ID   NPIIF_ARTGP             Reviewed;         372 AA.
AC   E4UYQ9;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Neutral protease 2 homolog MGYG_06241;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin MGYG_06241;
DE   Flags: Precursor;
GN   ORFNames=MGYG_06241;
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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; DS989826; EFR03239.1; -; Genomic_DNA.
DR   RefSeq; XP_003171693.1; XM_003171645.1.
DR   AlphaFoldDB; E4UYQ9; -.
DR   SMR; E4UYQ9; -.
DR   EnsemblFungi; EFR03239; EFR03239; MGYG_06241.
DR   GeneID; 10026947; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_1_0_1; -.
DR   InParanoid; E4UYQ9; -.
DR   OMA; RYNTWFG; -.
DR   OrthoDB; 1038868at2759; -.
DR   Proteomes; UP000002669; 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; 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..188
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407144"
FT   CHAIN           189..372
FT                   /note="Neutral protease 2 homolog MGYG_06241"
FT                   /id="PRO_0000407145"
FT   ACT_SITE        314
FT                   /evidence="ECO:0000250"
FT   BINDING         313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         317
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         328
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   DISULFID        195..264
FT                   /evidence="ECO:0000250"
FT   DISULFID        271..289
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   372 AA;  41382 MW;  46A27611F47AADCB CRC64;
     MQFFTAIAAI SALVAPALAL PTQELPQAPT NQTLHVRLIP TGNTMVKAVV TNNGDRPLNL
     LKFNTIMDEN PTAKVNVVHE DGEEVEFTGM LPRYSMRSLP KSVFTRLAPK DSVEHVFDIA
     TVHNLKRSGK YTLSARGAVP VAEGDDTAII DHVYYQSNDL TMEIDARKAA LIPRAFEDTH
     FAGTLNRRGG LNSTCSPRRY QVIKRALNDA RMIASSASKA VSSNPEKFRE FFGTTDPNAM
     KQVSERLMAI AQASVENGPI KWHCFDSRGR CEQNVVAYTL PSRNEVFPCM PFFTESDFTN
     KCHAQDKPTT LIHEAAHNPS VVQPFCRDHG YGYDHVSRLP PRLALQNADN YSIYAQGKFH
     LHLPLKVVFS PN