Protein Family Models

This domain family is found in bacteria, and is approximately 40 amino acids in length. The family is found in association with Pfam:PF03841. There is a single completely conserved residue P that may be functionally important. This family is the N terminal region of selenocysteine synthase which catalyses the conversion of seryl-tRNA(Sec) into selenocysteyl-tRNA(Sec). [1]. 9688279. Bacterial selenocysteine synthase--structural and functional properties. Tormay P, Wilting R, Lottspeich F, Mehta PK, Christen P, Bock A;. Eur J Biochem. 1998;254:655-661. (from Pfam)

Date:

2024-10-16

Date:

2024-08-14

L-seryl-tRNA(Sec) selenium transferase catalyzes the formation of selenocysteinyl-tRNA(Sec) from seryl-tRNA(Sec) and L-selenophosphate in selenoprotein biosynthesis

Date:

2023-02-28

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 HMM 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.

Gene:

selA

Date:

2024-05-16