Searching in Sulfurivirga caldicuralii DSM 17737 (GCF_900141795.1)
Found 35 curated entries in PaperBLAST's database that match '2.3.1.1' as complete word(s).
These curated entries have 28 distinct sequences.
Running ublast with E ≤ 0.01
Found 3 relevant proteins in Sulfurivirga caldicuralii DSM 17737, or try another query
| argJ BUQ81_RS02245 SAMN05443662_0450 WP_074200756.1: bifunctional glutamate N-acetyltransferase/amino-acid acetyltransferase ArgJ is similar to: | PaperBLAST |
argJ: glutamate N-acetyltransferase/amino-acid acetyltransferase; EC 2.3.1.35 2.3.1.1 from Neisseria gonorrhoeae | 50% id, 100% cov |
ARGJ_GEOSE / Q07908: Arginine biosynthesis bifunctional protein ArgJ; EC 2.3.1.35; EC 2.3.1.1 from Geobacillus stearothermophilus | 43% id, 93% cov |
ARGJ_HALH5 / Q9K8V3: Arginine biosynthesis bifunctional protein ArgJ; EC 2.3.1.35; EC 2.3.1.1 from Halalkalibacterium halodurans | 41% id, 95% cov |
| argA BUQ81_RS02290 SAMN05443662_0460 WP_074200765.1: amino-acid N-acetyltransferase is similar to: | PaperBLAST |
P22567: amino-acid N-acetyltransferase (EC 2.3.1.1) from Pseudomonas aeruginosa | 41% id, 99% cov |
ARGA_ECOLI / P0A6C5: Amino-acid acetyltransferase; N-acetylglutamate synthase; AGS; NAGS; EC 2.3.1.1 from Escherichia coli | 38% id, 97% cov |
DVU1587: N-acetylglutamate synthase (EC 2.3.1.1) from Desulfovibrio vulgaris | 39% id, 82% cov |
| argB BUQ81_RS01510 SAMN05443662_0301 WP_074200628.1: acetylglutamate kinase is similar to: | PaperBLAST |
Q87EL2: amino-acid N-acetyltransferase (EC 2.3.1.1) from Xylella fastidiosa | 32% id, 64% cov |
P22567: amino-acid N-acetyltransferase (EC 2.3.1.1) from Pseudomonas aeruginosa | 30% id, 64% cov |
ABZR86_RS08705: N-acetylglutamate synthase; N-acetylglutamate kinase (EC 2.3.1.1; EC 2.7.2.8) from Dyella japonica | 28% id, 63% 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