Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation.
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Crystal structures of intact human eEFSec (GDP- and GTP-analogue-bound) reveal a four-domain chalice-like fold; eEFSec is a translational GTPase that binds Sec-tRNA(Sec) with high affinity and stringent specificity and delivers it during UGA decoding.
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Sec-binding-pocket (Asp229/His230/Arg285) and GTPase-site (Thr48/Asp92/His96) mutants abolish UGA read-through and selenoprotein synthesis, defining the residues required for Sec incorporation and GTP hydrolysis.
Structure of the mammalian ribosome as it decodes the selenocysteine UGA codon.
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Cryo-EM of the mammalian "selenosome" shows SBP2/SECIS docking on the 40S creates a binding site on the stalled 80S ribosome for the eEFSec:GTP:tRNA(Sec) ternary complex, which delivers Sec to the A-site; the preaccommodated state was captured.
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The GTPase-defective His96->Ala mutant confirms His96 as the catalytic residue; eEFSec engages tRNA(Sec) with all its domains and its D4 contacts the SECIS apical loop.
EEFSEC deficiency: A selenopathy with early-onset neurodegeneration.
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Biallelic EEFSEC variants reduce EEFSEC function in vitro and lower selenoprotein levels in patient fibroblasts, causing an autosomal recessive early-onset neurodegenerative disorder.
"These variants showed reduced EEFSEC function in vitro, leading to lower levels of selenoproteins in fibroblasts."