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OB-fold nucleic acid binding domain-containing protein
This family contains OB-fold domains that bind to nucleic acids [4]. The family includes the anti-codon binding domain of lysyl, aspartyl, and asparaginyl -tRNA synthetases (See Pfam:PF00152). Aminoacyl-tRNA synthetases catalyse the addition of an amino acid to the appropriate tRNA molecule EC:6.1.1.-. This family also includes part of RecG helicase involved in DNA repair. Replication factor A is a hetero-trimeric complex, that contains a subunit in this family [2,3]. This domain is also found at the C-terminus of bacterial DNA polymerase III alpha chain. [1]. 2047877. Class II aminoacyl transfer RNA synthetases: crystal structure. of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp).. Ruff M, Krishnaswamy S, Boeglin M, Poterszman A, Mitschler A,. Podjarny A, Rees B, Thierry JC, Moras D;. Science 1991;252:1682-1689.. [2]. 7760808. Rpa4, a homolog of the 34-kilodalton subunit of the replication. protein A complex.. Keshav KF, Chen C, Dutta A;. Mol Cell Biol 1995;15:3119-3128.. [3]. 8990123. Structure of the single-stranded-DNA-binding domain of. replication protein A bound to DNA.. Bochkarev A, Pfuetzner RA, Edwards AM, Frappier L;. Nature 1997;385:176-181.. [4]. 10829230. Protein fold recognition using sequence profiles and its. application in structural genomics.. Koonin EV, Wolf YI, Aravind L;. Adv Protein Chem 2000;54:245-275. (from Pfam)
amino acid--tRNA ligase-related protein
Members of this family contain a domain found in class II ligases of amino acids to tRNA for protein translation, but also in related proteins such as the EF-P-lysine lysyltransferase EpmA.
lysine--tRNA ligase
lysine--tRNA ligase, a class II aminoacyl-tRNA synthetase, catalyzes the specific aminoacylation of tRNA(Lys)
Class II; LysRS2; catalyzes a two-step reaction, first charging a lysine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; in Methanosarcina barkeri, LysRS2 charges both tRNA molecules for lysine that exist in this organism and in addition can charge the tRNAPyl with lysine in the presence of LysRS1
This model represents the lysyl-tRNA synthetases that are class II amino-acyl tRNA synthetases. It includes all eukaryotic and most bacterial examples of the enzyme, but not archaeal or spirochete forms.
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