Searching for up to 100 curated homologs for H281DRAFT_06482 FitnessBrowser__Burk376:H281DRAFT_06482 (446 a.a.)
Found high-coverage hits (≥70%) to 8 curated proteins.
You can add additional sequences or change the %identity threshold for inclusion. Once you have selected sequences, you can build an alignment and a tree.
Sama_1321 Succinylarginine dihydrolase (EC 3.5.3.23) from Shewanella amazonensis SB2B
61% identity, 100% coverage of query (559 bits)
SO2706 Succinylarginine dihydrolase (EC 3.5.3.23) from Shewanella oneidensis MR-1
61% identity, 100% coverage of query (557 bits)
Shewana3_1728 Succinylarginine dihydrolase (EC 3.5.3.23) from Shewanella sp. ANA-3
60% identity, 100% coverage of query (552 bits)
YdjT / b1745 N-succinylarginine dihydrolase (EC 3.5.3.23) from Escherichia coli K-12 substr. MG1655 (see 3 papers)
astB / P76216 N-succinylarginine dihydrolase (EC 3.5.3.23) from Escherichia coli (strain K12) (see 4 papers)
ASTB_ECOLI / P76216 N-succinylarginine dihydrolase; EC 3.5.3.23 from Escherichia coli (strain K12) (see 3 papers)
astB / RF|NP_416259.1 N-succinylarginine dihydrolase; EC 3.5.3.23 from Escherichia coli K12 (see 6 papers)
59% identity, 100% coverage of query (522 bits)
1ynhB / P76216 Crystal structure of n-succinylarginine dihydrolase, astb, bound to substrate and product, an enzyme from the arginine catabolic pathway of escherichia coli (see paper)
59% identity, 100% coverage of query (520 bits)
1yniA Crystal structure of n-succinylarginine dihydrolase, astb, bound to substrate and product, an enzyme from the arginine catabolic pathway of escherichia coli
58% identity, 100% coverage of query (516 bits)
ASTB_SALTY / Q8ZPU9 N-succinylarginine dihydrolase; EC 3.5.3.23 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
57% identity, 100% coverage of query (503 bits)
BWI76_RS11685 Succinylarginine dihydrolase (EC 3.5.3.23) from Klebsiella michiganensis M5al
58% identity, 100% coverage of query (489 bits)
Build an alignment for H281DRAFT_06482 and 8 homologs with ≥ 30% identity
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Lawrence Berkeley National Laboratory