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Links from Protein

Items: 12

1.

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
2.

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:
2024-10-16
Family Accession:
NF019869.5
Method:
HMM
3.

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:
2024-10-16
Family Accession:
NF012361.5
Method:
HMM
4.
new record, indexing in progress
Family Accession:
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.

valine--tRNA ligase

valine--tRNA ligase catalyzes the attachment of valine to tRNA(Val)

Date:
2017-09-28
Family Accession:
11486468
Method:
Sparcle
11.

valine--tRNA ligase

ValRS; converts valine ATP and tRNA(Val) to AMP PPi and valyl-tRNA(Val); class-I aminoacyl-tRNA synthetase type 1 subfamily; has a posttransfer editing process to hydrolyze mischarged Thr-tRNA(Val) which is done by the editing domain

Date:
2020-10-26
Family Accession:
NF009687.0
Method:
HMM
12.

valine--tRNA ligase

The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase.

Gene:
valS
GO Terms:
Molecular Function:
nucleotide binding (GO:0000166)
Molecular Function:
valine-tRNA ligase activity (GO:0004832)
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
valyl-tRNA aminoacylation (GO:0006438)
Date:
2024-05-15
Family Accession:
TIGR00422.1
Method:
HMM
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