Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.
The yeast tRNA splicing endonuclease: a tetrameric enzyme with two active site subunits homologous to the archaeal tRNA endonucleases.
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The S. cerevisiae endonuclease has four essential subunits; the 5' and 3' splice-site active sites are in Sen2 and Sen34, not Sen15.
"Our results demonstrate that the eucaryal tRNA splicing endonuclease contains two functionally independent active sites for cleavage of the 5' and 3' splice sites, encoded by SEN2 and SEN34, respectively."
Three-dimensional structure determined for a subunit of human tRNA splicing endonuclease (Sen15) reveals a novel dimeric fold.
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Sen15 is a structural (noncatalytic) subunit with a fold related to the C-terminal domain of archaeal endonuclease; S. pombe Sen15 shares only ~23% identity with human Sen15.
"it shows only 23% and 20% sequence identities, respectively, to two yeast orthologs, Sp Sen15 from Schizosaccharomyces pombe and Sc Sen15 from Saccharomyces cerevisiae."
Structural basis of pre-tRNA intron removal by human tRNA splicing endonuclease.
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In human TSEN-pre-tRNA structures the tRNA mature domain is recognized by TSEN34, TSEN54 and TSEN2.
"The mature domain of pre-tRNA is recognized by conserved structural elements of TSEN34, TSEN54, and TSEN2."
Assembly defects of human tRNA splicing endonuclease contribute to impaired pre-tRNA processing in pontocerebellar hypoplasia.
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Human TSEN is assembled from inactive heterodimers, including a TSEN15-TSEN34 heterodimer whose crystal structure was determined.
"The 2.1-Å resolution X-ray crystal structure of a TSEN15-34 heterodimer"
Reconstitution of the human tRNA splicing endonuclease complex: insight into the regulation of pre-tRNA cleavage.
UniProt entry Q7LKV3 (SEN15_SCHPO)