Q9IA92 · Q9IA92_XENLA
- ProteinmRNA-capping enzyme
- GenexCAP1b
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids511 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
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.
Catalytic activity
- a 5'-end diphospho-ribonucleoside in mRNA + GTP + H+ = a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 126 | Phosphocysteine intermediate | ||||
Sequence: C | ||||||
Active site | 295 | N6-GMP-lysine intermediate | ||||
Sequence: K | ||||||
Binding site | 300 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 316 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 344-346 | GTP (UniProtKB | ChEBI) | ||||
Sequence: DGE | ||||||
Binding site | 459-461 | GTP (UniProtKB | ChEBI) | ||||
Sequence: KWK |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | ATP binding | |
Molecular Function | GTP binding | |
Molecular Function | mRNA 5'-triphosphate monophosphatase activity | |
Molecular Function | mRNA guanylyltransferase activity | |
Molecular Function | polynucleotide 5'-phosphatase activity | |
Molecular Function | protein tyrosine/serine/threonine phosphatase activity | |
Biological Process | 7-methylguanosine mRNA capping |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namemRNA-capping enzyme
Including 2 domains:
- Recommended namemRNA 5'-triphosphate monophosphatase
- EC number
- Alternative names
- Recommended namemRNA guanylyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus
Accessions
- Primary accessionQ9IA92
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 25-183 | Tyrosine-protein phosphatase | ||||
Sequence: LPLKTMLGPKYDDQVPEENRFHPSMLSNYLKSLKVKMGLLVDLTNTTRFYDRNDIEKEGIKYIKLQCKGHGECPSQENTDTFLRLCDHFIDRNPTELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYKADYLKELFRRYGDIEDA | ||||||
Domain | 104-171 | Tyrosine specific protein phosphatases | ||||
Sequence: DTFLRLCDHFIDRNPTELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYKADYLK |
Sequence similarities
In the C-terminal section; belongs to the eukaryotic GTase family.
In the N-terminal section; belongs to the non-receptor class of the protein-tyrosine phosphatase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length511
- Mass (Da)58,656
- Last updated2000-10-01 v1
- Checksum9860AF677D1EF85A