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Threonyl and Alanyl tRNA synthetase second additional domain
The catalytically active from of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain [1]. [1]. 10319817. The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site. Sankaranarayanan R, Dock-Bregeon AC, Romby P, Caillet J, Springer M, Rees B, Ehresmann C, Ehresmann B, Moras D;. Cell 1999;97:371-381. (from Pfam)
alanine--tRNA ligase-related protein
Proteins belonging to this family include alanine--tRNA ligases and related smaller proteins such as alanyl-tRNA editing proteins.
DHHA1 domain-containing protein
DHHA1 ( DHH-associated domain) is often found with DHH, and is suggested to have an RNA-binding function.
alanine--tRNA ligase
alanine--tRNA ligase catalyzes the attachment of alanine to the ribose 3' OH group of tRNA(Ala)
The model describes alanine--tRNA ligase. This enzyme catalyzes the reaction (tRNAala + L-alanine + ATP = L-alanyl-tRNAala + pyrophosphate + AMP).
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