Q6CPU0 · DXO1_KLULA
- ProteinDecapping and exoribonuclease protein 1
- GeneDXO1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids403 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 (PubMed:28283058).
The NAD-cap is present at the 5'-end of some RNAs and snoRNAs (By similarity).
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 and mediates their subsequent degradation (PubMed:22961381).
Has decapping and 5'-3' exonuclease activities (PubMed:22961381).
Has decapping activity toward incomplete 5'-end cap mRNAs such as unmethylated 5'-end-capped RNA to release GpppN and 5'-end monophosphate RNA (PubMed:22961381).
The 5'-end monophosphate RNA is then degraded by the 5'-3' exoribonuclease activity, enabling this enzyme to decap and degrade incompletely capped mRNAs (PubMed:22961381).
The NAD-cap is present at the 5'-end of some RNAs and snoRNAs (By similarity).
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 and mediates their subsequent degradation (PubMed:22961381).
Has decapping and 5'-3' exonuclease activities (PubMed:22961381).
Has decapping activity toward incomplete 5'-end cap mRNAs such as unmethylated 5'-end-capped RNA to release GpppN and 5'-end monophosphate RNA (PubMed:22961381).
The 5'-end monophosphate RNA is then degraded by the 5'-3' exoribonuclease activity, enabling this enzyme to decap and degrade incompletely capped mRNAs (PubMed:22961381).
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.
Cofactor
Note: Divalent metal cation.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 223 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 260 | substrate | ||||
Sequence: E | ||||||
Binding site | 262 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 273 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 274 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 275 | substrate | ||||
Sequence: K | ||||||
Binding site | 297 | substrate | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleus | |
Molecular Function | 5'-3' exonuclease activity | |
Molecular Function | metal ion binding | |
Molecular Function | mRNA 5'-diphosphatase activity | |
Molecular Function | nucleotide binding | |
Molecular Function | RNA binding | |
Molecular Function | RNA NAD+-cap (NAD+-forming) hydrolase activity | |
Biological Process | NAD-cap decapping | |
Biological Process | nuclear mRNA surveillance | |
Biological Process | nucleic acid metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDecapping and exoribonuclease protein 1
- EC number
- Short namesKlDxo1
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Kluyveromyces
Accessions
- Primary accessionQ6CPU0
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 161 | Reduced decapping activity without affecting the exonuclease activity. Reduced decapping and exonuclease activities; when associated with G-163. | ||||
Sequence: L → W | ||||||
Mutagenesis | 163 | Does not affect the exonuclease activity. Reduced decapping and exonuclease activities; when associated with W-161. Reduced decapping and exonuclease activities; when associated with K-167. | ||||
Sequence: H → G | ||||||
Mutagenesis | 167 | Does not affect the decapping and exonuclease activities. Reduced decapping and exonuclease activities; when associated with G-163. | ||||
Sequence: D → K |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000422597 | 1-403 | Decapping and exoribonuclease protein 1 | |||
Sequence: MTTVSCDKDENKVDQLGESLSQLRISTRKNNKPSQKKGSLVLSCKKFPHVSVNYVVDKTPKLLTDCKEVHNCSYIINDATLLWNEASRKPRLRPEVCTYIKDSKWENKAVKDSFIGIDLTKGYDDYVPLDRNVLNSLVILKEAYQRYEKTLNPEKTTFVSLRHHIIDIIMCPFLDEPLSLLMTVQPDKNILISVDKSKDKPNGIHETRNSFNKKICYTGFALEDLLIESPTEGHILEHELYYSIVHGSLNDEIDLLIQAEMDSINTLTDTYTEIKSSVHFKLGNTYHRRKLLRMWIQTNLLPKSDLLIGFRNSYSNELEQLKAYKIQDIYHKINNSSIVGKPGKFYKFNPNVANDWFQHIFQVLKQNLLLLSQESTSTTFKVQIDTNLTLSISPASQFVTALG |
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Sequence similarities
Belongs to the DXO/Dom3Z family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length403
- Mass (Da)46,312
- Last updated2004-08-16 v1
- ChecksumD2E6DA0EE3FE4894
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CR382125 EMBL· GenBank· DDBJ | CAG99136.1 EMBL· GenBank· DDBJ | Genomic DNA |