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Items: 1 to 20 of 22

1.

Anticodon binding domain of methionyl tRNA ligase

This domain is found in methionyl tRNA ligase. The domain binds to the anticodon of the tRNA ligase. (from Pfam)

Date:
2024-08-14
Family Accession:
NF039287.4
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.

Putative tRNA binding domain

This domain is found in prokaryotic methionyl-tRNA synthetases, prokaryotic phenylalanyl tRNA synthetases the yeast GU4 nucleic-binding protein (G4p1 or p42, ARC1) [2], human tyrosyl-tRNA synthetase [1], and endothelial-monocyte activating polypeptide II. G4p1 binds specifically to tRNA form a complex with methionyl-tRNA synthetases [2]. In human tyrosyl-tRNA synthetase this domain may direct tRNA to the active site of the enzyme [2]. This domain may perform a common function in tRNA aminoacylation [1]. [1]. 9162081. Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine. Kleeman TA, Wei D, Simpson KL, First EA;. J Biol Chem 1997;272:14420-14425. [2]. 8895587. The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl-and glutamyl-tRNA synthetases. Simos G, Segref A, Fasiolo F, Hellmuth K, Shevchenko A, Mann M, Hurt EC;. EMBO J 1996;15:5437-5448. (from Pfam)

GO Terms:
Molecular Function:
tRNA binding (GO:0000049)
Date:
2024-10-16
Family Accession:
NF013734.5
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
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9.
new record, indexing in progress
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10.
new record, indexing in progress
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11.
new record, indexing in progress
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12.
new record, indexing in progress
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13.
new record, indexing in progress
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14.
new record, indexing in progress
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15.
new record, indexing in progress
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16.
new record, indexing in progress
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17.
new record, indexing in progress
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18.
new record, indexing in progress
Family Accession:
19.

methionine--tRNA ligase

MetRS; adds methionine to tRNA(Met) with cleavage of ATP to AMP and diphosphate; some MetRS enzymes form dimers depending on a C-terminal domain that is also found in other proteins such as Trbp111 in Aquifex aeolicus and the cold-shock protein CsaA from Bacillus subtilis while others do not; four subfamilies exist based on sequence motifs and zinc content

Gene:
metG
GO Terms:
Molecular Function:
tRNA binding (GO:0000049)
Molecular Function:
methionine-tRNA ligase activity (GO:0004825)
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
methionyl-tRNA aminoacylation (GO:0006431)
Date:
2021-07-22
Family Accession:
NF008900.0
Method:
HMM
20.

methionine--tRNA ligase

methionine--tRNA ligase aminoacylates the 2'-OH of the nucleotide at the 3' of tRNA(Met); it is required for elongation of protein synthesis as well as for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation

Date:
2023-01-12
Family Accession:
11485709
Method:
Sparcle
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