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Items: 14

1.

Leucyl-tRNA synthetase, editing domain

This entry represents the editing domain in Leucine-tRNA ligase or Leucyl-tRNA synthetase, EC:6.1.1.4. Paper describing PDB structure 1h3n. [1]. 10811626. The 2 A crystal structure of leucyl-tRNA synthetase and its. complex with a leucyl-adenylate analogue.. Cusack S, Yaremchuk A, Tukalo M;. EMBO J. 2000;19:2351-2361.. Paper describing PDB structure 1obc. [2]. 12718881. Structural and mechanistic basis of pre- and posttransfer. editing by leucyl-tRNA synthetase.. Lincecum TL Jr, Tukalo M, Yaremchuk A, Mursinna RS, Williams AM,. Sproat BS, Van Den Eynde W, Link A, Van Calenbergh S, Grotli M,. Martinis SA, Cusack S;. Mol Cell. 2003;11:951-963.. Paper describing PDB structure 1wk9. [3]. 15970591. Structural basis for non-cognate amino acid discrimination by. the valyl-tRNA synthetase editing domain.. Fukunaga R, Yokoyama S;. J Biol Chem. 2005;280:29937-29945.. Paper describing PDB structure 1wkb. [4]. 15663927. Crystal structure of leucyl-tRNA synthetase from the archaeon. Pyrococcus horikoshii reveals a novel editing domain. orientation.. Fukunaga R, Yokoyama S;. J Mol Biol. 2005;346:57-71.. Paper describing PDB structure 2ajg. [5]. 16277600. Crystal structures of the editing domain of Escherichia coli. leucyl-tRNA synthetase and its complexes with Met and Ile reveal. a lock-and-key mechanism for amino acid discrimination.. Liu Y, Liao J, Zhu B, Wang ED, Ding J;. Biochem J. 2006;394:399-407. (from Pfam)

GO Terms:
Molecular Function:
aminoacyl-tRNA editing activity (GO:0002161)
Biological Process:
tRNA aminoacylation for protein translation (GO:0006418)
Date:
2024-08-14

Family Accession:
NF024990.5
Method:
HMM

2.

class I tRNA ligase family protein

This family includes methionyl tRNA synthetases. (from Pfam)

GO Terms:
Molecular Function:
nucleotide binding (GO:0000166)
Molecular Function:
aminoacyl-tRNA ligase activity (GO:0004812)
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
tRNA aminoacylation for protein translation (GO:0006418)
Date:
2024-08-14

Family Accession:
NF020892.5
Method:
HMM

3.

class I tRNA ligase family protein

This domain is found mainly hydrophobic tRNA synthetases. The domain binds to the anticodon of the tRNA ligase. [1]. 11114335. Structural basis for double-sieve discrimination of L-valine. from L-isoleucine and L-threonine by the complex of tRNA(Val). and valyl-tRNA synthetase.. Fukai S, Nureki O, Sekine S, Shimada A, Tao J, Vassylyev DG,. Yokoyama S;. Cell 2000;103:793-803. (from Pfam)

GO Terms:
Molecular Function:
aminoacyl-tRNA ligase activity (GO:0004812)
Biological Process:
tRNA aminoacylation for protein translation (GO:0006418)
Date:
2024-08-14

Family Accession:
NF019869.5
Method:
HMM

4.

class I tRNA ligase family protein

Other tRNA synthetase sub-families are too dissimilar to be included. Paper describing PDB structure 1a8h. [1]. 10673435. The 2.0 A crystal structure of Thermus thermophilus. methionyl-tRNA synthetase reveals two RNA-binding modules.. Sugiura I, Nureki O, Ugaji-Yoshikawa Y, Kuwabara S, Shimada A,. Tateno M, Lorber B, Giege R, Moras D, Yokoyama S, Konno M;. Structure. 2000;8:197-208.. Paper describing PDB structure 1f4l. [2]. 11243794. How methionyl-tRNA synthetase creates its amino acid recognition. pocket upon L-methionine binding.. Serre L, Verdon G, Choinowski T, Hervouet N, Risler JL, Zelwer. C;. J Mol Biol. 2001;306:863-876.. Paper describing PDB structure 1ffy. [3]. 10446055. Insights into editing from an ile-tRNA synthetase structure with. tRNAile and mupirocin.. Silvian LF, Wang J, Steitz TA;. Science. 1999;285:1074-1077.. Paper describing PDB structure 1gax. [4]. 11114335. Structural basis for double-sieve discrimination of L-valine. from L-isoleucine and L-threonine by the complex of tRNA(Val). and valyl-tRNA synthetase.. Fukai S, Nureki O, Sekine S, Shimada A, Tao J, Vassylyev DG,. Yokoyama S;. Cell 2000;103:793-803.. Paper describing PDB structure 1h3n. [5]. 10811626. The 2 A crystal structure of leucyl-tRNA synthetase and its. complex with a leucyl-adenylate analogue.. Cusack S, Yaremchuk A, Tukalo M;. EMBO J. 2000;19:2351-2361. (from Pfam)

GO Terms:
Molecular Function:
nucleotide binding (GO:0000166)
Molecular Function:
aminoacyl-tRNA ligase activity (GO:0004812)
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
tRNA aminoacylation for protein translation (GO:0006418)
Date:
2024-08-14

Family Accession:
NF012361.5
Method:
HMM

5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.
new record, indexing in progress
Family Accession:
8.
new record, indexing in progress
Family Accession:
9.
new record, indexing in progress
Family Accession:
10.
new record, indexing in progress
Family Accession:
11.
new record, indexing in progress
Family Accession:
12.
new record, indexing in progress
Family Accession:
13.

leucine--tRNA ligase

leucine--tRNA ligase attaches leucine to the ribose 3' OH group of tRNA(Leu)

Date:
2024-04-09

Family Accession:
11423059
Method:
Sparcle

14.

leucine--tRNA ligase

The leucyl-tRNA synthetases belong to two families so broadly different that they are represented by separate models. This model includes both eubacterial and mitochondrial leucyl-tRNA synthetases. It generates higher scores for some valyl-tRNA synthetases than for any archaeal or eukaryotic cytosolic leucyl-tRNA synthetase. Note that the enzyme from Aquifex aeolicus is split into alpha and beta chains; neither chain is long enough to score above the trusted cutoff, but the alpha chain scores well above the noise cutoff. The beta chain must be found by a model and search designed for partial length matches.

Gene:
leuS
GO Terms:
Molecular Function:
nucleotide binding (GO:0000166)
Molecular Function:
leucine-tRNA ligase activity (GO:0004823)
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
leucyl-tRNA aminoacylation (GO:0006429)
Date:
2024-05-13

Family Accession:
TIGR00396.1
Method:
HMM

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