Q68EL2 · DTD2_DANRE
- ProteinD-aminoacyl-tRNA deacylase 2
- Genedtd2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids160 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Deacylates mischarged D-aminoacyl-tRNAs (By similarity).
Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS (By similarity).
Probably acts by rejecting L-amino acids from its binding site rather than specific recognition of D-amino acids (By similarity).
Catalyzes the hydrolysis of D-tyrosyl-tRNA(Tyr), has no activity on correctly charged L-tyrosyl-tRNA(Tyr) (By similarity).
By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality. In contrast to DTD1, deacylates L-Ala mischarged on tRNA(Thr)(G4.U69) by alanine-tRNA ligase AARS (PubMed:29410408).
Can deacylate L-Ala due to a relaxed specificity for substrate chirality caused by the trans conformation of the Gly-Pro motif in the active site (PubMed:29410408).
Also hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly) in vitro, although in vivo eef1a1a/EF-Tu may protect cognate achiral glycyl-tRNA(Gly) from DTD2-mediated deacetylation (By similarity).
Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS (By similarity).
Probably acts by rejecting L-amino acids from its binding site rather than specific recognition of D-amino acids (By similarity).
Catalyzes the hydrolysis of D-tyrosyl-tRNA(Tyr), has no activity on correctly charged L-tyrosyl-tRNA(Tyr) (By similarity).
By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality. In contrast to DTD1, deacylates L-Ala mischarged on tRNA(Thr)(G4.U69) by alanine-tRNA ligase AARS (PubMed:29410408).
Can deacylate L-Ala due to a relaxed specificity for substrate chirality caused by the trans conformation of the Gly-Pro motif in the active site (PubMed:29410408).
Also hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly) in vitro, although in vivo eef1a1a/EF-Tu may protect cognate achiral glycyl-tRNA(Gly) from DTD2-mediated deacetylation (By similarity).
Catalytic activity
- a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H+
- D-tyrosyl-tRNA(Tyr) + H2O = D-tyrosine + tRNA(Tyr)
- H2O + L-alanyl-tRNA(Thr) = H+ + L-alanine + tRNA(Thr)
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | Ala-tRNA(Thr) hydrolase activity | |
Molecular Function | D-tyrosyl-tRNA(Tyr) deacylase activity | |
Molecular Function | tRNA binding | |
Biological Process | aminoacyl-tRNA metabolism involved in translational fidelity | |
Biological Process | tRNA metabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameD-aminoacyl-tRNA deacylase 2
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionQ68EL2
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000254051 | 1-160 | D-aminoacyl-tRNA deacylase 2 | |||
Sequence: MKARVVLQQCLHARLQVKPPDEESEAEWVEVNRGMVIYICFFKGATEDLIPKMVNTLLNVKLCETESGKFTSVLQLPGSVLIVPQATLGGKPKGRGMQYHGNIGKDEGLKLYETFVSLCQSELSSCKNSDILTEVKHGTYGNRQVLKLDTNGPYTHLMEF |
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 152-153 | Gly-transPro motif, allows the protein to recognize chirality of D-amino acids | ||||
Sequence: GP |
Domain
A Gly-transPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of most L-amino acids except L-Ala. The trans conformation of the motif is maintained by Arg-143.
Sequence similarities
Belongs to the DTD family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length160
- Mass (Da)17,847
- Last updated2004-10-11 v1
- ChecksumEC85396F80C603CD
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC080214 EMBL· GenBank· DDBJ | AAH80214.1 EMBL· GenBank· DDBJ | mRNA |