Searching in Trichormus variabilis ATCC 29413 (GCF_000204075.1)
Found 64 curated entries in PaperBLAST's database that match '2.4.2.1' as complete word(s).
These curated entries have 45 distinct sequences.
Running ublast with E ≤ 0.01
Found 3 relevant proteins in Trichormus variabilis ATCC 29413, or try another query
AVA_RS08380 Ava_1653 WP_011318466.1: S-methyl-5'-thioadenosine phosphorylase is similar to: | PaperBLAST |
flB / Q1EMV9: 5'-fluoro-5'-deoxy-adenosine phosphorylase (EC 2.4.2.1) from Streptantibioticus cattleyicolor | 51% id, 94% cov |
Q97W94: purine-nucleoside phosphorylase (EC 2.4.2.1); S-methyl-5'-thioadenosine phosphorylase (EC 2.4.2.28) from Saccharolobus solfataricus | 44% id, 97% cov |
pnp / Q5JEQ6: adenosine phosphorylase (EC 2.4.2.1) from Thermococcus kodakarensis | 42% id, 98% cov |
tpiA AVA_RS16660 Ava_3290 WP_011320017.1: triose-phosphate isomerase is similar to: | PaperBLAST |
P00941: purine-nucleoside phosphorylase (EC 2.4.2.1) from Homo sapiens | 37% id, 95% cov |
pgeF AVA_RS07175 Ava_1419 WP_011318243.1: peptidoglycan editing factor PgeF is similar to: | PaperBLAST |
PURNU_ECOLI / P33644: Purine nucleoside phosphorylase YfiH; Adenosine deaminase YfiH; Polyphenol oxidase YfiH; S-methyl-5'-thioadenosine phosphorylase YfiH; EC 2.4.2.1; EC 3.5.4.4; EC 1.10.3.-; EC 2.4.2.28 from Escherichia coli | 32% id, 68% cov |
PURNU_BACTN / Q89ZI8: Purine nucleoside phosphorylase BT_4389; Adenosine deaminase BT_4389; S-methyl-5'-thioadenosine phosphorylase BT_4389; EC 2.4.2.1; EC 3.5.4.4; EC 2.4.2.28 from Bacteroides thetaiotaomicron | 29% id, 71% cov |
PURNU_GEOS3 / P84138: Purine nucleoside phosphorylase YlmD; Adenosine deaminase YlmD; S-methyl-5'-thioadenosine phosphorylase YlmD; EC 2.4.2.1; EC 3.5.4.4; EC 2.4.2.28 from Geobacillus stearothermophilus | 30% id, 66% 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