UniProt ID: Q6NY98 |
FUNCTION: Bifunctional mRNA-capping enzyme exhibiting RNA 5'- triphosphate monophosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the GMP moiety of GTP to the 5'-diphosphate terminus of RNA via a covalent enzyme-GMP reaction intermediate. {ECO:0000250|UniProtKB:O60942}. CATALYTIC ACTIVITY: Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + H(+) + phosphate; Xref=Rhea:RHEA:67004, Rhea:RHEA-COMP:17164, Rhea:RHEA-COMP:17165, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:167616, ChEBI:CHEBI:167618; EC=3.6.1.74; Evidence={ECO:0000250|UniProtKB:O60942}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67005; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'- end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate; Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67013; Evidence={ECO:0000305}; SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. SIMILARITY: In the N-terminal section; belongs to the non-receptor class of the protein-tyrosine phosphatase family. {ECO:0000305}. SIMILARITY: In the C-terminal section; belongs to the eukaryotic GTase family. {ECO:0000305}. |
This information was provided by UniProt through a collaboration with ZFIN. (1) |