ID   NPIIA_PARBP             Reviewed;         358 AA.
AC   C0S3U8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   04-FEB-2015, sequence version 2.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Neutral protease 2 homolog PABG_02362;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin PABG_02362;
DE   Flags: Precursor;
GN   ORFNames=PABG_02362;
OS   Paracoccidioides brasiliensis (strain Pb03).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=482561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb03;
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=EEH20103.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; KN305533; EEH20103.2; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; C0S3U8; -.
DR   SMR; C0S3U8; -.
DR   MEROPS; M35.002; -.
DR   EnsemblFungi; EEH20103; EEH20103; PABG_02362.
DR   HOGENOM; CLU_039313_1_1_1; -.
DR   InParanoid; C0S3U8; -.
DR   Proteomes; UP000002740; 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; Secreted; Signal;
KW   Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..182
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407110"
FT   CHAIN           183..358
FT                   /note="Neutral protease 2 homolog PABG_02362"
FT                   /id="PRO_0000407111"
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;  38451 MW;  CD69060CB5982BC7 CRC64;
     MRRVSGILAV AAFTISAFAG VIQPVAKDAR DSAELDVKLT QVDGTVIKAV VTNNGDKDLN
     ILNLNFFRDT APVKKVSIYS QGVEVPFGGI RVRHKTSGLS 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