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Links from Protein

Items: 13

1.

DALR anticodon-binding domain-containing protein

This all alpha helical domain is the anticodon binding domain in Arginyl and glycyl tRNA synthetase. This domain is known as the DALR domain after characteristic conserved amino acids [1]. [1]. 10447505. Evolution of aminoacyl-tRNA synthetases--analysis of unique. domain architectures and phylogenetic trees reveals a complex. history of horizontal gene transfer events.. Wolf YI, Aravind L, Grishin NV, Koonin EV;. Genome Res 1999;9:689-710. (from Pfam)

GO Terms:
Molecular Function:
arginine-tRNA ligase activity (GO:0004814)
Molecular Function:
ATP binding (GO:0005524)
Biological Process:
arginyl-tRNA aminoacylation (GO:0006420)
Date:
2024-08-14
Family Accession:
NF017555.5
Method:
HMM
2.

Arginyl tRNA synthetase N terminal domain

This domain is found at the amino terminus of Arginyl tRNA synthetase, also called additional domain 1 (Add-1). It is about 140 residues long and it has been suggested that this domain will be involved in tRNA recognition [1]. [1]. 9736621. L-arginine recognition by yeast arginyl-tRNA synthetase.. Cavarelli J, Delagoutte B, Eriani G, Gangloff J, Moras D;. EMBO J 1998;17:5438-5448. (from Pfam)

GO Terms:
Molecular Function:
nucleotide binding (GO:0000166)
Molecular Function:
arginine-tRNA ligase activity (GO:0004814)
Molecular Function:
ATP binding (GO:0005524)
Cellular Component:
cytoplasm (GO:0005737)
Biological Process:
arginyl-tRNA aminoacylation (GO:0006420)
Date:
2024-08-14
Family Accession:
NF015450.5
Method:
HMM
3.

arginine--tRNA ligase

Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only arginyl tRNA synthetase. (from Pfam)

Gene:
argS
Date:
2024-08-14
Family Accession:
NF012952.5
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.

arginine--tRNA ligase

arginine--tRNA ligase catalyzes the esterification reaction between L-arginine and its cognate tRNA

Date:
2024-04-09
Family Accession:
11414312
Method:
Sparcle
13.

arginine--tRNA ligase

This HMM recognizes arginyl-tRNA synthetase in every completed genome to date. An interesting feature of the alignment of all arginyl-tRNA synthetases is a fairly deep split between two families. One family includes archaeal, eukaryotic and organellar, spirochete, E. coli, and Synechocystis sp. The second, sharing a deletion of about 25 residues in the central region relative to the first, includes Bacillus subtilis, Aquifex aeolicus, the Mycoplasmas and Mycobacteria, and the Gram-negative bacterium Helicobacter pylori.

Gene:
argS
GO Terms:
Molecular Function:
arginine-tRNA ligase activity (GO:0004814)
Molecular Function:
ATP binding (GO:0005524)
Cellular Component:
cytoplasm (GO:0005737)
Biological Process:
arginyl-tRNA aminoacylation (GO:0006420)
Date:
2024-05-30
Family Accession:
TIGR00456.1
Method:
HMM
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