A0A0C7N7F2 · A0A0C7N7F2_9SACH
- ProteinmRNA-capping enzyme subunit alpha
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids471 (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 | 66 | N6-GMP-lysine intermediate | ||||
Sequence: K |
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
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Lachancea
Accessions
- Primary accessionA0A0C7N7F2
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 | 43-245 | mRNA capping enzyme adenylation | ||||
Sequence: QPISFHHSDIEEKLLAQDYYVCEKTDGLRGLMLMVINPVTKEQGCFIIDRENNYFQVSGFRFPRLPKQSRKELLETFQDGTLIDGELVIQTNPVTKLKELRYLMFDCLAINGRCIAQSPTSSRLAHLGKEFFKPYYDLRSLYPAQCSTFPFKISMKVMNFSTDLSKVAHSLDKLPHVSDGLIFTPVNTPYTIGGKDSLLLKWK | ||||||
Domain | 249-393 | mRNA capping enzyme C-terminal | ||||
Sequence: ENSVDFKMILEIPLAEDTSLPKNDANRFYHNYEVKPSFHLYTWQGGADVNARLQAFDQPFSKKELDLLDRTYKKFAELEISNEKWQELKSLDEPLNGRVVECTKDQETGVWHMLRFRDDKLNGNHVSVVKKVLESISDSVKIEDL | ||||||
Compositional bias | 404-424 | Basic and acidic residues | ||||
Sequence: WQLRHSDRKRSFQEAHRPSAS | ||||||
Region | 404-471 | Disordered | ||||
Sequence: WQLRHSDRKRSFQEAHRPSASEDVDLNTTNGGQSFKQPDYVDDDDEDDDDMWPDNDEDLETEPKKPKL | ||||||
Compositional bias | 425-439 | Polar residues | ||||
Sequence: EDVDLNTTNGGQSFK | ||||||
Compositional bias | 443-460 | Acidic residues | ||||
Sequence: YVDDDDEDDDDMWPDNDE |
Sequence similarities
Belongs to the eukaryotic GTase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length471
- Mass (Da)54,276
- Last updated2015-04-29 v1
- Checksum41E4FE1FEB0A9021
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 404-424 | Basic and acidic residues | ||||
Sequence: WQLRHSDRKRSFQEAHRPSAS | ||||||
Compositional bias | 425-439 | Polar residues | ||||
Sequence: EDVDLNTTNGGQSFK | ||||||
Compositional bias | 443-460 | Acidic residues | ||||
Sequence: YVDDDDEDDDDMWPDNDE |
Keywords
- Technical term