ID   NPIIA_UNCRE             Reviewed;         356 AA.
AC   C4JLQ3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Neutral protease 2 homolog UREG_03761;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin UREG_03761;
DE   Flags: Precursor;
GN   ORFNames=UREG_03761;
OS   Uncinocarpus reesii (strain UAMH 1704).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX   NCBI_TaxID=336963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 1704;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC       proteinaceous substrates. Shows high activities on basic nuclear
CC       substrates such as histone and protamine (By similarity).
CC       {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; CH476616; EEP78915.1; -; Genomic_DNA.
DR   RefSeq; XP_002544244.1; XM_002544198.1.
DR   AlphaFoldDB; C4JLQ3; -.
DR   SMR; C4JLQ3; -.
DR   EnsemblFungi; EEP78915; EEP78915; UREG_03761.
DR   GeneID; 8444137; -.
DR   KEGG; ure:UREG_03761; -.
DR   VEuPathDB; FungiDB:UREG_03761; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_1_1_1; -.
DR   InParanoid; C4JLQ3; -.
DR   OrthoDB; 1038868at2759; -.
DR   BRENDA; 3.4.24.39; 8258.
DR   Proteomes; UP000002058; 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; IPR029463; Lys_MEP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001384; Peptidase_M35.
DR   Pfam; PF02102; Peptidase_M35; 1.
DR   PRINTS; PR00768; DEUTEROLYSIN.
DR   SMART; SM01351; Aspzincin_M35; 1.
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; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..181
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407116"
FT   CHAIN           182..356
FT                   /note="Neutral protease 2 homolog UREG_03761"
FT                   /id="PRO_0000407117"
FT   ACT_SITE        309
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         312
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   DISULFID        189..259
FT                   /evidence="ECO:0000250"
FT   DISULFID        266..284
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   356 AA;  38395 MW;  51FCE35FEC869EC5 CRC64;
     MRFSSSFLSV LALASQALAF PLNDLPTTDS GLEVKLTSVG NTRMKAVLTN TADHDLSFLK
     FNTFFDDAPT QKVRIAKDGS LVPFNGIHRY YNIDDLPQEA FIPLAPGESV EAEFDIAETS
     DLSAGGSYKI FASGVIPIVA GPGIKVTSAV SFSTDEMTVD VDGAEAAQVQ SALPEATLDK
     RTRIDRNTCT GNYYNALARA LQTAAGYASR AAQAAQAGNR FQEFFKTTSP QVRQNVAARF
     SAIAQECRSP SGGRTTYHCQ DVYRACQQGI IAYTIPARSA VVNCPPYWRL PAVVNQGFAP
     DMGYVVVHEF AHAPSIFRPG TVDHAYGYAQ CVRLNSQQAL SNADNYALFA AAASRR