ID   NPIIB_ARTGP             Reviewed;         375 AA.
AC   E5R1Z3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Neutral protease 2 homolog MGYG_00813;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin MGYG_00813;
DE   Flags: Precursor;
GN   ORFNames=MGYG_00813;
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; DS989822; EFQ97772.1; -; Genomic_DNA.
DR   RefSeq; XP_003176724.1; XM_003176676.1.
DR   AlphaFoldDB; E5R1Z3; -.
DR   SMR; E5R1Z3; -.
DR   MEROPS; M35.001; -.
DR   EnsemblFungi; EFQ97772; EFQ97772; MGYG_00813.
DR   GeneID; 10032046; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_1_0_1; -.
DR   InParanoid; E5R1Z3; -.
DR   OMA; GTQTMWD; -.
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.
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_0000407120"
FT   CHAIN           191..375
FT                   /note="Neutral protease 2 homolog MGYG_00813"
FT                   /id="PRO_0000407121"
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"
SQ   SEQUENCE   375 AA;  40677 MW;  37CEE6E5580BD521 CRC64;
     MQVIVALAAL SSLAAPALGF SIPRGVPVSQ SMIDVKLSAA GNSMVKATIT NNGDRALNLL
     KFHTIMDSNP TRKVTIESQD GKEVQFTGMM PRYKHTDLKP TYFISLPPKG TVEHSFDIAS
     THDLSRGGKF TLKAEGMVPL AEENGTTITG AAKYNSNELH MDIDGNKAAS VERAMGIVKR
     SGPLTRIGKR TSIDMQSCSN RQELQALTAA LRASAQLSSM AAQAVQQNQE KYMEYFKDPQ
     YAQTVQSRFQ SVAQESSSTS GGGTTYHCTD LMNGCEQGVL AYTLPSQNEV FNCPIYYSDL
     PPLSNECHAQ DQATTTLHEL THNPAVQEPF CEDNGYGYER ATALSAEKAV QNADSYALFA
     NGKFLPMSSM LVTQD