NDX2_CAEEL
ID NDX2_CAEEL Reviewed; 223 AA.
AC O61902;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Putative nudix hydrolase 2;
DE EC=3.6.1.-;
GN Name=ndx-2; ORFNames=W02G9.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Probably mediates the hydrolysis of some nucleoside
CC diphosphate derivatives. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; FO081762; CCD74269.1; -; Genomic_DNA.
DR PIR; T33225; T33225.
DR RefSeq; NP_503726.1; NM_071325.3.
DR AlphaFoldDB; O61902; -.
DR SMR; O61902; -.
DR BioGRID; 53776; 2.
DR STRING; 6239.W02G9.1; -.
DR EPD; O61902; -.
DR PaxDb; O61902; -.
DR PeptideAtlas; O61902; -.
DR EnsemblMetazoa; W02G9.1.1; W02G9.1.1; WBGene00003579.
DR GeneID; 189126; -.
DR KEGG; cel:CELE_W02G9.1; -.
DR UCSC; W02G9.1; c. elegans.
DR CTD; 189126; -.
DR WormBase; W02G9.1; CE18314; WBGene00003579; ndx-2.
DR eggNOG; KOG3041; Eukaryota.
DR GeneTree; ENSGT00940000154045; -.
DR HOGENOM; CLU_062658_0_2_1; -.
DR InParanoid; O61902; -.
DR OMA; CNTNLHM; -.
DR OrthoDB; 1466354at2759; -.
DR PhylomeDB; O61902; -.
DR Reactome; R-CEL-2393930; Phosphate bond hydrolysis by NUDT proteins.
DR PRO; PR:O61902; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003579; Expressed in adult organism and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006753; P:nucleoside phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0019693; P:ribose phosphate metabolic process; IBA:GO_Central.
DR InterPro; IPR020476; Nudix_hydrolase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..223
FT /note="Putative nudix hydrolase 2"
FT /id="PRO_0000057134"
FT DOMAIN 72..213
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 111..132
FT /note="Nudix box"
FT BINDING 126
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 223 AA; 24251 MW; 7D7493ED8D7DEEEE CRC64;
MTSSATSPTN GVDKNKNEEM VATPANCPYQ LFNQEVVWNG KWIQTRQVGF KTHTGQVGVW
QSVHRNTKPV EASADGVSII ARVRKQGKLY IVLVKQYRIP CGKLCLELPA GLIDAGETAQ
QAAIRELKEE TGYVSGKVVM ESKLCFLDPG LTDDSQCLVV VDVDGDAPEN QNPVQVLDST
ESIEVLLVEQ SALMAYVTNL DSSSIVVEST LLAYAMGIQF ATI
