Protein Domain : IPR004532

Type:  Family Name:  Phenylalanine-tRNA ligase, class IIc, beta subunit
Description:  Phenylalanine-tRNA ligase () is an alpha2/beta2 tetramer composed of 2 subunits that belongs to class IIc. In eubacteria, a small subunit (pheS gene) can be designated as beta (E. coli) or alpha subunit (see ). Reciprocally the large subunit (pheT gene) can be designated as alpha (E. coli) or beta. In all other kingdoms the two subunits have equivalent length in eukaryota, and can be identified by specific signatures. The enzyme from Thermus thermophilushas an alpha 2 beta 2 type quaternary structure and is one of the most complicated members of the synthetase family. Identification of phenylalanine-tRNA ligase as a member of class II aaRSs was based only on sequence alignment of the small alpha-subunit with other ligases [].This family describes the beta subunit. The beta subunits break into two subfamilies that are considerably different in sequence, length, and pattern of gaps (see also ). This family represents the subfamily that includes the beta subunit from bacteria other than spirochetes, as well as a chloroplast-encoded form from Porphyra purpurea. The chloroplast-derived sequence is considerably shorter at the N-terminal.The aminoacyl-tRNA synthetase (also known as aminoacyl-tRNA ligase) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. These proteins differ widely in size and oligomeric state, and have limited sequence homology []. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric []. Class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet fold flanked by alpha-helices [], and are mostly dimeric or multimeric, containing at least three conserved regions [, , ]. However, tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan and valine belong to class I synthetases. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, lysine, phenylalanine, proline, serine, and threonine belong to class-II synthetases. Based on their mode of binding to the tRNA acceptor stem, both classes of tRNA synthetases have been subdivided into three subclasses, designated 1a, 1b, 1c and 2a, 2b, 2c. Short Name:  Phe-tRNA-ligase_IIc_bsu
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0 Child Features

6 Contains

DB identifier Type Name
IPR005146 Domain B3/B4 tRNA-binding domain
IPR005147 Domain tRNA synthetase, B5-domain
IPR009061 Domain Putative DNA-binding domain
IPR020825 Domain Phenylalanyl-tRNA synthetase, B3/B4
IPR002547 Domain tRNA-binding domain
IPR005121 Domain Phenylalanine-tRNA ligase, beta subunit, ferrodoxin-fold anticodon-binding

2 Cross Referencess

Identifier
TIGR00472
MF_00283

0 Found In

5 GO Annotations

GO Term Gene Name
GO:0000287 IPR004532
GO:0004826 IPR004532
GO:0005524 IPR004532
GO:0006432 IPR004532
GO:0005737 IPR004532

5 Ontology Annotations

GO Term Gene Name
GO:0000287 IPR004532
GO:0004826 IPR004532
GO:0005524 IPR004532
GO:0006432 IPR004532
GO:0005737 IPR004532

0 Parent Features

10 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
35700.m000026 B9TFK1 PAC:16826705 Ricinus communis 381  
28809.m000038 B9T9G4 PAC:16801719 Ricinus communis 421  
Brdisv1pangenome1010055m.p PAC:33621573 Brachypodium distachyon Pangenome 678  
Brdisv1pangenome1010040m.p PAC:33608287 Brachypodium distachyon Pangenome 463  
Brdisv1BdTR11A1047852m.p PAC:35692062 Brachypodium distachyon BdTR11a 802  
Brdisv1BdTR11A1047819m.p PAC:35692766 Brachypodium distachyon BdTR11a 463  
35176.m000015 B9TCP4 PAC:16826507 Ricinus communis 608  
35176.m000015 B9TCP4 PAC:16826507 Ricinus communis 608  
Araha.11756s0350.1.p PAC:28856437 Arabidopsis halleri 790  
Araha.11756s0350.1.p PAC:28856437 Arabidopsis halleri 790  

7 Publications

First Author Title Year Journal Volume Pages PubMed ID
            8364025
            8274143
            1852601
            2053131
            10673435
            2203971
            8199244