SitesBLAST
Comparing WP_011737180.1 NCBI__GCF_000015045.1:WP_011737180.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 19 hits to proteins with known functional sites (download)
P27305 Glutamyl-Q tRNA(Asp) synthetase; Glu-Q-RSs; EC 6.1.1.- from Escherichia coli (strain K12) (see paper)
40% identity, 96% coverage: 5:302/309 of query aligns to 14:297/308 of P27305
- E55 (≠ D46) binding L-glutamate
- Y182 (= Y183) binding L-glutamate
- R200 (= R201) binding L-glutamate
4a91A Crystal structure of the glutamyl-queuosine trnaasp synthetase from e. Coli complexed with l-glutamate (see paper)
40% identity, 96% coverage: 5:302/309 of query aligns to 2:283/290 of 4a91A
- active site: S11 (= S14), K229 (= K242)
- binding glutamic acid: R7 (= R10), A9 (= A12), S11 (= S14), E43 (≠ D46), Y170 (= Y183), R188 (= R201), L192 (= L205)
- binding zinc ion: C99 (= C102), C101 (= C104), Y113 (= Y125), C117 (= C129)
Q8DLI5 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1) (see paper)
33% identity, 96% coverage: 10:305/309 of query aligns to 6:311/485 of Q8DLI5
- R6 (= R10) binding L-glutamate
- Y192 (= Y183) binding L-glutamate
2cfoA Non-discriminating glutamyl-tRNA synthetase from thermosynechococcus elongatus in complex with glu (see paper)
33% identity, 96% coverage: 10:305/309 of query aligns to 5:310/484 of 2cfoA
P04805 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Escherichia coli (strain K12) (see 4 papers)
32% identity, 84% coverage: 10:269/309 of query aligns to 6:264/471 of P04805
- C98 (= C102) mutation to S: 10-fold decrease in activity. Strong decrease in zinc content.
- C100 (= C104) mutation to S: Loss of activity. Strong decrease in zinc content.; mutation to Y: Does not prevent zinc binding. Reduces only 2-fold the binding affinity for tRNA(Glu), but reduces more than 10-fold the affinity for glutamate in the presence of tRNA(Glu).
- C125 (= C129) mutation to S: Loss of activity. Strong decrease in zinc content.
- H127 (≠ N131) mutation to Q: 10-fold decrease in activity. Strong decrease in zinc content.
- H129 (≠ M133) mutation to Q: No change in activity or in zinc content.
- H131 (≠ E135) mutation to Q: No change in activity or in zinc content.
- H132 (≠ G136) mutation to Q: No change in activity or in zinc content.
- C138 (≠ W142) mutation to S: No change in activity or in zinc content.
- S239 (= S241) modified: Phosphoserine; mutation to D: Does not aminoacylate tRNA(Glu), not phosphorylated by HipA.
8i9iA Glutamyl-tRNA synthetase from escherichia coli bound to glutamate and zinc
32% identity, 84% coverage: 10:269/309 of query aligns to 6:264/468 of 8i9iA
1g59A Glutamyl-tRNA synthetase complexed with tRNA(glu). (see paper)
31% identity, 94% coverage: 7:298/309 of query aligns to 2:310/468 of 1g59A
- binding : D44 (= D49), R45 (≠ S50), A46 (≠ Q51), R47 (= R52), P109 (≠ R106), V145 (≠ C152), R163 (= R158), V166 (≠ I161), E172 (≠ G168), V177 (≠ P173), K180 (≠ R176), S181 (≠ A177), D182 (= D178), E207 (≠ D203), E208 (≠ D204), R237 (≠ T233), K241 (≠ G237), T242 (= T238), K243 (= K239), M273 (≠ L269), G274 (= G270), E282 (vs. gap), S299 (≠ A287), L300 (≠ W288), P303 (≠ A291), V304 (≠ H292), K309 (= K297)
Sites not aligning to the query:
- binding : 312, 319, 357, 358, 417, 426, 427, 432, 435, 442, 443, 444, 445, 446, 447, 448
3al0C Crystal structure of the glutamine transamidosome from thermotoga maritima in the glutamylation state. (see paper)
30% identity, 84% coverage: 10:270/309 of query aligns to 106:360/564 of 3al0C
- active site: S110 (= S14), K335 (= K242)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R106 (= R10), A108 (= A12), P109 (= P13), G118 (= G22), T122 (≠ S26), E142 (≠ D46), Y276 (= Y183), R294 (= R201), G295 (= G202), D297 (= D204), H298 (≠ L205), L324 (= L231), I325 (≠ V232), L333 (= L240)
- binding : T144 (≠ L48), D145 (= D49), R148 (= R52), Y208 (≠ C104), P213 (≠ I109), K252 (≠ R158), M255 (≠ I161), I266 (≠ P173), K269 (≠ R176), S270 (≠ A177), Y276 (= Y183), D297 (= D204), H298 (≠ L205), L299 (= L206), S300 (≠ A207), N301 (≠ S208), K304 (≠ R211), R330 (≠ G237), P332 (≠ K239)
Sites not aligning to the query:
- binding : 363, 364, 365, 370, 387, 389, 391, 392, 397, 400, 407, 446, 447, 453, 457, 509, 520, 524, 527, 535, 536, 538, 539
2cv2A Glutamyl-tRNA synthetase from thermus thermophilus in complex with tRNA(glu) and an enzyme inhibitor, glu-ams (see paper)
31% identity, 94% coverage: 7:298/309 of query aligns to 2:310/468 of 2cv2A
- active site: K246 (= K242)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R5 (= R10), A7 (= A12), S9 (= S14), G17 (= G22), I21 (≠ S26), E41 (≠ D46), Y187 (= Y183), R205 (= R201), A206 (≠ G202), E208 (≠ D204), W209 (≠ L205), L235 (= L231), L236 (≠ V232)
- binding : S9 (= S14), T43 (≠ L48), D44 (= D49), R47 (= R52), V145 (vs. gap), R163 (= R158), Y168 (≠ Q163), E172 (≠ G168), V177 (≠ P173), K180 (≠ R176), S181 (≠ A177), Y187 (= Y183), E207 (≠ D203), E208 (≠ D204), W209 (≠ L205), V211 (≠ A207), R237 (≠ T233), K241 (≠ G237), L272 (≠ F268), M273 (≠ L269), G274 (= G270), E282 (vs. gap), S299 (≠ A287), P303 (≠ A291), V304 (≠ H292), K309 (= K297)
Sites not aligning to the query:
- binding : 312, 319, 357, 358, 417, 432, 435, 442, 443, 444, 446, 447, 448
2cv1A Glutamyl-tRNA synthetase from thermus thermophilus in complex with tRNA(glu), atp, and an analog of l-glutamate: a quaternary complex
31% identity, 94% coverage: 7:298/309 of query aligns to 2:310/468 of 2cv1A
- active site: K246 (= K242)
- binding adenosine-5'-triphosphate: P8 (= P13), S9 (= S14), G17 (= G22), T18 (≠ S23), I21 (≠ S26), R47 (= R52), A206 (≠ G202), W209 (≠ L205), L235 (= L231), L236 (≠ V232)
- binding (4s)-4-amino-5-hydroxypentanoic acid: R5 (= R10), A7 (= A12), E41 (≠ D46), Y187 (= Y183), R205 (= R201), W209 (≠ L205)
- binding : S9 (= S14), E41 (≠ D46), T43 (≠ L48), D44 (= D49), R47 (= R52), V145 (vs. gap), R163 (= R158), V166 (≠ I161), E172 (≠ G168), V177 (≠ P173), K180 (≠ R176), S181 (≠ A177), Y187 (= Y183), E207 (≠ D203), E208 (≠ D204), W209 (≠ L205), V211 (≠ A207), R237 (≠ T233), K241 (≠ G237), K243 (= K239), M273 (≠ L269), G274 (= G270), S276 (≠ E272), E282 (vs. gap), S299 (≠ A287), P303 (≠ A291), V304 (≠ H292), K309 (= K297)
Sites not aligning to the query:
- binding : 312, 319, 357, 358, 417, 427, 432, 435, 442, 443, 444, 446, 447, 448
2cuzA Glutamyl-tRNA synthetase from thermus thermophilus in complex with l- glutamate (see paper)
31% identity, 94% coverage: 7:298/309 of query aligns to 2:310/468 of 2cuzA
1n78A Crystal structure of thermus thermophilus glutamyl-tRNA synthetase complexed with tRNA(glu) and glutamol-amp. (see paper)
31% identity, 94% coverage: 7:298/309 of query aligns to 2:310/468 of 1n78A
- active site: K246 (= K242)
- binding glutamol-amp: R5 (= R10), A7 (= A12), P8 (= P13), S9 (= S14), G17 (= G22), T18 (≠ S23), I21 (≠ S26), E41 (≠ D46), Y187 (= Y183), N191 (≠ V187), R205 (= R201), A206 (≠ G202), E208 (≠ D204), W209 (≠ L205), L235 (= L231), L236 (≠ V232)
- binding : S9 (= S14), T43 (≠ L48), D44 (= D49), R47 (= R52), V145 (vs. gap), R163 (= R158), V166 (≠ I161), Y168 (≠ Q163), E172 (≠ G168), V177 (≠ P173), K180 (≠ R176), S181 (≠ A177), Y187 (= Y183), E207 (≠ D203), E208 (≠ D204), W209 (≠ L205), L210 (= L206), V211 (≠ A207), R237 (≠ T233), K241 (≠ G237), M273 (≠ L269), G274 (= G270), E282 (vs. gap), R297 (≠ I285), P303 (≠ A291), V304 (≠ H292), K309 (= K297)
Sites not aligning to the query:
- binding : 312, 319, 357, 358, 417, 427, 432, 435, 442, 443, 444, 446, 447, 448
1j09A Crystal structure of thermus thermophilus glutamyl-tRNA synthetase complexed with atp and glu (see paper)
31% identity, 94% coverage: 7:298/309 of query aligns to 2:310/468 of 1j09A
- active site: K246 (= K242)
- binding adenosine-5'-triphosphate: H15 (= H20), E208 (≠ D204), L235 (= L231), L236 (≠ V232), K243 (= K239), I244 (≠ L240), S245 (= S241), K246 (= K242), R247 (= R243)
- binding glutamic acid: R5 (= R10), A7 (= A12), S9 (= S14), E41 (≠ D46), Y187 (= Y183), N191 (≠ V187), R205 (= R201), W209 (≠ L205)
P27000 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
31% identity, 94% coverage: 7:298/309 of query aligns to 2:310/468 of P27000
Sites not aligning to the query:
- 358 R→Q: Reduces affinity for tRNA and abolishes the ability to discriminate between tRNA(Glu) and tRNA(Gln).
4g6zA Crystal structure of a glutamyl-tRNA synthetase glurs from burkholderia thailandensis bound to l-glutamate (see paper)
31% identity, 86% coverage: 6:271/309 of query aligns to 2:251/380 of 4g6zA
8vc5A Crystal structure of glutamyl-tRNA synthetase glurs from pseudomonas aeruginosa (zinc bound)
29% identity, 96% coverage: 5:302/309 of query aligns to 2:305/488 of 8vc5A
6brlA Crystal structure of a glutamate tRNA ligase from elizabethkingia meningosepticum ccug26117 in complex with its amino acid (see paper)
27% identity, 96% coverage: 10:306/309 of query aligns to 6:338/502 of 6brlA
4griB Crystal structure of a glutamyl-tRNA synthetase glurs from borrelia burgdorferi bound to glutamic acid and zinc (see paper)
29% identity, 76% coverage: 10:243/309 of query aligns to 5:254/485 of 4griB
- active site: S9 (= S14), K253 (= K242)
- binding glutamic acid: R5 (= R10), A7 (= A12), S9 (= S14), E41 (≠ D46), Y194 (= Y183), R212 (= R201), W216 (≠ L205)
- binding zinc ion: C105 (= C102), C107 (= C104), Y128 (= Y125), C132 (= C129)
3aiiA Archaeal non-discriminating glutamyl-tRNA synthetase from methanothermobacter thermautotrophicus (see paper)
26% identity, 81% coverage: 7:256/309 of query aligns to 11:251/455 of 3aiiA
Query Sequence
>WP_011737180.1 NCBI__GCF_000015045.1:WP_011737180.1
MFRTTPLIGRFAPSPTGALHTGSLVSAVGSWLMAKSAGGQWLVRIDDLDSQRQVPGMADD
ILATLERFALFWDGEISRQSLNLELYEQAFQELKRKALLYPCCCSRREISQAASAPHPTD
DCLPYPGSCRNGMPEGRTVRSWRVRVTDEPVCFHDLRRGMICQNLLTGCGDFPLRRADGE
FAYQLAVVLDDRISGVNQVVRGDDLLASTPRQIHLQRLLALPQPEYCHLPLVTGPGGTKL
SKRDNLVSHHLGNWKDREGVLLHRVLRFLGQEPPAELSGASCPQILAWGAAHFDLRKLPR
KGGELTLVS
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory