ID   NPIIB_TRIRU             Reviewed;         366 AA.
AC   C0IPP2;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Probable neutral protease 2 homolog B;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin B;
DE   Flags: Precursor;
GN   Name=NpII-B;
OS   Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=5551;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Monod M., Lechenne B., Zaugg C.;
RT   "Trichophyton rubrum secreted neutral proteases II.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable secreted metalloprotease that shows high activities
CC       on basic nuclear substrates such as histone and protamine (By
CC       similarity). May be involved in virulence. {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;
CC         Evidence={ECO:0000250|UniProtKB:P46076};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P46076};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M35 family. {ECO:0000305}.
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DR   EMBL; EU445235; ACC65886.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0IPP2; -.
DR   SMR; C0IPP2; -.
DR   MEROPS; M35.001; -.
DR   VEuPathDB; FungiDB:TERG_00673; -.
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; Secreted; Signal; Virulence;
KW   Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..189
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000388464"
FT   CHAIN           190..366
FT                   /note="Probable neutral protease 2 homolog B"
FT                   /id="PRO_0000388465"
FT   ACT_SITE        318
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         317
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         321
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         332
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   DISULFID        197..267
FT                   /evidence="ECO:0000250|UniProtKB:P46076"
FT   DISULFID        274..292
FT                   /evidence="ECO:0000250|UniProtKB:P46076"
FT   DISULFID        306..366
FT                   /evidence="ECO:0000250|UniProtKB:P46076"
SQ   SEQUENCE   366 AA;  39618 MW;  4268FBEA098D18F1 CRC64;
     MQVIVALAAL SSLAAPALGF SIPRGVPVSQ SMIDVKLSAT GNSMVKATIT NNGNRALNLL
     KFHTIMDSNP TRKVSIESED GKEIQFTGMM PTYKEKDLKP SYFISLPPKG TVEHSFDIAR
     THDLSRGGKF TLKAEGMVPI AEENGTEITG AAKYHSNELH MTIDGEKAAS VENAFGIVKR
     GPRSRITKRT SIDMQSCGNS QELQALTAAL KASAQLSSMS AQAVSQNQDK YMEYFKDPQY
     MQTVQSRFQA VAQESSSTTG GGTTYHCSDT MGGCEEGVLA YTLPSQNEVF NCPIYYSDLP
     PLSNECHAQD QATTTLHELT HNPAVQEPFC EDNGYGYERA TALSAEKAVQ NADSYALFAN
     AIYVGC