ID   NUDT6_XENLA             Reviewed;         217 AA.
AC   P13420;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Nucleoside diphosphate-linked moiety X motif 6;
DE            Short=Nudix motif 6;
DE            EC=3.6.1.-;
DE   AltName: Full=Protein GFG;
GN   Name=nudt6;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Oocyte;
RX   PubMed=2479540; DOI=10.1002/j.1460-2075.1989.tb08448.x;
RA   Volk R., Koester M., Poeting A., Hartmann L., Knoechel W.;
RT   "An antisense transcript from the Xenopus laevis bFGF gene coding for an
RT   evolutionarily conserved 24 kd protein.";
RL   EMBO J. 8:2983-2988(1989).
RN   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=8660369; DOI=10.1006/bbrc.1996.0839;
RA   Li A.W., Too C.K., Murphy P.R.;
RT   "The basic fibroblast growth factor (FGF-2) antisense RNA (GFG) is
RT   translated into a MutT-related protein in vivo.";
RL   Biochem. Biophys. Res. Commun. 223:19-23(1996).
CC   -!- FUNCTION: May contribute to the regulation of cell proliferation.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Mitochondrion {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC       {ECO:0000269|PubMed:8660369}.
CC   -!- MISCELLANEOUS: This protein is coded from a FGF2 (BFGF) gene antisense
CC       transcript.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR   EMBL; X16627; CAA34623.1; -; mRNA.
DR   RefSeq; XP_018124454.1; XM_018268965.1.
DR   AlphaFoldDB; P13420; -.
DR   SMR; P13420; -.
DR   DNASU; 380230; -.
DR   GeneID; 380230; -.
DR   CTD; 380230; -.
DR   Xenbase; XB-GENE-865534; nudt6.L.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 380230; Expressed in neurula embryo and 19 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR003293; Nudix_hydrolase6-like.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR040618; Pre-Nudix.
DR   PANTHER; PTHR13994; PTHR13994; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   Pfam; PF18290; Nudix_hydro; 1.
DR   PRINTS; PR01356; GFGPROTEIN.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Mitochondrion; Nucleus; Reference proteome.
FT   CHAIN           1..217
FT                   /note="Nucleoside diphosphate-linked moiety X motif 6"
FT                   /id="PRO_0000057110"
FT   DOMAIN          42..177
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           77..98
FT                   /note="Nudix box"
SQ   SEQUENCE   217 AA;  24307 MW;  A121E4124F097E19 CRC64;
     MQSRLISIAA SEGFTFHHAE RNESTLTLWL KDGPSKLPGY ATHQVGVAGA VLDEDNGKVL
     VVQDRNKTVN AWKFPGGLSD QGEDIGATAV REVLEETGIH SEFKSLLSIR QQHNHPGAFG
     KSDLYIICRL KPLSYTINFC HQECLKCEWM DLQELAYCSN TTIITSRVAK LLLYGYNEGF
     HLVDLTMRTF PAVYSGLFYS LYHKELPETY EGSATLL