A0A2R8YCT7 is shorter than the experimentally characterized DTD1 editing core and lacks the conserved Gly-cisPro motif. ProtNLM describes the full editing mechanism, but the selected sequence does not preserve the machinery needed for that inference.
A0A2R8YCT7 and Q8TEA8 share HGNC:16219. The selected 127 residues align to reference 1–127 with 125 identities. Reference Gly139–Pro140 is outside the selected product. This is a sequence deletion, not a measured cis-to-trans conformational change or evidence of conversion into the DTD2/ATD paralog.
the N-terminal
core of DUE-B is shown to display both D-aminoacyl-tRNA deacylase activity and
ATPase activity.
how it uses an invariant
'cross-subunit' Gly-cisPro dipeptide to capture the chiral centre of incoming
D-aminoacyl-tRNA.
The complete emitted record is preserved in DTD1-protnlm-source.json. Assessments below address the selected protein product; evidence on longer products is identified explicitly.
D-tyrosyl-tRNA(Tyr) deacylase
NPI (CS 0) as an enzymatic name for A0A2R8YCT7: the short sequence lacks the reference Gly-cisPro motif needed for the conserved editing site. “DTD1-derived fragment” captures the supported identity without assigning deacylase activity. Sequence mapping; PMID:24302572(https://pubmed.ncbi.nlm.nih.gov/24302572/).
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. 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
NPI (CS 0) for the composite assertion that this selected protein executes the complete DTD editing mechanism. The family mechanism, D-aminoacyl-tRNA hydrolysis and chiral rejection are real, but its conserved Gly-cisPro element is deleted here. Gly-tRNA(Ala) hydrolysis and an in vivo protection phenotype have not been demonstrated for this truncated product. This does not challenge the full-length human DTD1 activity measured in PMID:17264083 or infer an ATD-like alternative specificity. PMID:17264083(https://pubmed.ncbi.nlm.nih.gov/17264083/); PMID:24302572(https://pubmed.ncbi.nlm.nih.gov/24302572/).
No GO or EC term was emitted in this record; the name, function and location assessments above constitute its prediction review.
PTHR10472:SF5 supports DTD1 ancestry. Functional transfer still requires the dimeric editing pocket: the benchmark target lacks a conserved motif present in the same-gene reference. No paralog switch or ancestral function change is asserted.
PMID:17264083 is abstract-only in the cache; the DTD structural/mechanistic paper has full text. Activity of the exact 127-residue product was not measured in these sources. No core MF is assigned. Proteomics-database cross-references alone do not establish the short product’s activity.
Exact sequence mapping: DTD1-bioinformatics/RESULTS.md. Global alignments can place nonhomologous alternative tails opposite gaps or distant residues; only conserved segments and explicitly retained feature intervals support functional transfer.
The genuine Falcon report supplies literature synthesis for DTD1. Its full-length enzyme mechanism is interpreted through the exact127-residue input and the mapped absence of the Gly-cisPro site; activity of the longer human editing core is not an assay of this short product.