SitesBLAST
Comparing WP_011885600.1 NCBI__GCF_000016205.1:WP_011885600.1 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 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)
43% identity, 99% coverage: 4:297/297 of query aligns to 16:297/308 of P27305
- E55 (= E43) binding L-glutamate
- Y182 (= Y182) binding L-glutamate
- R200 (= R200) binding L-glutamate
4a91A Crystal structure of the glutamyl-queuosine trnaasp synthetase from e. Coli complexed with l-glutamate (see paper)
43% identity, 99% coverage: 4:297/297 of query aligns to 4:283/290 of 4a91A
- active site: S11 (= S11), K229 (= K241)
- binding glutamic acid: R7 (= R7), A9 (= A9), S11 (= S11), E43 (= E43), Y170 (= Y182), R188 (= R200), L192 (= L204)
- binding zinc ion: C99 (= C99), C101 (= C101), Y113 (= Y122), C117 (= C126)
8i9iA Glutamyl-tRNA synthetase from escherichia coli bound to glutamate and zinc
35% identity, 97% coverage: 5:293/297 of query aligns to 4:299/468 of 8i9iA
P04805 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Escherichia coli (strain K12) (see 4 papers)
35% identity, 97% coverage: 5:293/297 of query aligns to 4:299/471 of P04805
- C98 (= C99) mutation to S: 10-fold decrease in activity. Strong decrease in zinc content.
- C100 (= C101) 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 (= C126) mutation to S: Loss of activity. Strong decrease in zinc content.
- H127 (vs. gap) mutation to Q: 10-fold decrease in activity. Strong decrease in zinc content.
- H129 (≠ G129) mutation to Q: No change in activity or in zinc content.
- H131 (= H131) mutation to Q: No change in activity or in zinc content.
- H132 (≠ G132) mutation to Q: No change in activity or in zinc content.
- C138 (≠ W138) mutation to S: No change in activity or in zinc content.
- S239 (= S240) 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)
36% identity, 82% coverage: 5:248/297 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)
37% identity, 82% coverage: 5:248/297 of query aligns to 4:258/485 of Q8DLI5
- R6 (= R7) binding L-glutamate
- Y192 (= Y182) binding L-glutamate
2cfoA Non-discriminating glutamyl-tRNA synthetase from thermosynechococcus elongatus in complex with glu (see paper)
37% identity, 82% coverage: 5:248/297 of query aligns to 3:257/484 of 2cfoA
6brlA Crystal structure of a glutamate tRNA ligase from elizabethkingia meningosepticum ccug26117 in complex with its amino acid (see paper)
34% identity, 81% coverage: 5:244/297 of query aligns to 4:264/502 of 6brlA
4griB Crystal structure of a glutamyl-tRNA synthetase glurs from borrelia burgdorferi bound to glutamic acid and zinc (see paper)
30% identity, 94% coverage: 5:282/297 of query aligns to 3:301/485 of 4griB
- active site: S9 (= S11), K253 (= K241)
- binding glutamic acid: R5 (= R7), A7 (= A9), S9 (= S11), E41 (= E43), Y194 (= Y182), R212 (= R200), W216 (≠ L204)
- binding zinc ion: C105 (= C99), C107 (= C101), Y128 (≠ H114), C132 (≠ T118)
3al0C Crystal structure of the glutamine transamidosome from thermotoga maritima in the glutamylation state. (see paper)
33% identity, 89% coverage: 5:268/297 of query aligns to 104:363/564 of 3al0C
- active site: S110 (= S11), K335 (= K241)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R106 (= R7), A108 (= A9), P109 (= P10), G118 (= G19), T122 (≠ G23), E142 (= E43), Y276 (= Y182), R294 (= R200), G295 (= G201), D297 (= D203), H298 (≠ L204), L324 (≠ V230), I325 (≠ V231), L333 (= L239)
- binding : T144 (≠ I45), D145 (= D46), R148 (= R49), Y208 (= Y97), P213 (≠ T102), K252 (≠ D147), M255 (≠ I150), I266 (≠ V172), K269 (≠ R175), S270 (≠ A176), Y276 (= Y182), D297 (= D203), H298 (≠ L204), L299 (= L205), S300 (≠ D206), N301 (≠ S207), K304 (≠ R210), R330 (≠ G236), P332 (≠ K238), G363 (= G268)
Sites not aligning to the query:
- binding : 364, 365, 370, 387, 389, 391, 392, 397, 400, 407, 446, 447, 453, 457, 509, 520, 524, 527, 535, 536, 538, 539
1g59A Glutamyl-tRNA synthetase complexed with tRNA(glu). (see paper)
32% identity, 96% coverage: 7:290/297 of query aligns to 5:297/468 of 1g59A
- binding : D44 (= D46), R45 (≠ G47), A46 (≠ P48), R47 (= R49), P109 (≠ R103), V145 (≠ A137), R163 (≠ D147), V166 (≠ I150), E172 (= E167), V177 (= V172), K180 (≠ R175), S181 (≠ A176), D182 (= D177), E207 (≠ A202), E208 (≠ D203), R237 (≠ V232), K241 (≠ G236), T242 (≠ E237), K243 (= K238), M273 (≠ L264), G274 (= G265), E282 (≠ A273)
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, 96% coverage: 7:290/297 of query aligns to 5:297/468 of 2cv2A
- active site: K246 (= K241)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R5 (= R7), A7 (= A9), S9 (= S11), G17 (= G19), I21 (≠ G23), E41 (= E43), Y187 (= Y182), R205 (= R200), A206 (≠ G201), E208 (≠ D203), W209 (≠ L204), L235 (≠ V230), L236 (≠ V231)
- binding : S9 (= S11), T43 (≠ I45), D44 (= D46), R47 (= R49), V145 (≠ A137), R163 (≠ D147), Y168 (≠ F152), E172 (= E167), V177 (= V172), K180 (≠ R175), S181 (≠ A176), Y187 (= Y182), E207 (≠ A202), E208 (≠ D203), W209 (≠ L204), V211 (≠ D206), R237 (≠ V232), K241 (≠ G236), L272 (≠ H263), M273 (≠ L264), G274 (= G265), E282 (≠ A273)
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, 96% coverage: 7:290/297 of query aligns to 5:297/468 of 2cv1A
- active site: K246 (= K241)
- binding adenosine-5'-triphosphate: P8 (= P10), S9 (= S11), G17 (= G19), T18 (≠ S20), I21 (≠ G23), R47 (= R49), A206 (≠ G201), W209 (≠ L204), L235 (≠ V230), L236 (≠ V231)
- binding (4s)-4-amino-5-hydroxypentanoic acid: R5 (= R7), A7 (= A9), E41 (= E43), Y187 (= Y182), R205 (= R200), W209 (≠ L204)
- binding : S9 (= S11), E41 (= E43), T43 (≠ I45), D44 (= D46), R47 (= R49), V145 (≠ A137), R163 (≠ D147), V166 (≠ I150), E172 (= E167), V177 (= V172), K180 (≠ R175), S181 (≠ A176), Y187 (= Y182), E207 (≠ A202), E208 (≠ D203), W209 (≠ L204), V211 (≠ D206), R237 (≠ V232), K241 (≠ G236), K243 (= K238), M273 (≠ L264), G274 (= G265), S276 (≠ A267), E282 (≠ A273)
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, 96% coverage: 7:290/297 of query aligns to 5:297/468 of 2cuzA
1n78A Crystal structure of thermus thermophilus glutamyl-tRNA synthetase complexed with tRNA(glu) and glutamol-amp. (see paper)
32% identity, 96% coverage: 7:290/297 of query aligns to 5:297/468 of 1n78A
- active site: K246 (= K241)
- binding glutamol-amp: R5 (= R7), A7 (= A9), P8 (= P10), S9 (= S11), G17 (= G19), T18 (≠ S20), I21 (≠ G23), E41 (= E43), Y187 (= Y182), N191 (≠ V186), R205 (= R200), A206 (≠ G201), E208 (≠ D203), W209 (≠ L204), L235 (≠ V230), L236 (≠ V231)
- binding : S9 (= S11), T43 (≠ I45), D44 (= D46), R47 (= R49), V145 (≠ A137), R163 (≠ D147), V166 (≠ I150), Y168 (≠ F152), E172 (= E167), V177 (= V172), K180 (≠ R175), S181 (≠ A176), Y187 (= Y182), E207 (≠ A202), E208 (≠ D203), W209 (≠ L204), L210 (= L205), V211 (≠ D206), R237 (≠ V232), K241 (≠ G236), M273 (≠ L264), G274 (= G265), E282 (≠ A273), R297 (= R290)
Sites not aligning to the query:
- binding : 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, 96% coverage: 7:290/297 of query aligns to 5:297/468 of 1j09A
- active site: K246 (= K241)
- binding adenosine-5'-triphosphate: H15 (= H17), E208 (≠ D203), L235 (≠ V230), L236 (≠ V231), K243 (= K238), I244 (≠ L239), S245 (= S240), K246 (= K241), R247 (≠ Q242)
- binding glutamic acid: R5 (= R7), A7 (= A9), S9 (= S11), E41 (= E43), Y187 (= Y182), N191 (≠ V186), R205 (= R200), W209 (≠ L204)
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, 96% coverage: 7:290/297 of query aligns to 5:297/468 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).
8vc5A Crystal structure of glutamyl-tRNA synthetase glurs from pseudomonas aeruginosa (zinc bound)
31% identity, 91% coverage: 1:271/297 of query aligns to 1:285/488 of 8vc5A
3aiiA Archaeal non-discriminating glutamyl-tRNA synthetase from methanothermobacter thermautotrophicus (see paper)
29% identity, 74% coverage: 7:227/297 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)
30% identity, 35% coverage: 5:107/297 of query aligns to 39:140/585 of 4h3sA
Sites not aligning to the query:
Query Sequence
>WP_011885600.1 NCBI__GCF_000016205.1:WP_011885600.1
MNGYRGRFAPSPTGPLHFGSLVGALASWLDARAHGGAWLVRIEDIDGPRTVPGADDDILA
TLAHFGMTPDEPPVWQSTRDARYAAELERLRAAGLVYPCGCTRKEIADSLRAAHERHTTL
AYPGTCRTGLHGKPARAWRLRVPDGADAIIRFDDRWQHEQQQNLATEVGDFVLKRADGQW
AYQLAVVVDDADARITHVVRGADLLDSTARQIYLQRCLGVPTPAYLHVPVVVAANGEKLS
KQTGALALERDDPLPALRAAAAHLGLAGDGELAGDTLESFYAAATAAWARRFGPRSA
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