Searching in Clostridium tyrobutyricum FAM22553 (GCF_000816635.1)
Found 9 curated entries in PaperBLAST's database that match '2.6.1.6' as complete word(s).
These curated entries have 7 distinct sequences.
Running ublast with E ≤ 0.01
Found 4 relevant proteins in Clostridium tyrobutyricum FAM22553, or try another query
PN53_RS13955 WP_017751620.1: branched-chain amino acid transaminase is similar to: | PaperBLAST |
ilvE / O86428: branched-chain-amino-acid aminotransferase subunit (EC 2.6.1.6; EC 2.6.1.42) from Pseudomonas aeruginosa | 38% id, 98% cov |
IlvE / b3770: branched-chain-amino-acid aminotransferase (EC 2.6.1.1; EC 2.6.1.57; EC 2.6.1.27; EC 2.6.1.42; EC 2.6.1.6) from Escherichia coli | 38% id, 94% cov |
ilvE / A6UWA0: branched-chain amino acid aminotransferase subunit (EC 2.6.1.6; EC 2.6.1.42) from Methanococcus aeolicus | 38% id, 95% cov |
PN53_RS11800 WP_039653399.1: aminotransferase class IV is similar to: | PaperBLAST |
ilvE / A6UWA0: branched-chain amino acid aminotransferase subunit (EC 2.6.1.6; EC 2.6.1.42) from Methanococcus aeolicus | 28% id, 89% cov |
IlvE / b3770: branched-chain-amino-acid aminotransferase (EC 2.6.1.1; EC 2.6.1.57; EC 2.6.1.27; EC 2.6.1.42; EC 2.6.1.6) from Escherichia coli | 26% id, 89% cov |
ilvE / O86428: branched-chain-amino-acid aminotransferase subunit (EC 2.6.1.6; EC 2.6.1.42) from Pseudomonas aeruginosa | 32% id, 35% cov |
PN53_RS11780 WP_039653379.1: D-amino acid aminotransferase is similar to: | PaperBLAST |
ilvE / O86428: branched-chain-amino-acid aminotransferase subunit (EC 2.6.1.6; EC 2.6.1.42) from Pseudomonas aeruginosa | 26% id, 91% cov |
PN53_RS07220 WP_017752177.1: D-amino acid aminotransferase is similar to: | PaperBLAST |
ilvE / O86428: branched-chain-amino-acid aminotransferase subunit (EC 2.6.1.6; EC 2.6.1.42) from Pseudomonas aeruginosa | 25% id, 90% 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