Biomaterial Database

Internal sequence homology in E. coli isoleucyl- and valyl-tRNA synthetases. 1976

F Kalousek, and W Konigsberg

UI	MeSH Term	Description	Entries
D007533	Isoleucine-tRNA Ligase	An enzyme that activates isoleucine with its specific transfer RNA. EC 6.1.1.5.	Isoleucyl T RNA Synthetase,Isoleucyl- tRNA Synthetase ILS1,Isoleucyl-tRNA Synthetase 1,Isoleucyl-tRNA Synthetase ILES1,Ile-tRNA Ligase,Isoleucyl-tRNA Synthetase,1, Isoleucyl-tRNA Synthetase,ILES1, Isoleucyl-tRNA Synthetase,Ile tRNA Ligase,Isoleucine tRNA Ligase,Isoleucyl tRNA Synthetase,Isoleucyl tRNA Synthetase 1,Isoleucyl tRNA Synthetase ILES1,Isoleucyl tRNA Synthetase ILS1,Ligase, Ile-tRNA,Ligase, Isoleucine-tRNA,Synthetase 1, Isoleucyl-tRNA,Synthetase ILES1, Isoleucyl-tRNA,Synthetase, Isoleucyl-tRNA
D010446	Peptide Fragments	Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.	Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D004926	Escherichia coli	A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.	Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000596	Amino Acids	Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.	Amino Acid,Acid, Amino,Acids, Amino
D000604	Amino Acyl-tRNA Synthetases	A subclass of enzymes that aminoacylate AMINO ACID-SPECIFIC TRANSFER RNA with their corresponding AMINO ACIDS.	Amino Acyl T RNA Synthetases,Amino Acyl-tRNA Ligases,Aminoacyl Transfer RNA Synthetase,Aminoacyl-tRNA Synthetase,Transfer RNA Synthetase,tRNA Synthetase,Acyl-tRNA Ligases, Amino,Acyl-tRNA Synthetases, Amino,Amino Acyl tRNA Ligases,Amino Acyl tRNA Synthetases,Aminoacyl tRNA Synthetase,Ligases, Amino Acyl-tRNA,RNA Synthetase, Transfer,Synthetase, Aminoacyl-tRNA,Synthetase, Transfer RNA,Synthetase, tRNA,Synthetases, Amino Acyl-tRNA
D001411	Geobacillus stearothermophilus	A species of GRAM-POSITIVE ENDOSPORE-FORMING BACTERIA in the family BACILLACEAE, found in soil, hot springs, Arctic waters, ocean sediments, and spoiled food products.	Bacillus stearothermophilus,Bacillus thermoliquefaciens
D013045	Species Specificity	The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.	Species Specificities,Specificities, Species,Specificity, Species
D014637	Valine-tRNA Ligase	An enzyme that activates valine with its specific transfer RNA. EC 6.1.1.9	Valyl T RNA Synthetase,Val-tRNA Ligase,Valyl-tRNA Synthetase,Ligase, Val-tRNA,Ligase, Valine-tRNA,Synthetase, Valyl-tRNA,Val tRNA Ligase,Valine tRNA Ligase,Valyl tRNA Synthetase