ID   NPIIB_ARTBC             Reviewed;         375 AA.
AC   D4ANL2;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Probable neutral protease 2 homolog ARB_05817;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin ARB_05817;
DE   Flags: Precursor;
GN   ORFNames=ARB_05817;
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: 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; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M35 family. {ECO:0000305}.
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DR   EMBL; ABSU01000003; EFE35773.1; -; Genomic_DNA.
DR   RefSeq; XP_003016418.1; XM_003016372.1.
DR   AlphaFoldDB; D4ANL2; -.
DR   SMR; D4ANL2; -.
DR   MEROPS; M35.002; -.
DR   EnsemblFungi; EFE35773; EFE35773; ARB_05817.
DR   GeneID; 9521901; -.
DR   KEGG; abe:ARB_05817; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_1_0_1; -.
DR   OMA; GTQTMWD; -.
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.
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; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..189
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397742"
FT   CHAIN           190..375
FT                   /note="Probable neutral protease 2 homolog ARB_05817"
FT                   /id="PRO_0000397743"
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"
FT   DISULFID        274..292
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   375 AA;  40633 MW;  0E2AACE5A6DE3742 CRC64;
     MQVIVALAAL GSLAAPALGF SIPRGVPVSQ SMIDVKLSST GNSMVKATIT NNGNRALNLL
     KFHTIMDSNP TRKVSIESED GKEIQFTGMM PTYKEKDLKP SYFISLPPKG TVEHSFDIAR
     THDLSRGGKF TLKAEGMVPI AEENGTEITG AAKYHSNELH MTIDGEKAAS VENAFGIVKR
     GPLTRINKRT SIDMQSCGNS QELQALTAAL KASAQLSSMS AQAVSQNQDK YMEYFKDPQY
     MQTVQSRFQA VAQESSSTTG GGTTYHCSDT MGGCEEGVLA YTLPSQNEVF NCPIYYSDLP
     PLSNECHAQD QATTTLHELT HNPAVQEPFC EDNGYGYERA TALSAEKAVQ NADSYALFAN
     GKLNLITLML IIDPD