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YbaK/EbsC family protein
This domain is found either on its own or in association with the tRNA synthetase class II core domain (Pfam:PF00587). It is involved in the tRNA editing of mis-charged tRNAs including Cys-tRNA(Pro), Cys-tRNA(Cys), Ala-tRNA(Pro)[2-5]. The structure of this domain shows a novel fold [1]. [1]. 10813833. Crystal structure of YbaK protein from Haemophilus influenzae (HI1434) at 1.8 A resolution: functional implications. Zhang H, Huang K, Li Z, Banerjei L, Fisher KE, Grishin NV, Eisenstein E, Herzberg O;. Proteins 2000;40:86-97. [2]. 15886196. The bacterial YbaK protein is a Cys-tRNAPro and Cys-tRNA Cys deacylase. Ruan B, Soll D;. J Biol Chem. 2005;280:25887-25891. [3]. 14663147. Trans-editing of mischarged tRNAs. Ahel I, Korencic D, Ibba M, Soll D;. Proc Natl Acad Sci U S A. 2003;100:15422-15427. [4]. 16087664. Cys-tRNA(Pro) editing by Haemophilus influenzae YbaK via a novel synthetase.YbaK.tRNA ternary complex. An S, Musier-Forsyth K;. J Biol Chem. 2005;280:34465-34472. [5]. 21768119. Substrate-mediated fidelity mechanism ensures accurate decoding of proline codons. So BR, An S, Kumar S, Das M, Turner DA, Hadad CM, Musier-Forsyth K;. J Biol Chem. 2011;286:31810-31820. (from Pfam)
aminoacyl-tRNA deacylase
aminoacyl-tRNA deacylase of the YbaK/EbsC family
Cys-tRNA(Pro) deacylase
This HMM represents the YbaK family, bacterial proteins whose full length sequence is homologous to an insertion domain in proline--tRNA ligases. The domain deacylates mischarged tRNAs. The YbaK protein of Haemophilus influenzae (HI1434) likewise deacylates Ala-tRNA(Pro), but not the correctly charged Pro-tRNA(Pro). A crystallographic study of HI1434 suggests a nucleotide binding function. Previously, a member of this family was described as EbsC and was thought to be involved in cell wall metabolism.
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