral protease 2 homolog SNOG_02177"
FT                   /id="PRO_0000407131"
FT   ACT_SITE        307
FT                   /evidence="ECO:0000250"
FT   BINDING         306
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         310
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        214
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        186..257
FT                   /evidence="ECO:0000250"
FT   DISULFID        264..282
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   354 AA;  37582 MW;  8FC1BBF72736966A CRC64;
     MKFQILSVAA LASLASAVSD ALDKRDSPLD VSLEVTDNTN VKATIKNTGT EDLKLFKTGT
     FLDDSHVEKV EVFRSGKQPE QVAFEGLRLR VSTANLDESA FKILKAGETI EAAFDIAVAH
     DLSVGGDFDL LTEGAFAYAN LDSTSIAGAV PFTSNKVTTA VDGAKAGKVR RDWIDLAKRT
     IVQSDCTGSR GTATRTALSN CASLARTAAN AAVNNSAKLN EYFKSTSSST ASSVQTVYNR
     IATQCGSTTS GDSTQYCSDI LGACAGGVLA YTSPSTSQMV NCPLFFNQSP LSSQCHAQDQ
     ATTILHEMTH LRQVKGTSDY GGYGYQFVRS LSAAQNLNHA DTYTLFAQAL YAQC