Protein Family Models

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)

Date:

2024-08-14

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)

Date:

2024-08-14

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

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

Date:

2024-04-09

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

Date:

2024-05-30