ID   NPIIF_ARTBC             Reviewed;         378 AA.
AC   D4AJ87;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Neutral protease 2 homolog ARB_04336;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin ARB_04336;
DE   Flags: Precursor;
GN   ORFNames=ARB_04336;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(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. May be involved in virulence
CC       (By similarity). {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; ABSU01000001; EFE36810.1; -; Genomic_DNA.
DR   RefSeq; XP_003017455.1; XM_003017409.1.
DR   AlphaFoldDB; D4AJ87; -.
DR   SMR; D4AJ87; -.
DR   EnsemblFungi; EFE36810; EFE36810; ARB_04336.
DR   GeneID; 9524565; -.
DR   KEGG; abe:ARB_04336; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_1_0_1; -.
DR   OMA; RYNTWFG; -.
DR   Proteomes; UP000008866; 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.
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; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..186
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407142"
FT   CHAIN           187..378
FT                   /note="Neutral protease 2 homolog ARB_04336"
FT                   /id="PRO_0000407143"
FT   ACT_SITE        312
FT                   /evidence="ECO:0000250"
FT   BINDING         311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         326
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   DISULFID        192..262
FT                   /evidence="ECO:0000250"
FT   DISULFID        269..287
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   378 AA;  41956 MW;  FDD569145E7D3801 CRC64;
     MKFFTALAAV GALLAPAVAL PTPASEASHN QTLSVRLVRA GHTMVRAIVT NNGERPLHLL
     SFNTIMDENP TSKVDVSHED GGEVEFLGML PRYDLSDLTE DLFTRLAPKD SVEHLFDIAT
     VHDLKWDGKY TLTARGAIPV AEDGGTDIID HVYYESNALE MDIDARKAAM VPRAFDDYFS
     KGLDKRRPLD ICNPMKEKAL RAALQDAQKV ATEAAAAAQN NTEKVFEFFR ARDPGTRKEV
     SKRLASISGV ATMDGGSVTW FCSDGPRRCS PRIIAYTFPA RNEVHPCSLF WQLPHRTNEC
     HRQDRIGTVI HEGAHNPNAV TPHCKDHGYG YNRATALSHQ RAMGNADNYA LFANARQLVF
     CLLHLFLALP FIYIFANF