Comparing Synpcc7942_2197 FitnessBrowser__SynE:Synpcc7942_2197 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 17 hits to proteins with known functional sites (download)
2j5tD Glutamate 5-kinase from escherichia coli complexed with glutamate (see paper)
43% identity, 99% coverage: 2:365/367 of query aligns to 2:363/365 of 2j5tD
P0A7B5 Glutamate 5-kinase; Gamma-glutamyl kinase; GK; EC 2.7.2.11 from Escherichia coli (strain K12) (see paper)
43% identity, 99% coverage: 2:365/367 of query aligns to 4:365/367 of P0A7B5
2j5vB Glutamate 5-kinase from escherichia coli complexed with glutamyl-5- phosphate and pyroglutamic acid (see paper)
39% identity, 99% coverage: 2:365/367 of query aligns to 2:323/325 of 2j5vB
2j5vA Glutamate 5-kinase from escherichia coli complexed with glutamyl-5- phosphate and pyroglutamic acid (see paper)
38% identity, 99% coverage: 2:365/367 of query aligns to 2:321/323 of 2j5vA
7wx3B Gk domain of drosophila p5cs filament with glutamate, atp, and NADPH (see paper)
35% identity, 68% coverage: 5:254/367 of query aligns to 15:256/258 of 7wx3B
2akoA Crystal structure of glutamate 5-kinase from campylobacter jejuni
33% identity, 63% coverage: 5:235/367 of query aligns to 3:219/241 of 2akoA
7f5xA Gk domain of drosophila p5cs filament with glutamate (see paper)
35% identity, 68% coverage: 5:254/367 of query aligns to 15:234/236 of 7f5xA
Q8U122 Uridylate kinase; UK; Uridine monophosphate kinase; UMP kinase; UMPK; EC 2.7.4.22 from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) (see paper)
30% identity, 30% coverage: 148:256/367 of query aligns to 120:225/225 of Q8U122
Sites not aligning to the query:
2bmuB Ump kinase from pyrococcus furiosus complexed with its substrate ump and its substrate analog amppnp (see paper)
30% identity, 30% coverage: 148:256/367 of query aligns to 121:226/226 of 2bmuB
Sites not aligning to the query:
2ji5A Structure of ump kinase from pyrococcus furiosus complexed with utp
30% identity, 30% coverage: 148:256/367 of query aligns to 122:219/219 of 2ji5A
Sites not aligning to the query:
7lnuB Ternary complex of the isopentenyl phosphate kinase from candidatus methanomethylophilus alvus bound to isopentenyl monophosphate and atp (see paper)
24% identity, 68% coverage: 2:250/367 of query aligns to 2:252/261 of 7lnuB
7lntB Ternary complex of the isopentenyl phosphate kinase from candidatus methanomethylophilus alvus bound to benzyl monophosphate and atp (see paper)
24% identity, 68% coverage: 2:250/367 of query aligns to 1:251/260 of 7lntB
7n9dA I74a mutant of the isopentenyl phosphate kinase from candidatus methanomethylophilus alvus (see paper)
24% identity, 37% coverage: 114:250/367 of query aligns to 115:248/253 of 7n9dA
Sites not aligning to the query:
7lnxB I146a mutant of the isopentenyl phosphate kinase from candidatus methanomethylophilus alvus (see paper)
23% identity, 68% coverage: 2:250/367 of query aligns to 4:238/247 of 7lnxB
7lnuA Ternary complex of the isopentenyl phosphate kinase from candidatus methanomethylophilus alvus bound to isopentenyl monophosphate and atp (see paper)
22% identity, 68% coverage: 2:250/367 of query aligns to 1:230/239 of 7lnuA
7lntA Ternary complex of the isopentenyl phosphate kinase from candidatus methanomethylophilus alvus bound to benzyl monophosphate and atp (see paper)
22% identity, 68% coverage: 2:250/367 of query aligns to 1:230/238 of 7lntA
7lnwA I146a mutant of the isopentenyl phosphate kinase from candidatus methanomethylophilus alvus (see paper)
23% identity, 67% coverage: 5:250/367 of query aligns to 3:247/256 of 7lnwA
>Synpcc7942_2197 FitnessBrowser__SynE:Synpcc7942_2197
MSETLVVKIGTSSLTNPHHPGLALSTIAGLVEVICQLRRQGYNVVLVSSGAVGVGCTRLG
LRDRPSRIAQRQAIAAVGQGRLMRTYDDLFTTLGQPIAQVLLTRGDLAQRQRYINAYQTF
QELFELGVVPIVNENDTVAVEELKFGDNDTLSALVASLVEAQWLFLLTDVDRLYTADPRQ
DPNAKPITIVHDLSELESIQAGGQGSRWGTGGMATKLTAAKIATQASVRTVITQGRSPEN
LLKILAGEAIGTWFEPQPETVNARKRWIAHGLVPTGKLLLDAGAVQAIQAGGKSLLAAGI
QAIEGDFEAQDAVQLCDLNGTEIARGLVNYDSHELQQIRGCQSDQIVQILGYEGAETIVH
RDNLVLS
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SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.
Lawrence Berkeley National Laboratory