Searching in Synechococcus elongatus PCC 7942 (SynE)
Found 8 curated entries in PaperBLAST's database that match '1.13.12.2' as complete word(s).
These curated entries have 8 distinct sequences.
Running ublast with E ≤ 0.01
Found 4 relevant proteins in Synechococcus elongatus PCC 7942, or try another query
| Synpcc7942_0369: putative flavin-containing monoamine oxidase is similar to: | PaperBLAST |
davB / B3IVI6: L-lysine monooxygenase monomer (EC 1.13.12.2) from Pseudomonas putida | 25% id, 87% cov |
Q88QV1: lysine 2-monooxygenase (EC 1.13.12.2) from Pseudomonas putida | 25% id, 87% cov |
Pf1N1B4_2505: Lysine 2-monooxygenase (EC 1.13.12.2) from Pseudomonas fluorescens | 33% id, 24% cov |
| Synpcc7942_1512: zeta-carotene desaturase is similar to: | PaperBLAST |
W6JQJ6: lysine 2-monooxygenase (EC 1.13.12.2); L-amino-acid oxidase (EC 1.4.3.2) from Pseudomonas sp. | 30% id, 23% cov |
AO353_07420: Lysine 2-monooxygenase (EC 1.13.12.2) from Pseudomonas fluorescens | 30% id, 23% cov |
AO356_14230: lysine 2-monooxygenase (EC 1.13.12.2) from Pseudomonas fluorescens | 30% id, 23% cov |
| Synpcc7942_0841: putative flavoprotein involved in K+ transport is similar to: | PaperBLAST |
davB / B3IVI6: L-lysine monooxygenase monomer (EC 1.13.12.2) from Pseudomonas putida | 42% id, 9% cov |
AO356_14230: lysine 2-monooxygenase (EC 1.13.12.2) from Pseudomonas fluorescens | 42% id, 9% cov |
Q88QV1: lysine 2-monooxygenase (EC 1.13.12.2) from Pseudomonas putida | 42% id, 9% cov |
| Synpcc7942_0623: thioredoxin reductase is similar to: | PaperBLAST |
davB / B3IVI6: L-lysine monooxygenase monomer (EC 1.13.12.2) from Pseudomonas putida | 40% id, 8% cov |
Q88QV1: lysine 2-monooxygenase (EC 1.13.12.2) from Pseudomonas putida | 40% id, 8% cov |
W6JQJ6: lysine 2-monooxygenase (EC 1.13.12.2); L-amino-acid oxidase (EC 1.4.3.2) from Pseudomonas sp. | 38% id, 8% 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