ID   NPIIA_ARTOC             Reviewed;         373 AA.
AC   C5FR79;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Probable neutral protease 2 homolog MCYG_05201;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin MCYG_05201;
DE   Flags: Precursor;
GN   ORFNames=MCYG_05201;
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; DS995705; EEQ32382.1; -; Genomic_DNA.
DR   RefSeq; XP_002845332.1; XM_002845286.1.
DR   AlphaFoldDB; C5FR79; -.
DR   SMR; C5FR79; -.
DR   MEROPS; M35.001; -.
DR   EnsemblFungi; EEQ32382; EEQ32382; MCYG_05201.
DR   GeneID; 9230288; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_1_0_1; -.
DR   OMA; QYCTDVY; -.
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; 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..187
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000388452"
FT   CHAIN           188..373
FT                   /note="Probable neutral protease 2 homolog MCYG_05201"
FT                   /id="PRO_0000388453"
FT   ACT_SITE        315
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         314
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         318
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         329
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   DISULFID        195..265
FT                   /evidence="ECO:0000250"
FT   DISULFID        272..290
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   373 AA;  40217 MW;  8CD21163BE19D636 CRC64;
     MQFFTALAAV GALVAPALAL PTQVPANQSL IDVQLSATGN SMIKAVITNK GTRALNLLKF
     NTIMDENPTA KVMVFDKNGA EVEFTGMLPR YDMNSLSTDY FATLAPQASV EHSFDIAATH
     NIKESGKYTL SAHGLIPTAE EHGTTITGQA FYESNTLEME IDASKAAMVP RAFEELDAHI
     VGTIDKRSGI VTSSCDASQL RIVKQALANS RMLALNAARA ASSNPSKVRE YFGSSDSSIM
     QKVASRFQSV ARESTASGGQ TTYHCTDNRG SCKPGVLAYT LPSTNTVYNC PSYYREPSLT
     KRCHAQDQAT TTLHELTHNP VVVSPFCKDL GYGYRLATGL PTSKAIQNAD NYALFANEES
     SPVFFVPVFY SNG