Protein Family Models

The catalytically active from of threonyl/alanyl tRNA synthetase is a dimer. Within the tRNA synthetase class II dimer, the bound tRNA interacts with both monomers making specific interactions with the catalytic domain, the C-terminal domain, and this domain (the second additional domain). The second additional domain is comprised of a pair of perpendicularly orientated antiparallel beta sheets, of four and three strands, respectively, that surround a central alpha helix that forms the core of the domain [1]. [1]. 10319817. The structure of threonyl-tRNA synthetase-tRNA(Thr) complex. enlightens its repressor activity and reveals an essential zinc. ion in the active site.. Sankaranarayanan R, Dock-Bregeon AC, Romby P, Caillet J,. Springer M, Rees B, Ehresmann C, Ehresmann B, Moras D;. Cell 1999;97:371-381. (from Pfam)

Date:

2024-07-11

This HMM hits a C-terminal region, thought to be the anticodin-binding domain, of tRNA ligases for amino acids His, Gly, Thr, and Pro. Proteins named by this HMM are mostly partials, scoring below cutoffs of more specific models because incomplete sequences generate insufficient scores.

Date:

2024-07-10

The TGS domain is named after ThrRS, GTPase, and SpoT [1]. Interestingly, TGS domain was detected also at the amino terminus of the uridine kinase from the spirochaete Treponema pallidum (but not any other organism, including the related spirochaete Borrelia burgdorferi). TGS is a small domain that consists of ~50 amino acid residues and is predicted to possess a predominantly beta-sheet structure. There is no direct information on the functions of the TGS domain, but its presence in two types of regulatory proteins (the GTPases and guanosine polyphosphate phosphohydrolases/synthetases) suggests a ligand (most likely nucleotide)-binding, regulatory role [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.. [2]. 10319817. The structure of threonyl-tRNA synthetase-tRNA(Thr) complex. enlightens its repressor activity and reveals an essential zinc. ion in the active site.. Sankaranarayanan R, Dock-Bregeon AC, Romby P, Caillet J,. Springer M, Rees B, Ehresmann C, Ehresmann B, Moras D;. Cell 1999;97:371-381. (from Pfam)

Date:

2024-07-10

This HMM finds multiple types of aminoacyl--tRNA ligase, such as those for Thr, Pro, His, and Ser in Escherichia coli. Because equivalog-level HMMs exist to identify full-length members of the tRNA ligase families, any protein receiving annotation from this HMM is most likely to be either a partial sequence or a tRNA ligase-related protein involved in some process other than protein translation on the ribosome.

Date:

2024-07-09

threonine--tRNA ligase catalyzes the attachment of threonine to the 3' OH group of ribose of tRNA(Thr)

Date:

2024-04-09

This HMM represents the threonyl-tRNA synthetase found in most organisms. This protein is a class II tRNA synthetase, and is recognized by the pfam HMM tRNA-synt_2b. Note that B. subtilis has closely related isozymes thrS and thrZ. The N-terminal regions are quite dissimilar between archaeal and eubacterial forms, while some eukaryotic forms are missing sequence there altogether. .

Gene:

thrS

Date:

2024-05-30