ID   NPIIA_ARTGP             Reviewed;         366 AA.
AC   E4UUX3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Neutral protease 2 homolog MGYG_04094;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin MGYG_04094;
DE   Flags: Precursor;
GN   ORFNames=MGYG_04094;
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; DS989824; EFR01090.1; -; Genomic_DNA.
DR   RefSeq; XP_003173920.1; XM_003173872.1.
DR   AlphaFoldDB; E4UUX3; -.
DR   SMR; E4UUX3; -.
DR   MEROPS; M35.001; -.
DR   EnsemblFungi; EFR01090; EFR01090; MGYG_04094.
DR   GeneID; 10029207; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_1_0_1; -.
DR   InParanoid; E4UUX3; -.
DR   OMA; DVTFVHL; -.
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..188
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407084"
FT   CHAIN           189..366
FT                   /note="Neutral protease 2 homolog MGYG_04094"
FT                   /id="PRO_0000407085"
FT   ACT_SITE        318
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         317
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         321
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         332
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   DISULFID        196..267
FT                   /evidence="ECO:0000250"
FT   DISULFID        274..292
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   366 AA;  39130 MW;  1A87BE5A88FB8208 CRC64;
     MQILAALSAI GALVATATAA AVPNAPAKQS MIDIQLSATG NTLIKATITN KGDKALNLLQ
     FNTILDKNPT RKVRVYQNGT EVKFTGMLAR YKMSNLSPDY FTTLGPKSSV ESTFDIARTH
     DLTRGGKITV MASGTIPTAE GHGNGTSITG YARYESNKLE LDVDAKKASS VAQAMGKVNK
     SRSTIDKRTN IDTSSCSQSQ LEALEGALYN SAALAQAAAE AAPQSTDTVA EFFKSTSRNT
     IKTLVSRFQS VARESTYVND GRTTYYCTDS MNGCSPGVLA YTLPDQNLIF NCPIYYSDLP
     PLAQSCYEQD QATTTLHEMT HNSAVVSPFC DDLGYGYDDA TSLSASQALQ NADSYALFAN
     AIYLGC