SitesBLAST
Comparing BPHYT_RS06160 FitnessBrowser__BFirm:BPHYT_RS06160 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 20 (the maximum) 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)
45% identity, 96% coverage: 3:287/296 of query aligns to 16:288/308 of P27305
- E55 (= E42) binding
- Y182 (= Y181) binding
- R200 (= R199) binding
4a91A Crystal structure of the glutamyl-queuosine trnaasp synthetase from e. Coli complexed with l-glutamate (see paper)
45% identity, 96% coverage: 3:287/296 of query aligns to 4:274/290 of 4a91A
- active site: S11 (= S10), K229 (= K240)
- binding glutamic acid: R7 (= R6), A9 (= A8), S11 (= S10), E43 (= E42), Y170 (= Y181), R188 (= R199), L192 (= L203)
- binding zinc ion: C99 (= C98), C101 (= C100), Y113 (= Y121), C117 (= C125)
8i9iA Glutamyl-tRNA synthetase from escherichia coli bound to glutamate and zinc
35% identity, 83% coverage: 1:247/296 of query aligns to 1:247/468 of 8i9iA
P04805 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Escherichia coli (strain K12) (see 4 papers)
34% identity, 83% coverage: 1:247/296 of query aligns to 1:247/471 of P04805
- C98 (= C98) mutation to S: 10-fold decrease in activity. Strong decrease in zinc content.
- C100 (= C100) 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 (= C125) mutation to S: Loss of activity. Strong decrease in zinc content.
- H127 (≠ D127) mutation to Q: 10-fold decrease in activity. Strong decrease in zinc content.
- H129 (≠ L129) mutation to Q: No change in activity or in zinc content.
- H131 (= H130) mutation to Q: No change in activity or in zinc content.
- H132 (≠ G131) mutation to Q: No change in activity or in zinc content.
- C138 (≠ W137) mutation to S: No change in activity or in zinc content.
- S239 (= S239) modified: Phosphoserine; mutation to D: Does not aminoacylate tRNA(Glu), not phosphorylated by HipA.
4g6zA Crystal structure of a glutamyl-tRNA synthetase glurs from burkholderia thailandensis bound to l-glutamate (see paper)
37% identity, 82% coverage: 4:247/296 of query aligns to 4:232/380 of 4g6zA
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)
34% identity, 88% coverage: 1:259/296 of query aligns to 1:270/485 of Q8DLI5
- R6 (= R6) binding
- Y192 (= Y181) binding
2cfoA Non-discriminating glutamyl-tRNA synthetase from thermosynechococcus elongatus in complex with glu (see paper)
34% identity, 87% coverage: 2:259/296 of query aligns to 1:269/484 of 2cfoA
1g59A Glutamyl-tRNA synthetase complexed with tRNA(glu). (see paper)
32% identity, 94% coverage: 6:284/296 of query aligns to 5:294/468 of 1g59A
- binding : D44 (= D45), R45 (≠ G46), A46 (≠ P47), R47 (= R48), P109 (≠ R102), V145 (≠ A136), R163 (≠ Q156), V166 (≠ Q159), E172 (= E166), V177 (= V171), K180 (≠ R174), S181 (≠ A175), D182 (= D176), E207 (≠ A201), E208 (≠ D202), R237 (≠ T231), K241 (≠ G235), T242 (≠ E236), K243 (= K237), M273 (≠ L263), G274 (= G264), E282 (≠ A272)
Sites not aligning to the query:
- binding : 299, 300, 303, 304, 309, 312, 319, 357, 358, 417, 426, 427, 432, 435, 442, 443, 444, 445, 446, 447, 448
2cv2A Glutamyl-tRNA synthetase from thermus thermophilus in complex with tRNA(glu) and an enzyme inhibitor, glu-ams (see paper)
32% identity, 94% coverage: 6:284/296 of query aligns to 5:294/468 of 2cv2A
- active site: K246 (= K240)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R5 (= R6), A7 (= A8), S9 (= S10), G17 (= G18), I21 (≠ S22), E41 (= E42), Y187 (= Y181), R205 (= R199), A206 (≠ G200), E208 (≠ D202), W209 (≠ L203), L235 (≠ V229), L236 (≠ V230)
- binding : S9 (= S10), T43 (≠ I44), D44 (= D45), R47 (= R48), V145 (≠ A136), R163 (≠ Q156), Y168 (≠ Q161), E172 (= E166), V177 (= V171), K180 (≠ R174), S181 (≠ A175), Y187 (= Y181), E207 (≠ A201), E208 (≠ D202), W209 (≠ L203), V211 (≠ D205), R237 (≠ T231), K241 (≠ G235), L272 (vs. gap), M273 (≠ L263), G274 (= G264), E282 (≠ A272)
Sites not aligning to the query:
- binding : 299, 303, 304, 309, 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
32% identity, 94% coverage: 6:284/296 of query aligns to 5:294/468 of 2cv1A
- active site: K246 (= K240)
- binding adenosine-5'-triphosphate: P8 (= P9), S9 (= S10), G17 (= G18), T18 (≠ S19), I21 (≠ S22), R47 (= R48), A206 (≠ G200), W209 (≠ L203), L235 (≠ V229), L236 (≠ V230)
- binding (4s)-4-amino-5-hydroxypentanoic acid: R5 (= R6), A7 (= A8), E41 (= E42), Y187 (= Y181), R205 (= R199), W209 (≠ L203)
- binding : S9 (= S10), E41 (= E42), T43 (≠ I44), D44 (= D45), R47 (= R48), V145 (≠ A136), R163 (≠ Q156), V166 (≠ Q159), E172 (= E166), V177 (= V171), K180 (≠ R174), S181 (≠ A175), Y187 (= Y181), E207 (≠ A201), E208 (≠ D202), W209 (≠ L203), V211 (≠ D205), R237 (≠ T231), K241 (≠ G235), K243 (= K237), M273 (≠ L263), G274 (= G264), S276 (≠ D266), E282 (≠ A272)
Sites not aligning to the query:
- binding : 299, 303, 304, 309, 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)
32% identity, 94% coverage: 6:284/296 of query aligns to 5:294/468 of 2cuzA
1n78A Crystal structure of thermus thermophilus glutamyl-tRNA synthetase complexed with tRNA(glu) and glutamol-amp. (see paper)
32% identity, 94% coverage: 6:284/296 of query aligns to 5:294/468 of 1n78A
- active site: K246 (= K240)
- binding glutamol-amp: R5 (= R6), A7 (= A8), P8 (= P9), S9 (= S10), G17 (= G18), T18 (≠ S19), I21 (≠ S22), E41 (= E42), Y187 (= Y181), N191 (≠ V185), R205 (= R199), A206 (≠ G200), E208 (≠ D202), W209 (≠ L203), L235 (≠ V229), L236 (≠ V230)
- binding : S9 (= S10), T43 (≠ I44), D44 (= D45), R47 (= R48), V145 (≠ A136), R163 (≠ Q156), V166 (≠ Q159), Y168 (≠ Q161), E172 (= E166), V177 (= V171), K180 (≠ R174), S181 (≠ A175), Y187 (= Y181), E207 (≠ A201), E208 (≠ D202), W209 (≠ L203), L210 (≠ M204), V211 (≠ D205), R237 (≠ T231), K241 (≠ G235), M273 (≠ L263), G274 (= G264), E282 (≠ A272)
Sites not aligning to the query:
- binding : 297, 303, 304, 309, 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)
32% identity, 94% coverage: 6:284/296 of query aligns to 5:294/468 of 1j09A
- active site: K246 (= K240)
- binding adenosine-5'-triphosphate: H15 (= H16), E208 (≠ D202), L235 (≠ V229), L236 (≠ V230), K243 (= K237), I244 (≠ L238), S245 (= S239), K246 (= K240), R247 (≠ Q241)
- binding glutamic acid: R5 (= R6), A7 (= A8), S9 (= S10), E41 (= E42), Y187 (= Y181), N191 (≠ V185), R205 (= R199), W209 (≠ L203)
P27000 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
32% identity, 94% coverage: 6:284/296 of query aligns to 5:294/468 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).
6brlA Crystal structure of a glutamate tRNA ligase from elizabethkingia meningosepticum ccug26117 in complex with its amino acid
31% identity, 81% coverage: 4:243/296 of query aligns to 4:264/502 of 6brlA
3al0C Crystal structure of the glutamine transamidosome from thermotoga maritima in the glutamylation state. (see paper)
31% identity, 83% coverage: 4:248/296 of query aligns to 104:343/564 of 3al0C
- active site: S110 (= S10), K335 (= K240)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R106 (= R6), A108 (= A8), P109 (= P9), G118 (= G18), T122 (≠ S22), E142 (= E42), Y276 (= Y181), R294 (= R199), G295 (= G200), D297 (= D202), H298 (≠ L203), L324 (≠ V229), I325 (≠ V230), L333 (= L238)
- binding : T144 (≠ I44), D145 (= D45), R148 (= R48), Y208 (≠ C100), P213 (≠ I105), K252 (≠ Q156), M255 (≠ Q159), I266 (≠ V171), K269 (≠ R174), S270 (≠ A175), Y276 (= Y181), D297 (= D202), H298 (≠ L203), L299 (≠ M204), S300 (≠ D205), N301 (≠ S206), K304 (≠ R209), R330 (≠ G235), P332 (≠ K237)
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
4griB Crystal structure of a glutamyl-tRNA synthetase glurs from borrelia burgdorferi bound to glutamic acid and zinc (see paper)
31% identity, 82% coverage: 4:247/296 of query aligns to 3:260/485 of 4griB
- active site: S9 (= S10), K253 (= K240)
- binding glutamic acid: R5 (= R6), A7 (= A8), S9 (= S10), E41 (= E42), Y194 (= Y181), R212 (= R199), W216 (≠ L203)
- binding zinc ion: C105 (= C98), C107 (= C100), Y128 (= Y121), C132 (= C125)
8vc5A Crystal structure of glutamyl-tRNA synthetase glurs from pseudomonas aeruginosa (zinc bound)
30% identity, 83% coverage: 2:247/296 of query aligns to 3:261/488 of 8vc5A
3aiiA Archaeal non-discriminating glutamyl-tRNA synthetase from methanothermobacter thermautotrophicus (see paper)
30% identity, 75% coverage: 6:226/296 of query aligns to 14:228/455 of 3aiiA
Sites not aligning to the query:
4h3sA The structure of glutaminyl-tRNA synthetase from saccharomyces cerevisiae (see paper)
29% identity, 34% coverage: 4:105/296 of query aligns to 39:139/585 of 4h3sA
Sites not aligning to the query:
Query Sequence
>BPHYT_RS06160 FitnessBrowser__BFirm:BPHYT_RS06160
MTYRGRFAPSPTGPLHFGSLVSALASWLDARAHRGAWLVRVEDIDGPRTVPGAAEDILAT
LERFGMHADEPPVWQSARMPRYQEALEQLKANGVIYPCGCTRKEIADSLLNAHTRNTTLA
YPGTCRDGLHGKPARAWRLRVPDGDSAVITFEDRWQGKQTQNLATEVGDFVLKRADDQWA
YQLAVVVDDADAGITHIVRGADLMDSTARQIYLQRCLGVPTPEYLHVPVVTNEAGEKLSK
QNGATALDSEKPFEALSAAARHLGLDLENAAAQTTLDGFYAAATAAWAKRMGLPAA
Or try a new SitesBLAST search
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