ID   NPIIB_ARTOC             Reviewed;         367 AA.
AC   C5FCA7;
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_00239;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin MCYG_00239;
DE   Flags: Precursor;
GN   ORFNames=MCYG_00239;
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; DS995701; EEQ27351.1; -; Genomic_DNA.
DR   RefSeq; XP_002850135.1; XM_002850089.1.
DR   AlphaFoldDB; C5FCA7; -.
DR   SMR; C5FCA7; -.
DR   MEROPS; M35.001; -.
DR   EnsemblFungi; EEQ27351; EEQ27351; MCYG_00239.
DR   GeneID; 9225115; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_1_0_1; -.
DR   OMA; GTQTMWD; -.
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..190
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000388454"
FT   CHAIN           191..367
FT                   /note="Probable neutral protease 2 homolog MCYG_00239"
FT                   /id="PRO_0000388455"
FT   ACT_SITE        319
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         322
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         333
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   DISULFID        198..268
FT                   /evidence="ECO:0000250"
FT   DISULFID        275..293
FT                   /evidence="ECO:0000250"
FT   DISULFID        307..367
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   367 AA;  39737 MW;  23C76D5110C4E743 CRC64;
     MQVLVALAAL SSLAAPVVGF SIPRGVPVSQ SMIDVKLSSA GNSMVKATIT NNGDRALNLL
     KFHTIMDSNP TRKVSIESQD GKEVQFTGMM PRYKNTDLKP TYFMSLPPKG TVEHSFDIAA
     THDLSRGGQF TLKAEGMVPI AEENSTNITG AAQYHSNELH MTIDGDQAAS VKSAIGVAKR
     DGPFTRIDKR TKIDMQSCGN RQELQALTAA LSASAKLSSM SAQAVGQNQQ KYMEYFKDPK
     YAKTVQSRFQ AVAKESSSTN NGGTTYFCSD VMGGCEEGVL AYTLPSRNQV YNCPIYYSEL
     PPLTKECHAQ DQATTTLHEL THNPAVQEPF CEDNGYGYER ATALSAEKAV QNADSYALFA
     NAVYVGC