DTD1 encodes D-aminoacyl-tRNA deacylase, also known as the DNA-unwinding element-binding protein DUE-B. The 127-residue human product A0A2R8YCT7 retains an N-terminal portion of the 209-residue reference but ends before the conserved Gly-cisPro substrate-selection motif. Its biochemical activity is unresolved; the tRNA-editing and DNA-binding functions established for larger DTD1 constructs cannot be assumed for this product.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0002161 aminoacyl-tRNA deacylase activity | IEA GO_REF:0000002 | REMOVE | Summary: The selected 127-residue product lacks the conserved cross-subunit Gly-cisPro motif of the DTD editing pocket. Human DTD1 editing activity was measured for a larger N-terminal core, not this truncated product. Domain-family matching does not support a complete aminoacyl-tRNA deacylase activity in A0A2R8YCT7. Supporting Evidence: PMID:17264083 the N-terminal core of DUE-B is shown to display both D-aminoacyl-tRNA deacylase activity and ATPase activity. PMID:24302572 how it uses an invariant 'cross-subunit' Gly-cisPro dipeptide to capture the chiral centre of incoming D-aminoacyl-tRNA. file:human/DTD1/DTD1-bioinformatics/RESULTS.md | Motif: Gly-cisPro motif, important for rejection of L-amino acids | 139–140 | 0 / 2 | 0 | |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | UNDECIDED | Summary: Cytoplasmic localization is biologically plausible for a short DTD1-derived protein but has not been shown for A0A2R8YCT7. The deletion also prevents assuming that normal tRNA-editing complexes determine its localization. Supporting Evidence: file:human/DTD1/DTD1-bioinformatics/RESULTS.md | Motif: Gly-cisPro motif, important for rejection of L-amino acids | 139–140 | 0 / 2 | 0 | PMID:17264083 the N-terminal core of DUE-B is shown to display both D-aminoacyl-tRNA deacylase activity and ATPase activity. |
| GO:0006399 tRNA metabolic process | IEA GO_REF:0000104 | UNDECIDED | Summary: The gene encodes a tRNA editor, but this product lacks an essential substrate-selection element. A noncatalytic contribution to tRNA metabolism is conceivable but untested; the broad process cannot be resolved from the remaining N-terminal sequence. Supporting Evidence: file:human/DTD1/DTD1-bioinformatics/RESULTS.md | Motif: Gly-cisPro motif, important for rejection of L-amino acids | 139–140 | 0 / 2 | 0 | PMID:24302572 how it uses an invariant 'cross-subunit' Gly-cisPro dipeptide to capture the chiral centre of incoming D-aminoacyl-tRNA. |
| GO:0051499 D-aminoacyl-tRNA deacylase activity | IEA GO_REF:0000120 | REMOVE | Summary: The DTD1-family assignment is sound, but the selected sequence terminates before the Gly-cisPro motif required to form the conserved chiral proofreading site. The full-length editing activity is not transferable to this incomplete product. Supporting Evidence: file:human/DTD1/DTD1-bioinformatics/RESULTS.md | Motif: Gly-cisPro motif, important for rejection of L-amino acids | 139–140 | 0 / 2 | 0 | PMID:24302572 how it uses an invariant 'cross-subunit' Gly-cisPro dipeptide to capture the chiral centre of incoming D-aminoacyl-tRNA. PMID:17264083 the N-terminal core of DUE-B is shown to display both D-aminoacyl-tRNA deacylase activity and ATPase activity. |
| GO:0106026 Gly-tRNA(Ala) deacylase activity | IEA GO_REF:0000116 | REMOVE | Summary: Gly-tRNA(Ala) deacylation requires a functional DTD editing pocket. The selected sequence lacks the reference Gly-cisPro substrate-selection motif, so this specific catalytic assignment is not justified by an intact family mechanism. No alternative catalytic mechanism is demonstrated. Supporting Evidence: file:human/DTD1/DTD1-bioinformatics/RESULTS.md | Motif: Gly-cisPro motif, important for rejection of L-amino acids | 139–140 | 0 / 2 | 0 | PMID:24302572 how it uses an invariant 'cross-subunit' Gly-cisPro dipeptide to capture the chiral centre of incoming D-aminoacyl-tRNA. |
| GO:0106074 aminoacyl-tRNA metabolism involved in translational fidelity | IEA GO_REF:0000120 | UNDECIDED | Summary: Aminoacyl-tRNA proofreading is established for the DTD1 gene, but contribution of this 127-residue form to translational fidelity is unresolved because it lacks the conserved editing motif. This broad process is not rejected solely from the absence of an exact-product assay. Supporting Evidence: PMID:17264083 the N-terminal core of DUE-B is shown to display both D-aminoacyl-tRNA deacylase activity and ATPase activity. file:human/DTD1/DTD1-bioinformatics/RESULTS.md | Motif: Gly-cisPro motif, important for rejection of L-amino acids | 139–140 | 0 / 2 | 0 | |
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