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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)
DHHA1 domain-containing protein
DHHA1 ( DHH-associated domain) is often found with DHH, and is suggested to have an RNA-binding function.
alanyl-tRNA editing protein
alanyl-tRNA editing protein functions in trans to edit the amino acid moiety from incorrectly charged Ser-tRNA(Ala) or Gly-tRNA(Ala)
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