Curated BLAST for Genomes

 

Curated BLAST

Searching in Methanobacterium arcticum M2 (GCF_000746075.1)

Found 44 curated entries in PaperBLAST's database that match '6.2.1.1' as complete word(s).

These curated entries have 32 distinct sequences.

Running ublast with E ≤ 0.01

Found 6 relevant proteins in Methanobacterium arcticum M2, or try another query

acs EI99_RS14430 WP_048082644.1: acetate--CoA ligase
is similar to:
PaperBLAST

Q2XNL6: acetate-CoA ligase (EC 6.2.1.1) from Methanothermobacter thermautotrophicus

76% id,
100% cov

Q2I0L7: acetate-CoA ligase (EC 6.2.1.1) from Methanothermobacter thermautotrophicus

76% id,
100% cov

ACSA_METTP / A0B8F1: Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Methanothrix thermoacetophila
A0B8F1: acetate-CoA ligase (EC 6.2.1.1) from Methanothrix thermoacetophila

53% id,
97% cov

More...

acs EI99_RS05765 WP_048080955.1: acetate--CoA ligase
is similar to:
PaperBLAST

ACSA_METTP / A0B8F1: Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Methanothrix thermoacetophila
A0B8F1: acetate-CoA ligase (EC 6.2.1.1) from Methanothrix thermoacetophila

58% id,
98% cov

Q2XNL6: acetate-CoA ligase (EC 6.2.1.1) from Methanothermobacter thermautotrophicus

54% id,
100% cov

Q2I0L7: acetate-CoA ligase (EC 6.2.1.1) from Methanothermobacter thermautotrophicus

54% id,
100% cov

More...

EI99_RS12525 WP_048082315.1: AMP-binding protein
is similar to:
PaperBLAST

HBCL1_METS5 / A4YDT1: 4-hydroxybutyrate--CoA ligase 1; Acetate--CoA ligase; Butyrate--CoA ligase; Propionate--CoA ligase; EC 6.2.1.40; EC 6.2.1.1; EC 6.2.1.2; EC 6.2.1.17 from Metallosphaera sedula

41% id,
91% cov

ACSA_BACSU / P39062: Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Bacillus subtilis

33% id,
94% cov

acs1 / Q2LWR8: acetate—CoA ligase (EC 6.2.1.1) from Syntrophus aciditrophicus

31% id,
86% cov

More...

EI99_RS01785 WP_048080214.1: AMP-binding protein
is similar to:
PaperBLAST

HBCL2_METS5 / A4YDR9: 4-hydroxybutyrate--CoA ligase 2; Acetate--CoA ligase; Butyrate--CoA ligase; Propionate--CoA ligase; acyl-activating enzyme; EC 6.2.1.40; EC 6.2.1.1; EC 6.2.1.2; EC 6.2.1.17 from Metallosphaera sedula

33% id,
94% cov

CCL4 / M4IQQ5: isobutanoate/2-methylbutanoate--CoA ligase (EC 6.2.1.1) from Humulus lupulus

29% id,
94% cov

ACSA_BACSU / P39062: Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Bacillus subtilis

27% id,
89% cov

More...

EI99_RS08045 WP_048081453.1: non-ribosomal peptide synthetase
is similar to:
PaperBLAST

HBCL1_METS5 / A4YDT1: 4-hydroxybutyrate--CoA ligase 1; Acetate--CoA ligase; Butyrate--CoA ligase; Propionate--CoA ligase; EC 6.2.1.40; EC 6.2.1.1; EC 6.2.1.2; EC 6.2.1.17 from Metallosphaera sedula

25% id,
92% cov

HBCL2_METS5 / A4YDR9: 4-hydroxybutyrate--CoA ligase 2; Acetate--CoA ligase; Butyrate--CoA ligase; Propionate--CoA ligase; acyl-activating enzyme; EC 6.2.1.40; EC 6.2.1.1; EC 6.2.1.2; EC 6.2.1.17 from Metallosphaera sedula

23% id,
92% cov

facA: acetyl-coenzyme A synthetase; EC 6.2.1.1 from Emericella nidulans

23% id,
89% cov

More...

EI99_RS11220 WP_245611172.1: AMP-binding protein
is similar to:
PaperBLAST

CCL2 / M4IRL4: isovalerate--CoA ligase (EC 6.2.1.1) from Humulus lupulus

25% id,
54% cov

Q2XNL6: acetate-CoA ligase (EC 6.2.1.1) from Methanothermobacter thermautotrophicus

23% id,
44% cov

ACSA_METTP / A0B8F1: Acetyl-coenzyme A synthetase; AcCoA synthetase; Acs; Acetate--CoA ligase; Acyl-activating enzyme; EC 6.2.1.1 from Methanothrix thermoacetophila
A0B8F1: acetate-CoA ligase (EC 6.2.1.1) from Methanothrix thermoacetophila

23% id,
41% cov

More...

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 6 reading frames. These were all redundant with annotated proteins.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory