ID   NPIIB_UNCRE             Reviewed;         357 AA.
AC   C4JK49;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Neutral protease 2 homolog UREG_02006;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin UREG_02006;
DE   Flags: Precursor;
GN   ORFNames=UREG_02006;
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; EEP77157.1; -; Genomic_DNA.
DR   RefSeq; XP_002542490.1; XM_002542444.1.
DR   AlphaFoldDB; C4JK49; -.
DR   SMR; C4JK49; -.
DR   PRIDE; C4JK49; -.
DR   EnsemblFungi; EEP77157; EEP77157; UREG_02006.
DR   GeneID; 8440442; -.
DR   KEGG; ure:UREG_02006; -.
DR   VEuPathDB; FungiDB:UREG_02006; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_1_1_1; -.
DR   InParanoid; C4JK49; -.
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.
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..179
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407132"
FT   CHAIN           180..357
FT                   /note="Neutral protease 2 homolog UREG_02006"
FT                   /id="PRO_0000407133"
FT   ACT_SITE        309
FT                   /evidence="ECO:0000250"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         312
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         323
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   DISULFID        187..259
FT                   /evidence="ECO:0000250"
FT   DISULFID        266..284
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   357 AA;  38434 MW;  495A489C1869F26C CRC64;
     MLFSSRFLAL AALLGQALAL PIDDFSQSDA GLKVKLTSMG NTRVKAVVTN EGEQEISFLK
     FNTFFDSAPT QKVQIMKAGS LIPFSGVDFY FNMANLPAEA FKTLAPGASA EAEFDIAATA
     DLSPGGSYTV SSAGFLRIAG GNGTAITGRM RYRSNQMKLN VDGDMAAKVQ SAVPTIEKRT
     RIDGNSCRGN YGQLLSRALQ GCSSYAGRAA QAASNGDAQK FQEYFKTNSP QVRQSVAARF
     QAIVQECSSA SNGKTTYLCE DRFRFCQPGL IAYTIPTQSV VANCPSYWKL PPVVNRGLEP
     DHGYVVVHEF THATSIFSPG TEDHGYGYEE CRRLNAQQSL SNADNYSLFA AAVSRGA