Searching in Desulfovibrio vulgaris Hildenborough (882)
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 Desulfovibrio vulgaris Hildenborough, or try another query
| DVU2230: purine nucleoside phosphorylase is similar to: | PaperBLAST |
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 | 50% id, 99% cov |
A0A3G5E8S8: purine-nucleoside phosphorylase (EC 2.4.2.1) from Aneurinibacillus migulanus | 50% id, 94% cov |
Q72L69: purine-nucleoside phosphorylase (EC 2.4.2.1) from Thermus thermophilus | 47% id, 99% cov |
| DVU1677: triosephosphate isomerase is similar to: | PaperBLAST |
P00941: purine-nucleoside phosphorylase (EC 2.4.2.1) from Homo sapiens | 42% id, 94% cov |
| DVU0365: conserved hypothetical protein 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 | 34% id, 100% 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, 89% cov |
LACC1_HUMAN / Q8IV20: Purine nucleoside phosphorylase LACC1; Adenosine deaminase LACC1; Fatty acid metabolism-immunity nexus; Guanosine phosphorylase LACC1; Laccase domain-containing protein 1; S-methyl-5'-thioadenosine phosphorylase LACC1; EC 2.4.2.1; EC 3.5.4.4; EC 2.4.2.28 from Homo sapiens | 26% id, 55% 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