Protein Family Models

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)

Date:

2024-08-14

prolyl-tRNA synthetase associated domain-containing protein similar to Clostridium sticklandii prolyl-tRNA editing protein ProX, which edits the amino acid moiety from incorrectly charged Ala-tRNA(Pro), preventing translation errors

Date:

2016-09-19