ID   NPIIA_BLAGS             Reviewed;         357 AA.
AC   C5JKQ0; A0A179UGV8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 2.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Neutral protease 2 homolog BDBG_03102;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin BDBG_03102;
DE   Flags: Precursor;
GN   ORFNames=BDBG_03102;
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}.
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; GG657451; OAT06983.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5JKQ0; -.
DR   SMR; C5JKQ0; -.
DR   MEROPS; M35.002; -.
DR   EnsemblFungi; OAT06983; OAT06983; BDBG_03102.
DR   VEuPathDB; FungiDB:BDBG_03102; -.
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; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001384; Peptidase_M35.
DR   Pfam; PF02102; Peptidase_M35; 1.
DR   PRINTS; PR00768; DEUTEROLYSIN.
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..182
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407082"
FT   CHAIN           183..357
FT                   /note="Neutral protease 2 homolog BDBG_03102"
FT                   /id="PRO_0000407083"
FT   ACT_SITE        309
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         312
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   DISULFID        188..259
FT                   /evidence="ECO:0000250"
FT   DISULFID        266..284
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   357 AA;  38190 MW;  7337CF3036067932 CRC64;
     MRSPQSILAI VAFATTAIAG VVPSTEKRAD DIPELDVKLT QVEGTLVKAV VTNNGDEDLN
     ILNLNFFKDT APVKKVSVYS QGAEVPFAGV RLRHKTSGLS PEVFTHLGPG ESFEDEFDVA
     FTADLSQGGR IVVKAEGFAS TTDTDGDTLS GVVHYKSNEL EIDVDGKAAA KNFASLNQFS
     KRTRLTGCTG SRGSAATRAI RDSAPLAAMA AGAARNGGRA FTQYFKTNDQ QVRNLVAARF
     DAVAREASST TSGRTTYYCD DPYGICSPNV LAYALPSRNI ISNCPAYYSL SHLTWRCHGQ
     DRVTTSIHEF THTPGVFSPG TDDLAYGHQA ATSLSTWEAL NNADSFSLFA NAVYLGC