ID   NPIIC_ARTGP             Reviewed;         358 AA.
AC   E4UR63;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Neutral protease 2 homolog MGYG_02351;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin MGYG_02351;
DE   Flags: Precursor;
GN   ORFNames=MGYG_02351;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS989823; EFQ99338.1; -; Genomic_DNA.
DR   RefSeq; XP_003174821.1; XM_003174773.1.
DR   AlphaFoldDB; E4UR63; -.
DR   SMR; E4UR63; -.
DR   MEROPS; M35.001; -.
DR   EnsemblFungi; EFQ99338; EFQ99338; MGYG_02351.
DR   GeneID; 10030122; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_1_0_1; -.
DR   InParanoid; E4UR63; -.
DR   OMA; NTIMDEH; -.
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..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..183
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407134"
FT   CHAIN           184..358
FT                   /note="Neutral protease 2 homolog MGYG_02351"
FT                   /id="PRO_0000407135"
FT   ACT_SITE        310
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         309
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         324
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   DISULFID        191..260
FT                   /evidence="ECO:0000250"
FT   DISULFID        267..285
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   358 AA;  38654 MW;  5D0A4D1E94D5A372 CRC64;
     MQFVALLAAL GAPLALAASI PAAHNNSSII DVKLAATGNS MIKAIITNNG DRTLNLLKFN
     TIMDEHPTRK VKVYQDGAEV QFTGMLPRYK MSDLTPDFFV NLGPKASVEH SFDLAATHDL
     SRGGKITVSA NGVVPTAEEN ETTITGHTHY ESNELTMDVD GKEAAAVEQS MGGDSPAGVI
     DKRSNIVTSS CRGNQLQMLK TALANSARLS KAAASAAQRN PRKFQEYFKT TDSSTVQKVV
     SRFMSVARES TSTGKTTYYC NDTRDGCKPG VLAYTLPSKN QVFNCPSYYK LPALNNRCHG
     QDMATTTLHE LTHNPAVVTP FCEDLGYGYD RVSRLPASKA VQNADTYSLF ANAVYLGC