Searching in Thermus aquaticus YT-1 (GCF_001280255.1)
Found 1 curated entries in PaperBLAST's database that match '2.6.1.124' as complete word(s).
These curated entries have 1 distinct sequences.
Running ublast with E ≤ 0.01
Found 5 relevant proteins in Thermus aquaticus YT-1, or try another query
| BVI061214_RS04805 BVI061214_00912 WP_053767489.1: aspartate aminotransferase family protein is similar to: | PaperBLAST |
lysJ / Q4JAP8: [amino group carrier protein]-C-terminal-L-glutamyl-γ-L-lysine aminotransferase (EC 2.6.1.118; EC 2.6.1.124) from Sulfolobus acidocaldarius | 47% id, 97% cov |
| BVI061214_RS10655 BVI061214_02105 WP_053768359.1: aspartate aminotransferase family protein is similar to: | PaperBLAST |
lysJ / Q4JAP8: [amino group carrier protein]-C-terminal-L-glutamyl-γ-L-lysine aminotransferase (EC 2.6.1.118; EC 2.6.1.124) from Sulfolobus acidocaldarius | 35% id, 97% cov |
| BVI061214_RS10150 BVI061214_01997 WP_053768287.1: acetyl ornithine aminotransferase family protein is similar to: | PaperBLAST |
lysJ / Q4JAP8: [amino group carrier protein]-C-terminal-L-glutamyl-γ-L-lysine aminotransferase (EC 2.6.1.118; EC 2.6.1.124) from Sulfolobus acidocaldarius | 31% id, 95% cov |
| BVI061214_RS09220 BVI061214_01810 WP_053768137.1: aminotransferase class III-fold pyridoxal phosphate-dependent enzyme is similar to: | PaperBLAST |
lysJ / Q4JAP8: [amino group carrier protein]-C-terminal-L-glutamyl-γ-L-lysine aminotransferase (EC 2.6.1.118; EC 2.6.1.124) from Sulfolobus acidocaldarius | 30% id, 95% cov |
| hemL BVI061214_RS08935 BVI061214_01745 WP_053768090.1: glutamate-1-semialdehyde 2,1-aminomutase is similar to: | PaperBLAST |
lysJ / Q4JAP8: [amino group carrier protein]-C-terminal-L-glutamyl-γ-L-lysine aminotransferase (EC 2.6.1.118; EC 2.6.1.124) from Sulfolobus acidocaldarius | 33% id, 71% cov |
The hits are sorted by %identity * %coverage (highest first)
Running ublast against the 6-frame translation. All reading frames of at least 30 codons are included.
Found hits to 4 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory