ID   NPIIE_ARTOC             Reviewed;         363 AA.
AC   C5FIT1;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Probable neutral protease 2 homolog MCYG_01991;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin MCYG_01991;
DE   Flags: Precursor;
GN   ORFNames=MCYG_01991;
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; DS995702; EEQ29172.1; -; Genomic_DNA.
DR   RefSeq; XP_002849057.1; XM_002849011.1.
DR   AlphaFoldDB; C5FIT1; -.
DR   SMR; C5FIT1; -.
DR   MEROPS; M35.001; -.
DR   EnsemblFungi; EEQ29172; EEQ29172; MCYG_01991.
DR   GeneID; 9229109; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_1_0_1; -.
DR   OMA; DVTFVHL; -.
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..189
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000388460"
FT   CHAIN           190..363
FT                   /note="Probable neutral protease 2 homolog MCYG_01991"
FT                   /id="PRO_0000388461"
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        197..268
FT                   /evidence="ECO:0000250"
FT   DISULFID        275..293
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   363 AA;  38446 MW;  AD09616ECAC8BA74 CRC64;
     MQLIATLSAL GALVATATAA AVPSAPVKQS VIDIQLSATG NTMIKATITN KGDQALNLLQ
     FNTILDKNPT RKVRVYQNGT EVKFTGMLAR YKMTGLSPDY FTTLSPKASV ESSFDIARTH
     DLTRGGKITV MASGTIPTAE GHGANGTTIT GYAKYESNKI ELDVDAKKAA SVVQAMGTVK
     KSPGSIDKRT NIDTSTCTQS QLDALEGALY NSAALAQAAA QAAPSNLDTV AEYFKSTSRR
     TINTIVSRLQ SVASESTYVN SGSTTYYCTD VMNGCQPGVL AYTLPDQNII TNCPIYYSDL
     PALAQSCHEQ DQATTTLHEM THNSAVVSPY CDDLGYGYED ATSLSAGQAI QNADTYALFA
     NVS