ID   NPIIC_ARTBC             Reviewed;         356 AA.
AC   D4AM79;
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_04769;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin ARB_04769;
DE   Flags: Precursor;
GN   ORFNames=ARB_04769;
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; ABSU01000002; EFE35835.1; -; Genomic_DNA.
DR   RefSeq; XP_003016480.1; XM_003016434.1.
DR   AlphaFoldDB; D4AM79; -.
DR   SMR; D4AM79; -.
DR   MEROPS; M35.001; -.
DR   EnsemblFungi; EFE35835; EFE35835; ARB_04769.
DR   GeneID; 9521962; -.
DR   KEGG; abe:ARB_04769; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_1_0_1; -.
DR   OMA; NTIMDEH; -.
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; Glycoprotein;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Secreted; Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..183
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397746"
FT   CHAIN           184..356
FT                   /note="Probable neutral protease 2 homolog ARB_04769"
FT                   /id="PRO_0000397747"
FT   ACT_SITE        312
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         326
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        205
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        191..262
FT                   /evidence="ECO:0000250"
FT   DISULFID        269..287
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   356 AA;  38323 MW;  CE1F3872A6FF1877 CRC64;
     MQFTALLAAL GAPLALAASI PAAAHNHSMI DVQLAATGNS MIKATITNTG DRTLNLLKFN
     TIMDEHPTRK VMVYQDGAEV QFTGMLPRYK MSDLTPEYFV NLGPKASVEH SFDLAATHDL
     SRGGKIVVKA HGMVPTAEEN ATTITGHTLY ESNELTMDVD GKQAAAVEQA MGGDDSTGVI
     DKRSNIVTSS CRGSQLRVLQ TALSNASRLS RAAASAAQRN PSKMREYFKT ADSRTVQKVA
     SRFLSVARES SSGSTGRTTY YCNDNRGGCH PGVLAYTLPS KNQVFNCPSY YQLPALNNRC
     HGQDQATTTL HELTHNPAVV TPFCEDLGYG YQRVSALPAS KAIQNADTYS LFANGM