Searching in Caulobacter crescentus NA1000 (Caulo)
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 5 relevant proteins in Caulobacter crescentus NA1000, or try another query
CCNA_03162: bifunctional ornithine acetyltransferase/N-acetylglutamate synthase is similar to: | PaperBLAST |
argJ: glutamate N-acetyltransferase/amino-acid acetyltransferase; EC 2.3.1.35 2.3.1.1 from Neisseria gonorrhoeae | 42% id, 97% cov |
ARGJ_GEOSE / Q07908: Arginine biosynthesis bifunctional protein ArgJ; EC 2.3.1.35; EC 2.3.1.1 from Geobacillus stearothermophilus | 38% id, 97% cov |
ARGJ_THENN / Q9Z4S1: Arginine biosynthesis bifunctional protein ArgJ; EC 2.3.1.35; EC 2.3.1.1 from Thermotoga neapolitana | 38% id, 96% cov |
CCNA_00984: phosphinothricin N-acetyltransferase is similar to: | PaperBLAST |
MnaT / b1448: L-amino acid N-acyltransferase (EC 2.3.1.1) from Escherichia coli | 41% id, 99% cov |
CCNA_01681: RimI-like acetyltransferase is similar to: | PaperBLAST |
MnaT / b1448: L-amino acid N-acyltransferase (EC 2.3.1.1) from Escherichia coli | 27% id, 94% cov |
CCNA_00285: acetylglutamate kinase is similar to: | PaperBLAST |
Q0ASS9: amino-acid N-acetyltransferase (EC 2.3.1.1); acetylglutamate kinase (EC 2.7.2.8) from Maricaulis maris | 32% id, 61% cov |
P22567: amino-acid N-acetyltransferase (EC 2.3.1.1) from Pseudomonas aeruginosa | 29% 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, 64% cov |
CCNA_03989: MarR-family HTH transcriptional regulator / N-acyltransferase is similar to: | PaperBLAST |
DVU1587: N-acetylglutamate synthase (EC 2.3.1.1) from Desulfovibrio vulgaris | 27% id, 73% 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 5 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory