ID   NPIIB_TRIVH             Reviewed;         374 AA.
AC   D4DE03;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Probable neutral protease 2 homolog TRV_05367;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin TRV_05367;
DE   Flags: Precursor;
GN   ORFNames=TRV_05367;
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ACYE01000281; EFE39920.1; -; Genomic_DNA.
DR   RefSeq; XP_003020538.1; XM_003020492.1.
DR   AlphaFoldDB; D4DE03; -.
DR   SMR; D4DE03; -.
DR   MEROPS; M35.002; -.
DR   EnsemblFungi; EFE39920; EFE39920; TRV_05367.
DR   GeneID; 9577237; -.
DR   KEGG; tve:TRV_05367; -.
DR   HOGENOM; CLU_039313_1_0_1; -.
DR   Proteomes; UP000008383; 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; 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_0000397744"
FT   CHAIN           190..374
FT                   /note="Probable neutral protease 2 homolog TRV_05367"
FT                   /id="PRO_0000397745"
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   374 AA;  40607 MW;  759C89DAFAB5C67E CRC64;
     MQVIVALAAL GSLAAPALGF SIPRGVPVSQ SMIDVKLSST GNSMVKATIT NNGNRALNLL
     KFHTIMDSNP TRKVSIESED GKEIQFTGMM PTYKEKDLKP SYFIFLPPKG TVEHSFDIAR
     THDLSRGGKF TLKAEGMVPI AEENGTEITG AAKYHSNELH MTIDGEKAAS VENAFGIVKR
     GPLTRINKRT SIDMQSCGNN QELQALTAAL KASAQLSSMS AQAVSQNQDK YMEYFKDPQY
     MQTVQSRFQA VAQESSSTTG GGTTYHCSDT MGGCEEGVLA YTLPSQNEVF NCPIYYSDLP
     PLSNECHAQD QATTTLHELT HNPAVQEPFC EDNGYGYERA TALSAEKAVQ NADSYALFAN
     GKLNLITLML IDPD