ID   NPIIA_COLGM             Reviewed;         351 AA.
AC   E3QWD3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 40.
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=GLRG_10315;
OS   Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS   anthracnose fungus) (Glomerella graminicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=645133;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1.001 / M2 / FGSC 10212;
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
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; GG697389; EFQ35171.1; -; Genomic_DNA.
DR   RefSeq; XP_008099191.1; XM_008101000.1.
DR   AlphaFoldDB; E3QWD3; -.
DR   SMR; E3QWD3; -.
DR   EnsemblFungi; EFQ35171; EFQ35171; GLRG_10315.
DR   GeneID; 24415680; -.
DR   VEuPathDB; FungiDB:GLRG_10315; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_0_0_1; -.
DR   OrthoDB; 1038868at2759; -.
DR   Proteomes; UP000008782; 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.
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..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..177
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407100"
FT   CHAIN           178..351
FT                   /note="Neutral protease 2 homolog MGG_10927"
FT                   /id="PRO_0000407101"
FT   ACT_SITE        304
FT                   /evidence="ECO:0000250"
FT   BINDING         303
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         307
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   DISULFID        181..253
FT                   /evidence="ECO:0000250"
FT   DISULFID        260..278
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   351 AA;  37190 MW;  86E1BB7284CC1ABF CRC64;
     MKFSIGVSLL ATLAGAVNVD MAKRDTSPLN VKLEALGNSG VKAVLTNTGD SDIKLFKTGT
     FLDKSPVEKV EVFAAGSKID FDGVRLQIST TGLTEEAFQI VAAGETFEVE FDAAELHDLS
     KGGAVDIVTQ GSFLYADVDS TEIAGTIPFS SNSVHTEING DEAASVRAAF LAKRTIVQSD
     CTGTRRTATV NAISRCRALA AAASQAAASG PVARMTEYFK SSTTATRNSV ATVFRNIVSE
     CGSTTSGVSR QYCTDVYGAC SNGVIAYTVP AQNYMVNCPY FFNNMAAASS TCHAQDQQTT
     ILHEMTHLRQ IKGTSDYGGY GYNFVRSLSA AQNLNHADTY TLFAQSIYAG C