Searching in Shewanella sp. ANA-3 (ANA3)
Found 51 curated entries in PaperBLAST's database that match '3.1.3.3' as complete word(s).
These curated entries have 38 distinct sequences.
Running ublast with E ≤ 0.01
Found 10 relevant proteins in Shewanella sp. ANA-3, or try another query
Shewana3_1046: phosphoserine phosphatase (RefSeq) is similar to: | PaperBLAST |
SERB_IDILO / Q5QXU4: Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Idiomarina loihiensis | 47% id, 94% cov |
SERB_STRT2 / Q5M3B3: Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Streptococcus thermophilus | 42% id, 98% cov |
SERB_ECOLI / P0AGB0: Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Escherichia coli | 54% id, 75% cov |
Shewana3_3416: D-3-phosphoglycerate dehydrogenase (RefSeq) 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 | 51% id, 64% cov |
CA265_RS22635: phosphoserine phosphatase (EC 3.1.3.3) from Pedobacter sp. | 37% id, 24% cov |
Shewana3_3446: alkaline phosphatase (RefSeq) is similar to: | PaperBLAST |
PsiA / b0383: alkaline phosphatase (EC 3.1.3.1; EC 3.1.3.75; EC 3.1.3.41; EC 3.1.3.74; EC 3.1.3.99; EC 3.1.3.5; EC 3.1.3.6; EC 3.1.3.89; EC 3.1.3.91; EC 3.1.3.60; EC 3.1.3.15; EC 3.1.3.102; EC 3.1.3.108; EC 3.1.3.11; EC 3.1.3.20; EC 3.1.3.19; EC 3.1.3.3; EC 3.6.1.25; EC 3.6.1.1; EC 3.1.3.23; EC 3.1.3.38; EC 3.1.3.18; EC 3.1.3.68; EC 3.9.1.1) from Escherichia coli | 34% id, 72% cov |
Shewana3_3797: nucleotidase (RefSeq) is similar to: | PaperBLAST |
PSP_THET2 / Q72H00: Phosphoserine phosphatase; PSP; EC 3.1.3.3 from Thermus thermophilus | 39% id, 45% cov |
Shewana3_0394: HAD family hydrolase (RefSeq) is similar to: | PaperBLAST |
PSP_THET2 / Q72H00: Phosphoserine phosphatase; PSP; EC 3.1.3.3 from Thermus thermophilus | 34% id, 49% cov |
Shewana3_3540: peptidoglycan glycosyltransferase (RefSeq) is similar to: | PaperBLAST |
PsiA / b0383: alkaline phosphatase (EC 3.1.3.1; EC 3.1.3.75; EC 3.1.3.41; EC 3.1.3.74; EC 3.1.3.99; EC 3.1.3.5; EC 3.1.3.6; EC 3.1.3.89; EC 3.1.3.91; EC 3.1.3.60; EC 3.1.3.15; EC 3.1.3.102; EC 3.1.3.108; EC 3.1.3.11; EC 3.1.3.20; EC 3.1.3.19; EC 3.1.3.3; EC 3.6.1.25; EC 3.6.1.1; EC 3.1.3.23; EC 3.1.3.38; EC 3.1.3.18; EC 3.1.3.68; EC 3.9.1.1) from Escherichia coli | 31% id, 50% cov |
PsiA / b0383: alkaline phosphatase (EC 3.1.3.1; EC 3.1.3.75; EC 3.1.3.41; EC 3.1.3.74; EC 3.1.3.99; EC 3.1.3.5; EC 3.1.3.6; EC 3.1.3.89; EC 3.1.3.91; EC 3.1.3.60; EC 3.1.3.15; EC 3.1.3.102; EC 3.1.3.108; EC 3.1.3.11; EC 3.1.3.20; EC 3.1.3.19; EC 3.1.3.3; EC 3.6.1.25; EC 3.6.1.1; EC 3.1.3.23; EC 3.1.3.38; EC 3.1.3.18; EC 3.1.3.68; EC 3.9.1.1) from Escherichia coli | 34% id, 31% cov |
Shewana3_2013: response regulator receiver modulated serine phosphatase (RefSeq) is similar to: | PaperBLAST |
O07014: phosphoserine phosphatase (EC 3.1.3.3) from Bacillus subtilis | 25% id, 55% cov |
Shewana3_3201: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding (RefSeq) 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 | 30% id, 45% cov |
Shewana3_3319: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding (RefSeq) 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 | 29% id, 44% cov |
Shewana3_0583: D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding (RefSeq) 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 | 25% id, 35% 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 10 reading frames. These were all redundant with annotated proteins.
Lawrence Berkeley National Laboratory