NDX1_CAEEL
ID NDX1_CAEEL Reviewed; 365 AA.
AC O45830;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Putative nudix hydrolase 1;
DE EC=3.6.1.-;
GN Name=ndx-1; ORFNames=T26E3.2;
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; Z82053; CAB04835.1; -; Genomic_DNA.
DR PIR; T25296; T25296.
DR RefSeq; NP_493209.1; NM_060808.1.
DR AlphaFoldDB; O45830; -.
DR SMR; O45830; -.
DR BioGRID; 38535; 2.
DR DIP; DIP-26022N; -.
DR IntAct; O45830; 2.
DR STRING; 6239.T26E3.2; -.
DR iPTMnet; O45830; -.
DR EPD; O45830; -.
DR PaxDb; O45830; -.
DR PeptideAtlas; O45830; -.
DR EnsemblMetazoa; T26E3.2.1; T26E3.2.1; WBGene00003578.
DR GeneID; 173138; -.
DR KEGG; cel:CELE_T26E3.2; -.
DR UCSC; T26E3.2; c. elegans.
DR CTD; 173138; -.
DR WormBase; T26E3.2; CE14186; WBGene00003578; ndx-1.
DR eggNOG; KOG0648; Eukaryota.
DR GeneTree; ENSGT00390000002931; -.
DR HOGENOM; CLU_061042_0_0_1; -.
DR InParanoid; O45830; -.
DR OMA; PRYHWIP; -.
DR OrthoDB; 1327589at2759; -.
DR PhylomeDB; O45830; -.
DR Reactome; R-CEL-2393930; Phosphate bond hydrolysis by NUDT proteins.
DR PRO; PR:O45830; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00003578; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0016529; C:sarcoplasmic reticulum; HDA:WormBase.
DR GO; GO:0044715; F:8-oxo-dGDP phosphatase activity; IBA:GO_Central.
DR GO; GO:0044716; F:8-oxo-GDP phosphatase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; 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..365
FT /note="Putative nudix hydrolase 1"
FT /id="PRO_0000057133"
FT DOMAIN 72..201
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 109..130
FT /note="Nudix box"
FT BINDING 124
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 365 AA; 41641 MW; 9EF96D6054E9A6C9 CRC64;
MPLGKLDLVE EEYIAESGDH TPEASRLMGN GDSVVENLNG HTNGAVAKKK NEPRVPDMQL
GKCRYVRLHD NVNYVAAAII LRNQGDDTEV LLIQEAKKSC RGKWYMPAGR VEAGETIEEA
VVREVKEETG YSCDVVELLS LQVQGSGWYR YAFYCNITGG DLKTEPDQES LAAEWYNIKD
LKANKVQLRG RDFIRLVDEA VTYRTHGPVD SIPRVMPLNQ NVAGLFLEFM IVKHSRDGLR
TEVLVHKSIK DETYLLEEEQ PFPTVEFGFE YFFAMVVSKC YRHLLEEGAN VVFTPSHVTR
IKCHPKPMES LAHGVSIRVY CEHKQSASKA IIRSPRYHWI SVESPETRQR FHMAQKQFRP
SLHML
