ID   NPIIA_PARBD             Reviewed;         358 AA.
AC   C1G1N6;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Neutral protease 2 homolog PADG_00776;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin PADG_00776;
DE   Flags: Precursor;
GN   ORFNames=PADG_00776;
OS   Paracoccidioides brasiliensis (strain Pb18).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb18;
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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   -!- SEQUENCE CAUTION:
CC       Sequence=EEH44487.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; KN275957; EEH44487.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_010755974.1; XM_010757672.1.
DR   AlphaFoldDB; C1G1N6; -.
DR   SMR; C1G1N6; -.
DR   MEROPS; M35.002; -.
DR   EnsemblFungi; EEH44487; EEH44487; PADG_00776.
DR   GeneID; 22580559; -.
DR   KEGG; pbn:PADG_00776; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_1_1_1; -.
DR   BRENDA; 3.4.24.39; 6937.
DR   Proteomes; UP000001628; 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; 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..185
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407108"
FT   CHAIN           186..358
FT                   /note="Neutral protease 2 homolog PADG_00776"
FT                   /id="PRO_0000407109"
FT   ACT_SITE        310
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         309
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         324
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        249
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        188..259
FT                   /evidence="ECO:0000250"
FT   DISULFID        266..284
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   358 AA;  38509 MW;  CCCB960CB525BBC7 CRC64;
     MRRVSGILAV AAFTISAFAG VIQPVAKDAR DSAELDVKLT QVDGTVIKAV VTNNGDKDLN
     ILNLNFFRDT APVKKVSIYS QGVEVPFGGI RVRHKTSDLS SDVITYLAPG ESFEDEFDVA
     ITSDLSQGGP VVLQTQGYVP TTDTGGKTLS GVVRYKSNKL EIDVDGTTAA KSFAAMNQFV
     KIAKLSSCEG SQGDDTRRAL RDCASLSTLA AAQAWAGGPK MLEYFKANDD ATRKLVADRF
     TAVALESSNL TGGSTTYYCR DPYNICTNNI IAYTIPAENL ISNCPIYYTE FDNVNRKCHG
     QDRVTTSLHE FTHASSVFSP GTKDIAYGYN ACILLSTRDA LNNADTFALF AQSINAGC