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 27-MAR-2024, entry version 52.
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 STRING; 336963.C4JH04; -.
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 OMA; YWFQFPA; -.
DR OrthoDB; 1331996at2759; -.
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 CDD; cd11008; M35_deuterolysin_like; 1.
DR Gene3D; 2.60.40.2970; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001384; Peptidase_M35.
DR PANTHER; PTHR37016; -; 1.
DR PANTHER; PTHR37016:SF3; NEUTRAL PROTEASE 2 HOMOLOG AN3393-RELATED; 1.
DR Pfam; PF02102; Peptidase_M35; 1.
DR PRINTS; PR00768; DEUTEROLYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 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..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
//
