Searching in Sulfurimonas denitrificans DSM 1251 (GCF_000012965.1)
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 Sulfurimonas denitrificans DSM 1251, or try another query
SUDEN_RS10920 Suden_2102 WP_011373716.1: pyrimidine/purine nucleoside phosphorylase is similar to: | PaperBLAST |
PPNP_ECOLI / P0C037: Pyrimidine/purine nucleoside phosphorylase; Adenosine phosphorylase; Cytidine phosphorylase; Guanosine phosphorylase; Inosine phosphorylase; Thymidine phosphorylase; Uridine phosphorylase; Xanthosine phosphorylase; EC 2.4.2.1; EC 2.4.2.2 from Escherichia coli | 40% id, 98% cov |
pgeF SUDEN_RS02495 Suden_0476 WP_011372111.1: 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 | 33% id, 86% 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, 94% 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 | 25% id, 53% cov |
SUDEN_RS09120 Suden_1752 WP_011373367.1: triose-phosphate isomerase is similar to: | PaperBLAST |
P00941: purine-nucleoside phosphorylase (EC 2.4.2.1) from Homo sapiens | 34% id, 74% 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