Family

Serine-tRNA ligase, type1 (IPR002317)

Short name: Ser-tRNA-ligase_type_1

Family relationships

None.

Description

Serine-tRNA ligase (EC:6.1.1.11) exists as monomer and belongs to the aminoacyl-tRNA synthetase class IIa [PMID: 7540217]. It catalyses the attachment of serine to tRNA (Ser). It is also able to aminoacylate tRNA (Sec) with serine, to form the misacylated tRNA L-seryl-tRNA (Sec), which will be further converted into selenocysteinyl-tRNA (Sec).

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 [PMID: 10704480,PMID: 12458790]. These proteins differ widely in size and oligomeric state, and have limited sequence homology [PMID: 2203971]. 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 [PMID: 10673435]. Class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet fold flanked by alpha-helices [PMID: 8364025], and are mostly dimeric or multimeric, containing at least three conserved regions [PMID: 8274143, PMID: 2053131, PMID: 1852601]. 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 [PMID: 10447505].

GO terms

Biological Process

GO:0006434 seryl-tRNA aminoacylation

Molecular Function

GO:0005524 ATP binding
GO:0000166 nucleotide binding
GO:0004828 serine-tRNA ligase activity

Cellular Component

GO:0005737 cytoplasm

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PANTHER
HAMAP
PANTHER
TIGRFAMs
PRINTS
PIRSF