Searching in Phaeobacter inhibens BS107 (Phaeo)
Found 31 curated entries in PaperBLAST's database that match '3.1.2.6' as complete word(s).
These curated entries have 20 distinct sequences.
Running ublast with E ≤ 0.01
Found 5 relevant proteins in Phaeobacter inhibens BS107, or try another query
| PGA1_c31600: S-formylglutathione hydrolase FghA is similar to: | PaperBLAST |
YeiG / b2154: S-formylglutathione hydrolase / S-lactoylglutathione hydrolase (EC 3.1.2.12; EC 3.1.2.6) from Escherichia coli | 54% id, 100% cov |
| PGA1_c25140: hydroxyacylglutathione hydrolase GloB is similar to: | PaperBLAST |
Q8YZ99: hydroxyacylglutathione hydrolase (EC 3.1.2.6) from Nostoc sp. | 42% id, 100% cov |
GLO2C_ARATH / O24496: Hydroxyacylglutathione hydrolase cytoplasmic; Glyoxalase II; Glx II; EC 3.1.2.6 from Arabidopsis thaliana | 38% id, 99% cov |
GLO2_ECOLI / P0AC84: Hydroxyacylglutathione hydrolase GloB; Glyoxalase II; Glx II; EC 3.1.2.6 from Escherichia coli | 37% id, 100% cov |
| PGA1_c12760: beta-lactamase hydrolase-like protein Blh is similar to: | PaperBLAST |
A0A0D1GCF8: hydroxyacylglutathione hydrolase (EC 3.1.2.6) from Staphylococcus aureus | 35% id, 68% cov |
Q940L0: hydroxyacylglutathione hydrolase (EC 3.1.2.6) from Oryza sativa | 27% id, 64% cov |
GLO2N_ARATH / Q9SID3: Hydroxyacylglutathione hydrolase 2, mitochondrial; Glyoxalase II; Glx II; EC 3.1.2.6 from Arabidopsis thaliana | 30% id, 46% cov |
| PGA1_c13050: Zn-dependent hydrolases, including glyoxylases is similar to: | PaperBLAST |
GLO22_ECOLI / P75849: Hydroxyacylglutathione hydrolase GloC; Accessory type II glyoxalase; Glyoxalase II 2; GlxII-2; EC 3.1.2.6 from Escherichia coli | 30% id, 78% cov |
| PGA1_c10580: ribonuclease J 1 is similar to: | PaperBLAST |
A0A0D1GCF8: hydroxyacylglutathione hydrolase (EC 3.1.2.6) from Staphylococcus aureus | 37% id, 33% 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