A0A2B7WFW9 · A0A2B7WFW9_POLH7
- ProteinmRNA-capping enzyme subunit alpha
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids423 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Second step of mRNA capping. Transfer of the GMP moiety of GTP to the 5'-end of RNA via an enzyme-GMP covalent reaction intermediate.
Catalytic activity
- a 5'-end diphospho-ribonucleoside in mRNA + GTP + H+ = a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphateThis reaction proceeds in the forward direction.
Features
Showing features for active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 64 | N6-GMP-lysine intermediate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mRNA capping enzyme complex | |
Molecular Function | ATP binding | |
Molecular Function | GTP binding | |
Molecular Function | mRNA guanylyltransferase 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 subunit alpha
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Onygenales > Onygenales incertae sedis > Polytolypa
Accessions
- Primary accessionA0A2B7WFW9
Proteomes
Subcellular Location
Interaction
Subunit
Heterodimer. The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an mRNA 5'-triphosphate monophosphatase.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 42-242 | mRNA capping enzyme adenylation | |||
Domain | 246-368 | mRNA capping enzyme C-terminal | |||
Compositional bias | 381-395 | Basic and acidic residues | |||
Region | 381-423 | Disordered | |||
Sequence similarities
Belongs to the eukaryotic GTase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length423
- Mass (Da)49,198
- Last updated2017-12-20 v1
- ChecksumC4F2C9B47FBB21B9
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 381-395 | Basic and acidic residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
PDNA01000422 EMBL· GenBank· DDBJ | PGG95566.1 EMBL· GenBank· DDBJ | Genomic DNA |