Protein Family Models

This domain is found in the tRNA(Ile) lysidine synthetase (TilS) protein. [1]. 18073113. Structural basis of the initial binding of tRNA(Ile) lysidine synthetase TilS with ATP and L-lysine. Kuratani M, Yoshikawa Y, Bessho Y, Higashijima K, Ishii T, Shibata R, Takahashi S, Yutani K, Yokoyama S;. Structure. 2007;15:1642-1653. [2]. 15894617. Structural basis for lysidine formation by ATP pyrophosphatase accompanied by a lysine-specific loop and a tRNA-recognition domain. Nakanishi K, Fukai S, Ikeuchi Y, Soma A, Sekine Y, Suzuki T, Nureki O;. Proc Natl Acad Sci U S A. 2005;102:7487-7492. (from Pfam)

Date:

2024-10-16

This domain is found in the tRNA(Ile) lysidine synthetase (TilS) protein. [1]. 18073113. Structural basis of the initial binding of tRNA(Ile) lysidine synthetase TilS with ATP and L-lysine. Kuratani M, Yoshikawa Y, Bessho Y, Higashijima K, Ishii T, Shibata R, Takahashi S, Yutani K, Yokoyama S;. Structure. 2007;15:1642-1653. [2]. 15894617. Structural basis for lysidine formation by ATP pyrophosphatase accompanied by a lysine-specific loop and a tRNA-recognition domain. Nakanishi K, Fukai S, Ikeuchi Y, Soma A, Sekine Y, Suzuki T, Nureki O;. Proc Natl Acad Sci U S A. 2005;102:7487-7492. (from Pfam)

Date:

2024-10-16

This family of proteins belongs to the PP-loop superfamily [1]. [1]. 7731953. A P-loop-like motif in a widespread ATP pyrophosphatase domain: implications for the evolution of sequence motifs and enzyme activity. Bork P, Koonin EV;. Proteins 1994;20:347-355. (from Pfam)

Date:

2024-10-16

tRNA lysidine(34) synthetase TilS ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner; cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine

Date:

2023-04-27

Gene:

tilS

Date:

2018-09-13

The only examples in which the wobble position of a tRNA must discriminate between G and A of mRNA are AUA (Ile) vs. AUG (Met) and UGA (stop) vs. UGG (Trp). In all bacteria, the wobble position of the tRNA(Ile) recognizing AUA is lysidine, a lysine derivative of cytidine. This family describes a protein domain found, apparently, in all bacteria in a single copy. Eukaryotic sequences appear to be organellar. The domain archictecture of this protein family is variable; some, including characterized proteins of E. coli and B. subtilis known to be tRNA(Ile)-lysidine synthetase, include a conserved 50-residue domain that many other members lack. This protein belongs to the ATP-binding PP-loop family ( PF01171). It appears in the literature and protein databases as TilS, YacA, and putative cell cycle protein MesJ (a misnomer).

Gene:

tilS

Date:

2024-05-17

TIGRFAMs model TIGR02432 describes the family of the N-terminal domain of tRNA(Ile)-lysidine synthetase. This family (TIGR02433) describes a small C-terminal domain of about 50 residues present in about half the members of family TIGR02432,and in no other protein. Characterized examples of tRNA(Ile)-lysidine synthetase from E. coli and Bacillus subtilis both contain this domain.

Gene:

tilS

Date:

2024-05-17