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Links from Protein

Items: 14

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.

zinc finger domain-containing protein

This zinc binding domain is found at the C-terminus of isoleucyl tRNA synthetase and the enzyme Formamidopyrimidine-DNA glycosylase EC:3.2.2.23. (from Pfam)

GO Terms:
Molecular Function:
zinc ion binding (GO:0008270)
Date:
2024-08-14

Family Accession:
NF018531.5
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:
2024-10-16

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.

isoleucine--tRNA ligase

isoleucine--tRNA ligase catalyzes the attachment of isoleucine to tRNA(Ile)

Date:
2024-04-09

Family Accession:
11414613
Method:
Sparcle

14.

isoleucine--tRNA ligase

The isoleucyl tRNA synthetase (IleS) is a class I amino acyl-tRNA ligase and is particularly closely related to the valyl tRNA synthetase. It catalyzes the formation of isoleucyl-tRNA(Ile) from isoleucine and tRNA(Ile). Since isoleucine and other amino acids such as valine are similar, there is additional editing function in this enzyme; one is involved in hydrolysis of activated valine-AMP and the other is involved in deacylation of mischarged Val-tRNA(Ile). There are two active sites, one for aminoacylation and one for editing. Some organisms carry two different copies of this enzyme

Gene:
ileS
GO Terms:
Molecular Function:
nucleotide binding (GO:0000166)
Molecular Function:
isoleucine-tRNA ligase activity (GO:0004822)
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
isoleucyl-tRNA aminoacylation (GO:0006428)
Date:
2024-05-13

Family Accession:
TIGR00392.1
Method:
HMM

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