A3LNL5 · DXO_PICST
- ProteinDecapping nuclease RAI1
- GeneRAI1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids396 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (By similarity).
The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity).
Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs (PubMed:26101253).
Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1) (By similarity).
Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to release pyrophosphates (By similarity).
Stimulates exoribonuclease activity of Rat1, allowing it to degrade RNAs with stable secondary structure more effectively (By similarity).
The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity).
Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs (PubMed:26101253).
Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1) (By similarity).
Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to release pyrophosphates (By similarity).
Stimulates exoribonuclease activity of Rat1, allowing it to degrade RNAs with stable secondary structure more effectively (By similarity).
Catalytic activity
- a 5'-end NAD+-phospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + H+ + NAD+This reaction proceeds in the forward direction.
- a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside-ribonucleotide in mRNA + H2O = a (N7-methyl 5'-triphosphoguanosine)-nucleoside + a 5'-end phospho-ribonucleoside in mRNA + H+This reaction proceeds in the forward direction.
- a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + diphosphate + H+This reaction proceeds in the forward direction.
Cofactor
Note: Divalent metal cation.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 107-109 | substrate | ||||
Sequence: YRG | ||||||
Binding site | 179 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 228 | substrate | ||||
Sequence: E | ||||||
Binding site | 230 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 249 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 250 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 251 | substrate | ||||
Sequence: K | ||||||
Binding site | 275 | substrate | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | metal ion binding | |
Molecular Function | nuclease activity | |
Molecular Function | nucleotide binding | |
Molecular Function | RNA binding | |
Biological Process | mRNA processing |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDecapping nuclease RAI1
- EC number
- Short namesSsRai1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Debaryomycetaceae > Scheffersomyces
Accessions
- Primary accessionA3LNL5
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000451696 | 1-396 | Decapping nuclease RAI1 | |||
Sequence: MMKTLSLQSRAKTTALKQPKEIFAFARDIDGEFVYDQKIVKDENVSYYYLPDSKIDGSIDLQAGYAKFKKIPEEKNMSDMKCLLTALTKYEQEHNNGEKVNVDIITYRGLMTKLLALPYNLNDPVDLNVLAYDGQLFINSDEEIELARRKEEDEHKQQSMTPEKYDHMKRCEFSGYKFEAIATLPKPWADCSRQQIDKRGKKMVNNYEQYISVIKTGIGEAKMLLAGEVDCVWDYIPEDGKDVLSHYMELKTTRILESNGQVVNFEKKLFKTWAQCFLMGIRKVVYGFRDDSFFLRDVELYKTEEIPLLIKNNALTENKSGGKINCTTALKWYGAVIEWLLQEIPRDDTSKAYRVSFDPSTRTFTLRELMGNENSRLRNGEMLTSEFKQWRESIQK |
Interaction
Subunit
Interacts with RAT1; the interaction is direct, stabilizes RAT1 protein structure and stimulates its exoribonuclease activity (By similarity).
The interaction also stimulates RAI1 pyrophosphohydrolase activity, probably by recruiting it to mRNA substrates (By similarity).
The interaction also stimulates RAI1 pyrophosphohydrolase activity, probably by recruiting it to mRNA substrates (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Sequence similarities
Belongs to the DXO/Dom3Z family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length396
- Mass (Da)46,084
- Last updated2007-07-24 v2
- Checksum86FA8C46A0A96B86
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000496 EMBL· GenBank· DDBJ | ABN64879.2 EMBL· GenBank· DDBJ | Genomic DNA |