ID   NPIIC_ARTOC             Reviewed;         360 AA.
AC   C5FPC2;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Probable neutral protease 2 homolog MCYG_04257;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin MCYG_04257;
DE   Flags: Precursor;
GN   ORFNames=MCYG_04257;
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480;
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: 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; DS995704; EEQ31438.1; -; Genomic_DNA.
DR   RefSeq; XP_002846520.1; XM_002846474.1.
DR   AlphaFoldDB; C5FPC2; -.
DR   SMR; C5FPC2; -.
DR   MEROPS; M35.001; -.
DR   EnsemblFungi; EEQ31438; EEQ31438; MCYG_04257.
DR   GeneID; 9224590; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_1_0_1; -.
DR   OMA; NTIMDEH; -.
DR   OrthoDB; 1038868at2759; -.
DR   Proteomes; UP000002035; 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..182
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000388456"
FT   CHAIN           183..360
FT                   /note="Probable neutral protease 2 homolog MCYG_04257"
FT                   /id="PRO_0000388457"
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        262
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        190..261
FT                   /evidence="ECO:0000250"
FT   DISULFID        268..286
FT                   /evidence="ECO:0000250"
FT   DISULFID        300..360
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   360 AA;  38421 MW;  D214C6F79453B076 CRC64;
     MQLIAFLAAL GVPVAFAATI PSVPLNHSMI DVKLSAAGNS MVKATITNNG DRALNLLRFN
     TIMDEHPTRK VMVYQNGAEV QFTGMLPRYM MSNLTPDYFV SLGPKASVEH SFDLAATHDL
     SRGGKITVMA QGTVPTAEEH GTTITGHTVY ESNKITMEVD GNKAAAVVQA MGKVKAGSID
     KRSKVVTSSC HGNQLQVLQT ALANSARLSQ AAAKAAQSNP RKLQEYFKAT DSGTVQKVVS
     RFMSVARESS SNSAGGTTYY CNDSMGGCHP GVLAYTLPSQ NLVVNCPIYY SDIPALNKRC
     HGQDQATTTL HEFTHNPAVV SPFAQDLGYG YDRVAALPAS KAIQNADTYA LFANAIYVGC