Curated BLAST for Genomes

 

Curated BLAST

Searching in Echinicola vietnamensis KMM 6221, DSM 17526 (Cola)

Found 42 curated entries in PaperBLAST's database that match '1.4.1.2' as complete word(s).

These curated entries have 33 distinct sequences.

Running ublast with E ≤ 0.01

Found 3 relevant proteins in Echinicola vietnamensis KMM 6221, DSM 17526, or try another query

Echvi_1535: Glutamate dehydrogenase/leucine dehydrogenase
is similar to:
PaperBLAST

P96110: trimer complex (EC 1.4.1.2) from Thermotoga maritima

52% id,
98% cov

Q43314: glutamate dehydrogenase (EC 1.4.1.2); glutamate dehydrogenase [NAD(P)+] (EC 1.4.1.3) from Arabidopsis thaliana

47% id,
99% cov

GDH2 / Q38946: glutamate dehydrogenase β subunit (EC 1.4.1.2) from Arabidopsis thaliana

46% id,
99% cov

More...

Echvi_1756: Glutamate dehydrogenase/leucine dehydrogenase
is similar to:
PaperBLAST

DHE2_PYRCJ / A3MUY9: NAD(+)-dependent glutamate dehydrogenase; NAD-GDH; NAD-specific glutamate dehydrogenase; EC 1.4.1.2 from Pyrobaculum calidifontis
A3MUY9: glutamate dehydrogenase (EC 1.4.1.2) from Pyrobaculum calidifontis

28% id,
84% cov

Q9Y8I4: glutamate dehydrogenase (EC 1.4.1.2) from Pyrobaculum islandicum

28% id,
85% cov

Q0E5H9: glutamate dehydrogenase (EC 1.4.1.2) from Halobacillus halophilus

29% id,
35% cov

Echvi_0862: Glutamate dehydrogenase/leucine dehydrogenase
is similar to:
PaperBLAST

Q9TVN3: glutamate dehydrogenase (EC 1.4.1.2) from Entodinium caudatum

23% id,
84% cov

DHE2_PYRCJ / A3MUY9: NAD(+)-dependent glutamate dehydrogenase; NAD-GDH; NAD-specific glutamate dehydrogenase; EC 1.4.1.2 from Pyrobaculum calidifontis
A3MUY9: glutamate dehydrogenase (EC 1.4.1.2) from Pyrobaculum calidifontis

27% id,
67% cov

Q852M0: glutamate dehydrogenase (EC 1.4.1.2) from Oryza sativa

26% id,
67% cov

More...

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.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory