ID   NPIIA_MAGO7             Reviewed;         347 AA.
AC   Q2KH28; A4RCX3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Neutral protease 2 homolog MGG_10927;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin MGG_10927;
DE   Flags: Precursor;
GN   ORFNames=MGCH7_ch7g157, MGG_10927;
OS   Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Pyricularia oryzae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=242507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RA   Thon M.R., Pan H., Diener A., Papalas J., Taro A., Mitchell T., Dean R.A.;
RT   "The sequence of Magnaporthe grisea chromosome 7.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX   PubMed=15846337; DOI=10.1038/nature03449;
RA   Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA   Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA   Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA   Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA   Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA   Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT   "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL   Nature 434:980-986(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM000230; EAQ70750.1; -; Genomic_DNA.
DR   EMBL; JH165176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_016845997.1; XM_016990527.1.
DR   AlphaFoldDB; Q2KH28; -.
DR   SMR; Q2KH28; -.
DR   EnsemblFungi; MGG_10927T0; MGG_10927T0; MGG_10927.
DR   GeneID; 2677075; -.
DR   KEGG; mgr:MGG_10927; -.
DR   VEuPathDB; FungiDB:MGG_10927; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_0_0_1; -.
DR   InParanoid; Q2KH28; -.
DR   OMA; DVTFVHL; -.
DR   Proteomes; UP000009058; 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..176
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407104"
FT   CHAIN           177..347
FT                   /note="Neutral protease 2 homolog MGG_10927"
FT                   /id="PRO_0000407105"
FT   ACT_SITE        300
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         299
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
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   DISULFID        180..250
FT                   /evidence="ECO:0000250"
FT   DISULFID        257..275
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   347 AA;  36861 MW;  DE9CA88F75DCF9C0 CRC64;
     MKYSVGITAL LATLAQGAAV MSKRDIPLDV KIQVVNNSEV KASITNSGSS SIKVVKTGSI
     LDSADVEKSV IMAGENKVAF DGIRYQVATA GLPAEAFQII EAGETIEVSF NVASTHDFAQ
     GGDFDIAALG TFSVAESDSG DIFSAMAFES NHIKAHIDGT EAAKVRRSYL AKRTMVQSDC
     TGTRLTQTTN AINSCRSLAQ RAASAAQSNS AKMNEYFKST SSSAVNTVVT TFNRIASECN
     PSGGASRQYC TDQIGACSPG VIAYTVPSQS IMVNCPTFFT MPTTSNACRA QTQDNTILHE
     VTHLSQVKGT QDYNCYGYTC MRQLTSAQNL NHADTYTLFA QAIKVGC