UniProt functional annotation for Q6TEC1



	UniProt functional annotation for Q6TEC1

UniProt code: Q6TEC1.

Organism: Xenopus laevis (African clawed frog).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.

Function: RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA; metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation (PubMed:15053875, PubMed:10585477, PubMed:17567574, PubMed:18820299). Acts also as a phosphatase; hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms. The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP. Binds strongly to GTP, ITP and XTP. Participates in the hydrolysis of dIDP/IDP and probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions (By similarity). {ECO:0000250|UniProtKB:Q96DE0, ECO:0000269|PubMed:10585477, ECO:0000269|PubMed:15053875, ECO:0000269|PubMed:17567574, ECO:0000269|PubMed:18820299}.

Catalytic activity: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-adenosine in mRNA + H2O = a 5'-end phospho-adenosine in mRNA + 2 H(+) + N(7)- methyl-GDP; Xref=Rhea:RHEA:60868, Rhea:RHEA-COMP:15682, Rhea:RHEA- COMP:15686, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:63714, ChEBI:CHEBI:143974, ChEBI:CHEBI:143978; EC=3.6.1.62; Evidence={ECO:0000269|PubMed:15053875, ECO:0000269|PubMed:17567574, ECO:0000269|PubMed:18820299}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60869; Evidence={ECO:0000269|PubMed:15053875, ECO:0000269|PubMed:17567574, ECO:0000269|PubMed:18820299};

Catalytic activity: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-guanosine in mRNA + H2O = a 5'-end phospho-guanosine in mRNA + 2 H(+) + N(7)- methyl-GDP; Xref=Rhea:RHEA:60872, Rhea:RHEA-COMP:15683, Rhea:RHEA- COMP:15687, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:63714, ChEBI:CHEBI:143975, ChEBI:CHEBI:143979; EC=3.6.1.62; Evidence={ECO:0000269|PubMed:15053875, ECO:0000269|PubMed:17567574, ECO:0000269|PubMed:18820299}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60873; Evidence={ECO:0000269|PubMed:15053875, ECO:0000269|PubMed:17567574, ECO:0000269|PubMed:18820299};

Catalytic activity: Reaction=H2O + IDP = H(+) + IMP + phosphate; Xref=Rhea:RHEA:35207, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053, ChEBI:CHEBI:58280; EC=3.6.1.64; Evidence={ECO:0000250|UniProtKB:Q96DE0};

Catalytic activity: Reaction=dIDP + H2O = dIMP + H(+) + phosphate; Xref=Rhea:RHEA:35211, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:61194, ChEBI:CHEBI:62286; EC=3.6.1.64; Evidence={ECO:0000250|UniProtKB:Q96DE0};

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15053875, ECO:0000269|PubMed:17567574}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:15053875, ECO:0000269|PubMed:17567574}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:15053875, ECO:0000269|PubMed:17567574}; Note=Binds 3 or 4 divalent metal cations. Acts specifically on U8 snoRNA with magnesium as cofactor. Has broad substrate specificity with bound manganese or cobalt (in vitro). {ECO:0000269|PubMed:15053875, ECO:0000269|PubMed:17567574};

Biophysicochemical properties: pH dependence: Optimum pH is 8.5-9. {ECO:0000269|PubMed:17567574};

Subunit: Homodimer. {ECO:0000269|PubMed:16472752, ECO:0000269|PubMed:18820299}.

Subcellular location: Nucleus {ECO:0000269|PubMed:15053875}. Nucleus, nucleolus {ECO:0000269|PubMed:15053875}. Nucleus, nucleoplasm {ECO:0000269|PubMed:15053875}. Cytoplasm {ECO:0000250|UniProtKB:Q96DE0}. Note=Predominantly localized in nucleolus, and in a minor proportion in distinct foci in the nucleoplasm. {ECO:0000269|PubMed:15053875}.

Tissue specificity: Detected in ovary, and at very low levels in epithelial cells (at protein level). {ECO:0000269|PubMed:15053875}.

Similarity: Belongs to the Nudix hydrolase family. NUDT16 subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Xenopus laevis (African clawed frog).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.



Function:		RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA; metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation (PubMed:15053875, PubMed:10585477, PubMed:17567574, PubMed:18820299). Acts also as a phosphatase; hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms. The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP. Binds strongly to GTP, ITP and XTP. Participates in the hydrolysis of dIDP/IDP and probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions (By similarity). {ECO:0000250\|UniProtKB:Q96DE0, ECO:0000269\|PubMed:10585477, ECO:0000269\|PubMed:15053875, ECO:0000269\|PubMed:17567574, ECO:0000269\|PubMed:18820299}.


Catalytic activity:		Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-adenosine in mRNA + H2O = a 5'-end phospho-adenosine in mRNA + 2 H(+) + N(7)- methyl-GDP; Xref=Rhea:RHEA:60868, Rhea:RHEA-COMP:15682, Rhea:RHEA- COMP:15686, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:63714, ChEBI:CHEBI:143974, ChEBI:CHEBI:143978; EC=3.6.1.62; Evidence={ECO:0000269\|PubMed:15053875, ECO:0000269\|PubMed:17567574, ECO:0000269\|PubMed:18820299}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60869; Evidence={ECO:0000269\|PubMed:15053875, ECO:0000269\|PubMed:17567574, ECO:0000269\|PubMed:18820299};
Catalytic activity:		Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-guanosine in mRNA + H2O = a 5'-end phospho-guanosine in mRNA + 2 H(+) + N(7)- methyl-GDP; Xref=Rhea:RHEA:60872, Rhea:RHEA-COMP:15683, Rhea:RHEA- COMP:15687, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:63714, ChEBI:CHEBI:143975, ChEBI:CHEBI:143979; EC=3.6.1.62; Evidence={ECO:0000269\|PubMed:15053875, ECO:0000269\|PubMed:17567574, ECO:0000269\|PubMed:18820299}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60873; Evidence={ECO:0000269\|PubMed:15053875, ECO:0000269\|PubMed:17567574, ECO:0000269\|PubMed:18820299};
Catalytic activity:		Reaction=H2O + IDP = H(+) + IMP + phosphate; Xref=Rhea:RHEA:35207, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053, ChEBI:CHEBI:58280; EC=3.6.1.64; Evidence={ECO:0000250\|UniProtKB:Q96DE0};
Catalytic activity:		Reaction=dIDP + H2O = dIMP + H(+) + phosphate; Xref=Rhea:RHEA:35211, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:61194, ChEBI:CHEBI:62286; EC=3.6.1.64; Evidence={ECO:0000250\|UniProtKB:Q96DE0};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269\|PubMed:15053875, ECO:0000269\|PubMed:17567574}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269\|PubMed:15053875, ECO:0000269\|PubMed:17567574}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269\|PubMed:15053875, ECO:0000269\|PubMed:17567574}; Note=Binds 3 or 4 divalent metal cations. Acts specifically on U8 snoRNA with magnesium as cofactor. Has broad substrate specificity with bound manganese or cobalt (in vitro). {ECO:0000269\|PubMed:15053875, ECO:0000269\|PubMed:17567574};
Biophysicochemical properties:		pH dependence: Optimum pH is 8.5-9. {ECO:0000269\|PubMed:17567574};
Subunit:		Homodimer. {ECO:0000269\|PubMed:16472752, ECO:0000269\|PubMed:18820299}.
Subcellular location:		Nucleus {ECO:0000269\|PubMed:15053875}. Nucleus, nucleolus {ECO:0000269\|PubMed:15053875}. Nucleus, nucleoplasm {ECO:0000269\|PubMed:15053875}. Cytoplasm {ECO:0000250\|UniProtKB:Q96DE0}. Note=Predominantly localized in nucleolus, and in a minor proportion in distinct foci in the nucleoplasm. {ECO:0000269\|PubMed:15053875}.
Tissue specificity:		Detected in ovary, and at very low levels in epithelial cells (at protein level). {ECO:0000269\|PubMed:15053875}.
Similarity:		Belongs to the Nudix hydrolase family. NUDT16 subfamily. {ECO:0000305}.