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Items: 20

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:
2024-10-16

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:
2024-10-16

Family Accession:
NF019869.5
Method:
HMM

4.

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

5.

tRNA synthetases class I (C) catalytic domain

This family includes only cysteinyl tRNA synthetases. (from Pfam)

Date:
2024-08-14

Family Accession:
NF013565.5
Method:
HMM

6.

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

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.
new record, indexing in progress
Family Accession:
14.
new record, indexing in progress
Family Accession:
15.
new record, indexing in progress
Family Accession:
16.
new record, indexing in progress
Family Accession:
17.
new record, indexing in progress
Family Accession:
18.

isoleucine--tRNA ligase

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

Date:
2024-04-09

Family Accession:
11414613
Method:
Sparcle

19.

isoleucine--tRNA ligase

Gene:
ileS2
Date:
2018-10-10

Family Accession:
NBR006932
Method:
BlastRule

20.

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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