Curated BLAST
Searching in Methylococcus capsulatus str. Bath (GCF_000008325.1)
Found 18 curated entries in PaperBLAST's database that match '3.5.3.12' as complete word(s).
These curated entries have 14 distinct sequences.
Running ublast with E ≤ 0.01
Found 1 relevant proteins in Methylococcus capsulatus str. Bath, or try another query
MCA_RS09145 MCA1861 WP_338036785.1: agmatine deiminase family protein is similar to: | PaperBLAST |
Q9ZN18: agmatine deiminase (EC 3.5.3.12) from Helicobacter pylori | 41% id, 99% cov |
aguA / O24890: agmatine deiminase (EC 3.5.3.12) from Helicobacter pylori | 41% id, 99% cov |
C8J_0892 / A0A5Y8XU16: agmatine deaminase (EC 3.5.3.12) from Campylobacter jejuni | 37% id, 97% cov |
Q0P9V0: agmatine deiminase (EC 3.5.3.12) from Campylobacter jejuni | 37% id, 97% cov |
A0A0H2Z8C6: agmatine deiminase (EC 3.5.3.12) from Pseudomonas aeruginosa | 34% id, 96% cov |
AO356_10030: Agmatine deiminase (EC 3.5.3.12) from Pseudomonas fluorescens | 33% id, 94% cov |
Q5KR05: agmatine deiminase (EC 3.5.3.12) from Selenomonas ruminantium | 31% id, 95% cov |
AGUA_PSEAE / Q9I6J9: Agmatine deiminase; Agmatine iminohydrolase; EC 3.5.3.12 from Pseudomonas aeruginosa aguA / Q9I6J9: agmatine deiminase subunit (EC 3.5.3.12) from Pseudomonas aeruginosa Q9I6J9: agmatine deiminase (EC 3.5.3.12) from Pseudomonas aeruginosa | 31% id, 95% cov |
S0F349: agmatine deiminase (EC 3.5.3.12) from Lactococcus cremoris | 29% id, 96% cov |
AGUA_ENTFA / Q837U5: Putative agmatine deiminase; Agmatine iminohydrolase; EC 3.5.3.12 from Enterococcus faecalis Q837U5: agmatine deiminase (EC 3.5.3.12) from Enterococcus faecalis | 29% id, 96% cov |
A0A0H2Z743: agmatine deiminase (EC 3.5.3.12) from Pseudomonas aeruginosa | 32% id, 87% cov |
A0A0H3G8U9: agmatine deiminase (EC 3.5.3.12) from Listeria monocytogenes | 28% id, 97% 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 1 reading frames. These were all redundant with annotated proteins.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory