NDX7_CAEEL
ID NDX7_CAEEL Reviewed; 295 AA.
AC P91148;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Putative nudix hydrolase 7;
DE EC=3.6.1.-;
GN Name=ndx-7; ORFNames=C43E11.7;
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; FO080612; CCD65159.1; -; Genomic_DNA.
DR PIR; F87753; F87753.
DR RefSeq; NP_491336.2; NM_058935.6.
DR AlphaFoldDB; P91148; -.
DR SMR; P91148; -.
DR BioGRID; 48240; 3.
DR STRING; 6239.C43E11.7; -.
DR EPD; P91148; -.
DR PaxDb; P91148; -.
DR PeptideAtlas; P91148; -.
DR EnsemblMetazoa; C43E11.7.1; C43E11.7.1; WBGene00003584.
DR GeneID; 183413; -.
DR KEGG; cel:CELE_C43E11.7; -.
DR UCSC; C43E11.7.1; c. elegans.
DR CTD; 183413; -.
DR WormBase; C43E11.7; CE30504; WBGene00003584; ndx-7.
DR eggNOG; KOG3904; Eukaryota.
DR GeneTree; ENSGT00420000029858; -.
DR HOGENOM; CLU_1062590_0_0_1; -.
DR InParanoid; P91148; -.
DR OMA; HETVFFM; -.
DR OrthoDB; 1417901at2759; -.
DR PhylomeDB; P91148; -.
DR Reactome; R-CEL-390918; Peroxisomal lipid metabolism.
DR Reactome; R-CEL-9033241; Peroxisomal protein import.
DR PRO; PR:P91148; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00003584; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR039121; NUDT19.
DR PANTHER; PTHR12318; PTHR12318; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..295
FT /note="Putative nudix hydrolase 7"
FT /id="PRO_0000057137"
FT DOMAIN 9..182
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 52..73
FT /note="Nudix box"
FT BINDING 67
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 295 AA; 33500 MW; B2005132EC827147 CRC64;
MCIGKVTSSW RSAASIILAC KTTRRVLMLK RGTTAKFMPN TMVFPGGVVD KTDAKLGDEF
RIAAVRELFE ESGVLSTKNG WQTSANNPDM TSLKADIVND TSKFEQLSGT ICADNLIEWD
TFITPANYPR RFLTKFYLML VDDEPAIDLC TSEMSEYNWI EPKECVDEAY AGKYALPPPQ
VYELTRLSQV KDWDLCEKYG NVKKPICPQP IKTIGENLIT NCFPGDYMYI DENSLQQPLR
QMSADRVTVD PTQPTHRATY YSEPMYGKVR LYQHLLKPAD IAAFHQFDTH SKDLL