Curated BLAST for Genomes

 

Curated BLAST

Searching in Dechlorosoma suillum PS (PS)

Found 39 curated entries in PaperBLAST's database that match '1.1.1.3' as complete word(s).

These curated entries have 30 distinct sequences.

Running ublast with E ≤ 0.01

Found 3 relevant proteins in Dechlorosoma suillum PS, or try another query

Dsui_2907: homoserine dehydrogenase
is similar to:
PaperBLAST

DHOM_NEIG1 / Q5F8J4: Homoserine dehydrogenase; HDH; HSD; NAD(+)-dependent homoserine dehydrogenase; NAD(+)-dependent HSD; NgHSD; EC 1.1.1.3 from Neisseria gonorrhoeae

63% id,
100% cov

Ga0059261_2711: homoserine dehydrogenase (EC 1.1.1.3) from Sphingomonas koreensis

44% id,
97% cov

DvMF_1412: homoserine dehydrogenase (EC 1.1.1.3) from Desulfovibrio vulgaris

44% id,
94% cov

More...

Dsui_2134: aspartate kinase, monofunctional class
is similar to:
PaperBLAST

Q9WZ17: homoserine dehydrogenase (EC 1.1.1.3); aspartate kinase (EC 2.7.2.4) from Thermotoga maritima

42% id,
54% cov

BT2403: aspartate kinase / homoserine dehydrogenase (EC 2.7.2.4; EC 1.1.1.3) from Bacteroides thetaiotaomicron

30% id,
43% cov

ThrD / b0002: fused aspartate kinase/homoserine dehydrogenase 1 (EC 2.7.2.4; EC 1.1.1.3) from Escherichia coli
thrA / P00561: fused aspartate kinase/homoserine dehydrogenase 1 (EC 2.7.2.4; EC 1.1.1.3) from Escherichia coli
P00561: homoserine dehydrogenase (EC 1.1.1.3); aspartate kinase (EC 2.7.2.4) from Escherichia coli

31% id,
41% cov

More...

Dsui_2692: uridylate kinase
is similar to:
PaperBLAST

O63067: homoserine dehydrogenase (EC 1.1.1.3) from Glycine max

32% id,
11% cov

AKH2_ARATH / O81852: Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic; AK-HD 2; AK-HSDH 2; Beta-aspartyl phosphate homoserine 2; EC 2.7.2.4; EC 1.1.1.3 from Arabidopsis thaliana

37% id,
8% 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.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory