Gene Ontology annotation through association of InterPro records with GO terms
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Automatic Gene Ontology annotation based on Rhea mapping
Combined Automated Annotation using Multiple IEA Methods
Structure and function of the c-myc DNA-unwinding element-binding protein DUE-B.
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Purified human DUE-B/DTD1 N-terminal core has D-aminoacyl-tRNA deacylase and ATPase activities; C-terminal material is required for DNA binding.
"the N-terminal
core of DUE-B is shown to display both D-aminoacyl-tRNA deacylase activity and
ATPase activity."
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The crystallized active core is a dimer of the N-terminal domain; the disordered C-terminal region is dispensable for dimerization but essential for DNA binding.
"However, this region is"
Mechanism of chiral proofreading during translation of the genetic code.
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Structural and biochemical analysis establishes the conserved cross-subunit Gly-cisPro substrate-selection mechanism in the DTD family.
"how it uses an invariant
'cross-subunit' Gly-cisPro dipeptide to capture the chiral centre of incoming
D-aminoacyl-tRNA."
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The two DTD active sites lie at the dimer interface, formed partly by the conserved SQFTL and NxGP(V/F)T motifs.
"The ligand binds in the two active sites located at the dimer interface."
The c-myc DNA-unwinding element-binding protein modulates the assembly of DNA replication complexes in vitro.
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Human DUE-B is about 60 residues longer than yeast and worm orthologs, is primarily nuclear, chromatin-bound at the c-myc DUE, and co-purifies with ATPase activity as a dimer.
"the human protein is approximately 60 amino"
The DNA unwinding element binding protein DUE-B interacts with Cdc45 in preinitiation complex formation.
Exact DTD1 product-to-reference sequence and motif mapping
DTD1 re-review: gene-model analysis of A0A2R8YCT7 vs Q8TEA8
Frozen exact-input ProtNLM output and UniProt sequence for A0A2R8YCT7