ID   NPIID_TRIVH             Reviewed;         370 AA.
AC   D4D616;
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_02539;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin TRV_02539;
DE   Flags: Precursor;
GN   ORFNames=TRV_02539;
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}.
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DR   EMBL; ACYE01000131; EFE42695.1; -; Genomic_DNA.
DR   RefSeq; XP_003023313.1; XM_003023267.1.
DR   AlphaFoldDB; D4D616; -.
DR   SMR; D4D616; -.
DR   MEROPS; M35.001; -.
DR   EnsemblFungi; EFE42695; EFE42695; TRV_02539.
DR   GeneID; 9583332; -.
DR   KEGG; tve:TRV_02539; -.
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..188
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000397752"
FT   CHAIN           189..370
FT                   /note="Probable neutral protease 2 homolog TRV_02539"
FT                   /id="PRO_0000397753"
FT   ACT_SITE        317
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         316
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         320
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         331
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   DISULFID        196..267
FT                   /evidence="ECO:0000250"
FT   DISULFID        274..292
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   370 AA;  40033 MW;  BF666AD52D074A81 CRC64;
     MQLVAALAAL GALVAPAVAY PHAPMNETLV DVQLTAVGNT MVKATITNKG DSVLNMLKFN
     TIMDENPTRK VMVFQDGAEV PFTGMMPRYL MSDLTEEFFT TLAPQASVEH SFDIATTHDL
     SAGGKYVISA SGAIPTAEEY STTITSTALY ESNELHMEID GTQAAAVEQA MKFTPEMQSI
     HSRALQKRTK IVGGSCNQNT LRATQNALGN SARLAQAASR AASQNAAKFQ EYFRTNDANA
     KQRVIARLNS VARESSSANG GSTTYYCSDT VGGCKPRVLA YTLPSRNLVV NCPIYYNLPP
     LTKQCHAQDQ ATTTLHEFTH NPAVASPHCQ DYAYGYQQCI SLPAAKAVQN ADNYALFANG
     MFYSLFTIIF