L-seryl-tRNA(Sec) selenium transferase catalyzes the formation of selenocysteinyl-tRNA(Sec) from seryl-tRNA(Sec) and L-selenophosphate in selenoprotein biosynthesis
L-seryl-tRNA(Sec) selenium transferase; In bacteria, the incorporation of selenocysteine as ...
9-460
0e+00
L-seryl-tRNA(Sec) selenium transferase; In bacteria, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes SelA. This model excludes homologs that appear to differ in function from Frankia alni, Helicobacter pylori, Methanococcus jannaschii and other archaea, and so on. [Protein synthesis, tRNA aminoacylation]
:
Pssm-ID: 273099 [Multi-domain] Cd Length: 454 Bit Score: 647.32 E-value: 0e+00
L-seryl-tRNA(Sec) selenium transferase; In bacteria, the incorporation of selenocysteine as ...
9-460
0e+00
L-seryl-tRNA(Sec) selenium transferase; In bacteria, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes SelA. This model excludes homologs that appear to differ in function from Frankia alni, Helicobacter pylori, Methanococcus jannaschii and other archaea, and so on. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273099 [Multi-domain] Cd Length: 454 Bit Score: 647.32 E-value: 0e+00
L-seryl-tRNA(Sec) selenium transferase; In bacteria, the incorporation of selenocysteine as ...
9-460
0e+00
L-seryl-tRNA(Sec) selenium transferase; In bacteria, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes SelA. This model excludes homologs that appear to differ in function from Frankia alni, Helicobacter pylori, Methanococcus jannaschii and other archaea, and so on. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273099 [Multi-domain] Cd Length: 454 Bit Score: 647.32 E-value: 0e+00
Selenocysteine synthase N terminal; This domain family is found in bacteria, and is ...
11-48
8.07e-08
Selenocysteine synthase N terminal; This domain family is found in bacteria, and is approximately 40 amino acids in length. The family is found in association with pfam03841. There is a single completely conserved residue P that may be functionally important. This family is the N terminal region of selenocysteine synthase which catalyzes the conversion of seryl-tRNA(Sec) into selenocysteyl-tRNA(Sec).
Pssm-ID: 432519 Cd Length: 40 Bit Score: 48.16 E-value: 8.07e-08
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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