Curated BLAST for Genomes

 

Curated BLAST

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

Found 63 curated entries in PaperBLAST's database that match '2.4.2.1' as complete word(s).

These curated entries have 44 distinct sequences.

Running ublast with E ≤ 0.01

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

Echvi_0304: purine nucleoside phosphorylase I, inosine and guanosine-specific
is similar to:
PaperBLAST

A0A3G5E8S8: purine-nucleoside phosphorylase (EC 2.4.2.1) from Aneurinibacillus migulanus

49% id,
99% cov

PUNA_GEOSE / P77834: Purine nucleoside phosphorylase 1; PNP 1; Inosine phosphorylase; Inosine-guanosine phosphorylase; Purine nucleoside phosphorylase I; PNP I; Pu-NPase I; EC 2.4.2.1 from Geobacillus stearothermophilus
P77834: purine-nucleoside phosphorylase (EC 2.4.2.1) from Geobacillus stearothermophilus

48% id,
98% cov

P55859: purine-nucleoside phosphorylase (EC 2.4.2.1) from Bos taurus

51% id,
88% cov

More...

Echvi_1196: triosephosphate isomerase
is similar to:
PaperBLAST

P00941: purine-nucleoside phosphorylase (EC 2.4.2.1) from Homo sapiens

42% id,
97% cov

Echvi_1798: Uridine phosphorylase
is similar to:
PaperBLAST

DEOD_SALTY / Q8ZJV7: Purine nucleoside phosphorylase DeoD-type; PNP; EC 2.4.2.1 from Salmonella typhimurium

25% id,
96% cov

DEOD_ECOLI / P0ABP8: Purine nucleoside phosphorylase DeoD-type; PNP; EC 2.4.2.1 from Escherichia coli
Pup / b4384: purine nucleoside phosphorylase (EC 2.4.2.15; EC 2.4.2.1) from Escherichia coli
deoD / RF|NP_418801: purine nucleoside phosphorylase deoD-type; EC 2.4.2.1 from Escherichia coli
deoD / P0ABP8: purine nucleoside phosphorylase (EC 2.4.2.15; EC 2.4.2.1) from Escherichia coli

25% id,
96% cov

deoD: purine nucleoside phosphorylase; EC 2.4.2.1 from Bacillus anthracis

26% id,
89% 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