Protein Family Models

This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase. (from Pfam)

Date:

2024-08-14

This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase. (from Pfam)

Date:

2024-08-14

This domain family is found in eukaryotes, and is approximately 120 amino acids in length. There are two conserved sequence motifs: YGL and LRDR. This family is related to GATase enzyme domains. (from Pfam)

Date:

2024-08-14

This family of proteins participate in the biosynthesis of 7-carboxy-7-deazaguanine. They catalyse the conversion of 7-deaza-7-carboxyguanine to preQ0 [1-3]. [1]. 14660578. Identification of four genes necessary for biosynthesis of the modified nucleoside queuosine. Reader JS, Metzgar D, Schimmel P, de Crecy-Lagard V;. J Biol Chem. 2004;279:6280-6285. [2]. 16199558. Genetic analysis identifies a function for the queC (ybaX) gene product at an initial step in the queuosine biosynthetic pathway in Escherichia coli. Gaur R, Varshney U;. J Bacteriol. 2005;187:6893-6901. [3]. 19354300. The deazapurine biosynthetic pathway revealed: in vitro enzymatic synthesis of PreQ(0) from guanosine 5'-triphosphate in four steps. McCarty RM, Somogyi A, Lin G, Jacobsen NE, Bandarian V;. Biochemistry. 2009;48:3847-3852. [4]. 18491386. Crystal structure of QueC from Bacillus subtilis: an enzyme involved in preQ1 biosynthesis. Cicmil N, Huang RH;. Proteins. 2008;72:1084-1088. (from Pfam)

Date:

2024-10-16

Most members of this family are asparagine synthase, which catalyzes conversion of aspartate to asparagine. Exceptions that score well against the HMM include isopeptide bond formation proteins for lasso peptide biosynthesis. But note that many additional proteins, such as the 7-cyano-7-deazaguanine synthase QueC, hit with scores barely above the model's cutoff scores to N-terminal regions about 60 amino acids long, whereas the full length of the model is 355.

Date:

2024-08-14

This HMM describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff.

Gene:

asnB

Date:

2021-04-27

asparagine synthetase B (glutamine-hydrolyzing) family protein may catalyze the ATP-dependent conversion of aspartate into asparagine, using glutamine as a source of nitrogen

Date:

2024-07-18