ID   NPIIF_TRIVH             Reviewed;         379 AA.
AC   D4D7X4;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Neutral protease 2 homolog TRV_03208;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin TRV_03208;
DE   Flags: Precursor;
GN   ORFNames=TRV_03208;
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: 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; ACYE01000164; EFE42069.1; -; Genomic_DNA.
DR   RefSeq; XP_003022687.1; XM_003022641.1.
DR   AlphaFoldDB; D4D7X4; -.
DR   SMR; D4D7X4; -.
DR   EnsemblFungi; EFE42069; EFE42069; TRV_03208.
DR   GeneID; 9581346; -.
DR   KEGG; tve:TRV_03208; -.
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.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Signal;
KW   Virulence; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..187
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407146"
FT   CHAIN           188..379
FT                   /note="Neutral protease 2 homolog TRV_03208"
FT                   /id="PRO_0000407147"
FT   ACT_SITE        313
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         316
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         327
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        193..263
FT                   /evidence="ECO:0000250"
FT   DISULFID        270..288
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   379 AA;  42130 MW;  4E1AB840CF6CD71F CRC64;
     MKFFTALAAV GALLAPALAL PTPASEEASH NQTLSVRLVP AGHTMVRAIV TNNGERPLHL
     LSFNTILDED PTSKVEVFHE SGDEAEFLGM LPRYDLSDLT EDLFTRLAPK DSVEHLFDIA
     TVHDLKWDGK YTLAARGAIP VAEDGGTTII DHVYYESNEL DMEIDARKAA MVPRAFDDYF
     SKSLDKRRPL DICNPRKERD LRAALEGAQQ VAKEAAAAAQ NNTEKVFEFF RARDPGTRKE
     VSQHLSSISR AATKDGSSVT WFCSDGPGRC GPRTIAYTFP AKNEVHPCPL FWQMPHVNNK
     CHRQDRVGTV IHEGAHNPSV VTPYCKDLGY GYNRATGLTS QRAKRNADNY ALFAMARQLV
     FCLLHLFVAL PFIYIFASF