ID   NPIIC_UNCRE             Reviewed;         360 AA.
AC   C4JH04;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Neutral protease 2 homolog UREG_01255;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin UREG_01255;
DE   Flags: Precursor;
GN   ORFNames=UREG_01255;
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; CH476615; EEP76406.1; -; Genomic_DNA.
DR   RefSeq; XP_002541739.1; XM_002541693.1.
DR   AlphaFoldDB; C4JH04; -.
DR   SMR; C4JH04; -.
DR   EnsemblFungi; EEP76406; EEP76406; UREG_01255.
DR   GeneID; 8444615; -.
DR   KEGG; ure:UREG_01255; -.
DR   VEuPathDB; FungiDB:UREG_01255; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_1_1_1; -.
DR   InParanoid; C4JH04; -.
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; 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; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..182
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407138"
FT   CHAIN           183..360
FT                   /note="Neutral protease 2 homolog UREG_01255"
FT                   /id="PRO_0000407139"
FT   ACT_SITE        312
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         311
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         326
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   DISULFID        190..262
FT                   /evidence="ECO:0000250"
FT   DISULFID        269..287
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   360 AA;  38571 MW;  A421E288454EE8FC CRC64;
     MYIRSALLAL AALAGQALAF PLNSLPERDN AGLDIQLSST GNTRVKAVIT NNGDEAMSFV
     KFNTLFDSSM VRKVKISKDG SAVPFTGIFG YYDINNLPKE AFATLSPGAS LEAEFDIAET
     ADLSEGGSFK VSADGLLPIA ATKGSTKVDG AIQFKSNELT IDIDGDEAAK VHASVMSTLG
     KRSRVDGRTC QGRAGQIIVN SLRSCVGYAQ AAAQGAANGD AQKFQEYFKT TSPQVRQNVA
     RRFQAIAQEC SSPSQGRSIV FCQDVYGYCQ RGLIAYTVFA NSHVATCPDF YRLPARVNQG
     LGPDHGYVMV HELTHAPAVF SPYTQDYAYG YQQCRRLNAQ QSLGNADNYS LFAAAVARGA