ID   NPIIB_BLAGS             Reviewed;         366 AA.
AC   C5JHY1; A0A179UET9;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Neutral protease 2 homolog BDBG_02110;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin BDBG_02110;
DE   Flags: Precursor;
GN   ORFNames=BDBG_02110;
OS   Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=559298;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SLH14081;
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
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; GG657450; OAT05778.1; -; Genomic_DNA.
DR   EMBL; GG657450; OAT05779.1; -; Genomic_DNA.
DR   EMBL; GG657450; OAT05780.1; -; Genomic_DNA.
DR   RefSeq; XP_002627439.1; XM_002627393.1.
DR   AlphaFoldDB; C5JHY1; -.
DR   SMR; C5JHY1; -.
DR   EnsemblFungi; OAT05778; OAT05778; BDBG_02110.
DR   EnsemblFungi; OAT05779; OAT05779; BDBG_02110.
DR   EnsemblFungi; OAT05780; OAT05780; BDBG_02110.
DR   GeneID; 8506618; -.
DR   KEGG; bgh:BDBG_02110; -.
DR   VEuPathDB; FungiDB:BDBG_02110; -.
DR   HOGENOM; CLU_039313_1_1_1; -.
DR   Proteomes; UP000002038; 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; Glycoprotein;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..366
FT                   /note="Neutral protease 2 homolog BDBG_02110"
FT                   /id="PRO_0000407118"
FT   PROPEP          23..184
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407119"
FT   ACT_SITE        315
FT                   /evidence="ECO:0000250"
FT   BINDING         314
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         318
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        192
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        272..290
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   366 AA;  39271 MW;  6927F17556835CAD CRC64;
     MQLSSVLLTA AGLLAPVYSS AIISIGRRSE GLDVSLASTG NTKVQVSVTN TGSSEISILR
     ANTLFDASPT KKFTVYKEGS RKEVPFKGVH LRRSPSDLAK DNLQPIGPGQ TIDKEFDLAE
     TLNLSESGTY IVSADGVFPI IDPKSFSIAS VIPYESNELK IEVDGKQVSG VLSTRAKIHD
     HLAQRADFNN GNCTDHQKAV IASALKRDSS IAGEASNAAL SGDVRVFEQY FRTTDPSIRQ
     QVSDRFHAIS NEACSAEGGV VKYQCEDEMD VCRPGTVAYA LLGSNVVVNC PIYYSVTAVS
     QACDAGDQAL TVIHELSHID AVYYPATTDL AYGEDASMAL NADMSIRNAD SYTFYANAVR
     QNCNPS