Searching in Kyrpidia tusciae DSM 2912 (GCF_000092905.1)
Found 52 curated entries in PaperBLAST's database that match '3.1.3.3' as complete word(s).
These curated entries have 39 distinct sequences.
Running ublast with E ≤ 0.01
Found 9 relevant proteins in Kyrpidia tusciae DSM 2912, or try another query
| BTUS_RS03615 Btus_0713 WP_013074767.1: histidine phosphatase family protein is similar to: | PaperBLAST |
SERCL_ARATH / F4KI56: Metal-independent phosphoserine phosphatase; iPSP; Phosphoglycerate mutase-like protein 3; EC 3.1.3.3 from Arabidopsis thaliana | 41% id, 83% cov |
ABIE51_RS06160: phosphoserine phosphatase (EC 3.1.3.3) from Lysobacter sp. | 35% id, 92% cov |
| BTUS_RS02550 Btus_0507 WP_013074568.1: HAD-IIA family hydrolase is similar to: | PaperBLAST |
PSP_BACSU / P94512: Phosphoserine phosphatase; PSP; EC 3.1.3.3 from Bacillus subtilis | 29% id, 71% cov |
PSP_THET2 / Q72H00: Phosphoserine phosphatase; PSP; EC 3.1.3.3 from Thermus thermophilus | 33% id, 47% cov |
| serA BTUS_RS09020 Btus_1805 WP_013075791.1: phosphoglycerate dehydrogenase is similar to: | PaperBLAST |
Echvi_2777: fused D-3-phosphoglycerate dehydrogenase / phosphoserine phosphatase (EC 1.1.1.95; EC 3.1.3.3) from Echinicola vietnamensis | 31% id, 57% cov |
| spoIIE BTUS_RS00490 Btus_0092 WP_013074164.1: stage II sporulation protein E is similar to: | PaperBLAST |
RSBU_BACSU / P40399: Phosphoserine phosphatase RsbU; Sigma factor SigB regulation protein RsbU; EC 3.1.3.3 from Bacillus subtilis | 23% id, 59% cov |
| BTUS_RS01940 Btus_0385 WP_013074448.1: D-glycerate dehydrogenase is similar to: | PaperBLAST |
Echvi_2777: fused D-3-phosphoglycerate dehydrogenase / phosphoserine phosphatase (EC 1.1.1.95; EC 3.1.3.3) from Echinicola vietnamensis | 31% id, 43% cov |
| BTUS_RS12980 Btus_2588 WP_013076528.1: D-2-hydroxyacid dehydrogenase is similar to: | PaperBLAST |
Echvi_2777: fused D-3-phosphoglycerate dehydrogenase / phosphoserine phosphatase (EC 1.1.1.95; EC 3.1.3.3) from Echinicola vietnamensis | 28% id, 45% cov |
| BTUS_RS04660 Btus_0927 WP_013074959.1: C-terminal binding protein is similar to: | PaperBLAST |
Echvi_2777: fused D-3-phosphoglycerate dehydrogenase / phosphoserine phosphatase (EC 1.1.1.95; EC 3.1.3.3) from Echinicola vietnamensis | 27% id, 44% cov |
| kdpB BTUS_RS02855 Btus_0566 WP_041304804.1: potassium-transporting ATPase subunit KdpB is similar to: | PaperBLAST |
SERB_YEAST / P42941: Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Saccharomyces cerevisiae | 26% id, 44% cov |
| BTUS_RS01555 Btus_0308 WP_013074374.1: Cof-type HAD-IIB family hydrolase is similar to: | PaperBLAST |
SERB_ALBFT / Q21YU0: Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Albidiferax ferrireducens | 36% id, 24% cov |
SERB_ECOLI / P0AGB0: Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Escherichia coli | 29% id, 28% cov |
SERB_STRCO / Q9S281: Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Streptomyces coelicolor | 34% id, 20% 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 9 reading frames. Except for 2 reading frames, these were redundant with annotated proteins. These remaining reading frames may be pseudogenes, omissions in the genome annotation, or N-terminal extensions of annotated proteins.
| 709523-710278 (frame -1) on NC_014098.1 Kyrpidia tusciae DSM 2912, complete sequence is similar to: | PaperBLAST |
SERCL_ARATH / F4KI56: Metal-independent phosphoserine phosphatase; iPSP; Phosphoglycerate mutase-like protein 3; EC 3.1.3.3 from Arabidopsis thaliana | 40% id, 88% cov |
| 2613125-2614531 (frame -1) on NC_014098.1 Kyrpidia tusciae DSM 2912, complete sequence is similar to: | PaperBLAST |
Echvi_2777: fused D-3-phosphoglycerate dehydrogenase / phosphoserine phosphatase (EC 1.1.1.95; EC 3.1.3.3) from Echinicola vietnamensis | 26% id, 50% cov |
Lawrence Berkeley National Laboratory