Protein Family Models

This domain corresponds to the catalytic like domain (CLM) in the beta chain of phe tRNA synthetase [1]. [1]. 21082706. Idiosyncrasy and identity in the prokaryotic Phe-system: crystal structure of E. coli phenylalanyl-tRNA synthetase complexed with phenylalanine and AMP. Mermershtain I, Finarov I, Klipcan L, Kessler N, Rozenberg H, Safro MG;. Protein Sci. 2011;20:160-167. (from Pfam)

Date:

2024-10-16

This domain is found in phenylalanine-tRNA synthetase beta subunits. [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:

2024-10-16

This domain is found in tRNA synthetase beta subunits as well as in some non tRNA synthetase proteins. [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:

2024-10-16

This is the anticodon binding domain found in some phenylalanyl tRNA synthetases. The domain has a ferredoxin fold [1,2]. [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. [2]. 9016717. The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe. Goldgur Y, Mosyak L, Reshetnikova L, Ankilova V, Lavrik O, Khodyreva S, Safro M;. Structure 1997;5:59-68. (from Pfam)

Date:

2024-10-16

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:

2024-10-16

Gene:

ytpR

Date:

2024-03-01

phenylalanine--tRNA ligase subunit beta is part of the enzyme complex that catalyzes the attachment of phenylalanine to tRNA(Phe)

Date:

2024-04-09

Every known example of the phenylalanyl-tRNA synthetase, except the monomeric form of mitochondrial, is an alpha 2 beta 2 heterotetramer. The beta subunits break into two subfamilies that are considerably different in sequence, length, and pattern of gaps. This HMM 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 amino end, however, so this HMM was built in fragment mode

Gene:

pheT

Date:

2024-05-15