Protein Family Models

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)

Date:

2024-08-14

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)

Date:

2024-08-14

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.

Date:

2024-08-14

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

Date:

2020-10-26

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.

Gene:

lysS

Date:

2024-05-30