Searching in Herbaspirillum seropedicae SmR1 (HerbieS)
Found 6 curated entries in PaperBLAST's database that match '6.1.1.24' as complete word(s).
These curated entries have 6 distinct sequences.
Running ublast with E ≤ 0.01
Found 3 relevant proteins in Herbaspirillum seropedicae SmR1, or try another query
| HSERO_RS18065: glutaminyl-tRNA synthetase is similar to: | PaperBLAST |
P00962: glutamine-tRNA ligase (EC 6.1.1.18); glutamate-tRNAGln ligase (EC 6.1.1.24) from Escherichia coli | 53% id, 99% cov |
CCNA_01982: glutamyl-tRNA(Glx) synthetase (EC 6.1.1.24) from Caulobacter crescentus | 27% id, 63% cov |
SYEM_HUMAN / Q5JPH6: Nondiscriminating glutamyl-tRNA synthetase EARS2, mitochondrial; Glutamate--tRNA(Gln) ligase EARS2, mitochondrial; Glutamyl-tRNA synthetase; GluRS; Mitochondrial glutamyl-tRNA synthetase; mtGluRS; EC 6.1.1.24; EC 6.1.1.17 from Homo sapiens | 23% id, 46% cov |
| HSERO_RS15460: glutamyl-tRNA synthetase is similar to: | PaperBLAST |
CCNA_01982: glutamyl-tRNA(Glx) synthetase (EC 6.1.1.24) from Caulobacter crescentus | 43% id, 98% cov |
gltX / P22250: glutamyl-tRNAGlx synthetase (EC 6.1.1.17; EC 6.1.1.24) from Bacillus subtilis | 39% id, 100% cov |
Q9X2I8: glutamate-tRNAGln ligase (EC 6.1.1.24) from Thermotoga maritima | 34% id, 94% cov |
| HSERO_RS17850: glutamyl-Q tRNA(Asp) ligase is similar to: | PaperBLAST |
CCNA_01982: glutamyl-tRNA(Glx) synthetase (EC 6.1.1.24) from Caulobacter crescentus | 34% id, 59% cov |
SYEM_HUMAN / Q5JPH6: Nondiscriminating glutamyl-tRNA synthetase EARS2, mitochondrial; Glutamate--tRNA(Gln) ligase EARS2, mitochondrial; Glutamyl-tRNA synthetase; GluRS; Mitochondrial glutamyl-tRNA synthetase; mtGluRS; EC 6.1.1.24; EC 6.1.1.17 from Homo sapiens | 38% id, 49% cov |
gltX / P22250: glutamyl-tRNAGlx synthetase (EC 6.1.1.17; EC 6.1.1.24) from Bacillus subtilis | 31% id, 57% 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 3 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory