SitesBLAST
Comparing WP_012975077.1 NCBI__GCF_000010725.1:WP_012975077.1 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)
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)
39% identity, 93% coverage: 6:272/286 of query aligns to 5:265/485 of Q8DLI5
- R6 (= R7) binding L-glutamate
- Y192 (= Y199) binding L-glutamate
2cfoA Non-discriminating glutamyl-tRNA synthetase from thermosynechococcus elongatus in complex with glu (see paper)
39% identity, 93% coverage: 6:272/286 of query aligns to 4:264/484 of 2cfoA
8i9iA Glutamyl-tRNA synthetase from escherichia coli bound to glutamate and zinc
33% identity, 95% coverage: 4:275/286 of query aligns to 3:257/468 of 8i9iA
P04805 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Escherichia coli (strain K12) (see 4 papers)
33% identity, 95% coverage: 4:275/286 of query aligns to 3:257/471 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 (= C134) mutation to S: Loss of activity. Strong decrease in zinc content.
- H127 (= H136) mutation to Q: 10-fold decrease in activity. Strong decrease in zinc content.
- H129 (≠ S138) mutation to Q: No change in activity or in zinc content.
- H131 (≠ R145) mutation to Q: No change in activity or in zinc content.
- H132 (≠ I146) mutation to Q: No change in activity or in zinc content.
- C138 (≠ W152) mutation to S: No change in activity or in zinc content.
- S239 (≠ A257) 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)
35% identity, 95% coverage: 6:278/286 of query aligns to 5:245/380 of 4g6zA
P27305 Glutamyl-Q tRNA(Asp) synthetase; Glu-Q-RSs; EC 6.1.1.- from Escherichia coli (strain K12) (see paper)
37% identity, 92% coverage: 2:265/286 of query aligns to 14:248/308 of P27305
- E55 (= E43) binding L-glutamate
- Y182 (= Y199) binding L-glutamate
- R200 (= R217) binding L-glutamate
2cv2A Glutamyl-tRNA synthetase from thermus thermophilus in complex with tRNA(glu) and an enzyme inhibitor, glu-ams (see paper)
35% identity, 98% coverage: 4:284/286 of query aligns to 2:275/468 of 2cv2A
- active site: K246 (= K258)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R5 (= R7), A7 (= A9), S9 (= S11), G17 (= G19), I21 (≠ S23), E41 (= E43), Y187 (= Y199), R205 (= R217), A206 (≠ G218), E208 (≠ D220), W209 (≠ L221), L235 (= L247), L236 (= L248)
- binding : S9 (= S11), T43 (≠ I45), D44 (= D46), R47 (= R49), V145 (≠ A153), R163 (= R175), Y168 (≠ A180), E172 (≠ L184), V177 (= V189), K180 (≠ R192), S181 (≠ K193), Y187 (= Y199), E207 (= E219), E208 (≠ D220), W209 (≠ L221), V211 (≠ F223), R237 (= R249), K241 (≠ G253), L272 (= L281), M273 (≠ A282), G274 (= G283)
Sites not aligning to the query:
- binding : 282, 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
35% identity, 98% coverage: 4:284/286 of query aligns to 2:275/468 of 2cv1A
- active site: K246 (= K258)
- binding adenosine-5'-triphosphate: P8 (= P10), S9 (= S11), G17 (= G19), T18 (≠ H20), I21 (≠ S23), R47 (= R49), A206 (≠ G218), W209 (≠ L221), L235 (= L247), L236 (= L248)
- binding (4s)-4-amino-5-hydroxypentanoic acid: R5 (= R7), A7 (= A9), E41 (= E43), Y187 (= Y199), R205 (= R217), W209 (≠ L221)
- binding : S9 (= S11), E41 (= E43), T43 (≠ I45), D44 (= D46), R47 (= R49), V145 (≠ A153), R163 (= R175), V166 (≠ Q178), E172 (≠ L184), V177 (= V189), K180 (≠ R192), S181 (≠ K193), Y187 (= Y199), E207 (= E219), E208 (≠ D220), W209 (≠ L221), V211 (≠ F223), R237 (= R249), K241 (≠ G253), K243 (≠ R255), M273 (≠ A282), G274 (= G283)
Sites not aligning to the query:
- binding : 276, 282, 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)
35% identity, 98% coverage: 4:284/286 of query aligns to 2:275/468 of 2cuzA
1n78A Crystal structure of thermus thermophilus glutamyl-tRNA synthetase complexed with tRNA(glu) and glutamol-amp. (see paper)
35% identity, 98% coverage: 4:284/286 of query aligns to 2:275/468 of 1n78A
- active site: K246 (= K258)
- binding glutamol-amp: R5 (= R7), A7 (= A9), P8 (= P10), S9 (= S11), G17 (= G19), T18 (≠ H20), I21 (≠ S23), E41 (= E43), Y187 (= Y199), N191 (≠ V203), R205 (= R217), A206 (≠ G218), E208 (≠ D220), W209 (≠ L221), L235 (= L247), L236 (= L248)
- binding : S9 (= S11), T43 (≠ I45), D44 (= D46), R47 (= R49), V145 (≠ A153), R163 (= R175), V166 (≠ Q178), Y168 (≠ A180), E172 (≠ L184), V177 (= V189), K180 (≠ R192), S181 (≠ K193), Y187 (= Y199), E207 (= E219), E208 (≠ D220), W209 (≠ L221), L210 (≠ F222), V211 (≠ F223), R237 (= R249), K241 (≠ G253), M273 (≠ A282), G274 (= G283)
Sites not aligning to the query:
- binding : 282, 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)
35% identity, 98% coverage: 4:284/286 of query aligns to 2:275/468 of 1j09A
- active site: K246 (= K258)
- binding adenosine-5'-triphosphate: H15 (= H17), E208 (≠ D220), L235 (= L247), L236 (= L248), K243 (≠ R255), I244 (≠ L256), S245 (≠ A257), K246 (= K258), R247 (= R259)
- binding glutamic acid: R5 (= R7), A7 (= A9), S9 (= S11), E41 (= E43), Y187 (= Y199), N191 (≠ V203), R205 (= R217), W209 (≠ L221)
P27000 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
35% identity, 98% coverage: 4:284/286 of query aligns to 2:275/468 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).
1g59A Glutamyl-tRNA synthetase complexed with tRNA(glu). (see paper)
35% identity, 98% coverage: 4:284/286 of query aligns to 2:275/468 of 1g59A
- binding : D44 (= D46), R45 (≠ P47), A46 (≠ N48), R47 (= R49), P109 (≠ R103), V145 (≠ A153), R163 (= R175), V166 (≠ Q178), E172 (≠ L184), V177 (= V189), K180 (≠ R192), S181 (≠ K193), D182 (= D194), E207 (= E219), E208 (≠ D220), R237 (= R249), K241 (≠ G253), T242 (≠ E254), K243 (≠ R255), M273 (≠ A282), G274 (= G283)
Sites not aligning to the query:
- binding : 282, 299, 300, 303, 304, 309, 312, 319, 357, 358, 417, 426, 427, 432, 435, 442, 443, 444, 445, 446, 447, 448
4a91A Crystal structure of the glutamyl-queuosine trnaasp synthetase from e. Coli complexed with l-glutamate (see paper)
37% identity, 90% coverage: 2:259/286 of query aligns to 2:230/290 of 4a91A
- active site: S11 (= S11), K229 (= K258)
- binding glutamic acid: R7 (= R7), A9 (= A9), S11 (= S11), E43 (= E43), Y170 (= Y199), R188 (= R217), L192 (= L221)
- binding zinc ion: C99 (= C99), C101 (= C101), Y113 (= Y130), C117 (= C134)
3al0C Crystal structure of the glutamine transamidosome from thermotoga maritima in the glutamylation state. (see paper)
30% identity, 93% coverage: 6:272/286 of query aligns to 105:349/564 of 3al0C
- active site: S110 (= S11), K335 (= K258)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R106 (= R7), A108 (= A9), P109 (= P10), G118 (= G19), T122 (≠ S23), E142 (= E43), Y276 (= Y199), R294 (= R217), G295 (= G218), D297 (= D220), H298 (≠ L221), L324 (= L247), I325 (≠ L248), L333 (= L256)
- binding : T144 (≠ I45), D145 (= D46), R148 (= R49), Y208 (≠ C101), P213 (≠ I106), K252 (≠ R175), M255 (≠ Q178), I266 (≠ V189), K269 (≠ R192), S270 (≠ K193), Y276 (= Y199), D297 (= D220), H298 (≠ L221), L299 (≠ F222), S300 (≠ F223), N301 (≠ A224), K304 (≠ L227), R330 (≠ G253), P332 (≠ R255)
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
8vc5A Crystal structure of glutamyl-tRNA synthetase glurs from pseudomonas aeruginosa (zinc bound)
33% identity, 100% coverage: 1:286/286 of query aligns to 1:279/488 of 8vc5A
4griB Crystal structure of a glutamyl-tRNA synthetase glurs from borrelia burgdorferi bound to glutamic acid and zinc (see paper)
31% identity, 95% coverage: 6:278/286 of query aligns to 4:273/485 of 4griB
- active site: S9 (= S11), K253 (= K258)
- binding glutamic acid: R5 (= R7), A7 (= A9), S9 (= S11), E41 (= E43), Y194 (= Y199), R212 (= R217), W216 (≠ L221)
- binding zinc ion: C105 (= C99), C107 (= C101), Y128 (= Y130), C132 (= C134)
6brlA Crystal structure of a glutamate tRNA ligase from elizabethkingia meningosepticum ccug26117 in complex with its amino acid (see paper)
31% identity, 89% coverage: 6:260/286 of query aligns to 5:263/502 of 6brlA
3aiiA Archaeal non-discriminating glutamyl-tRNA synthetase from methanothermobacter thermautotrophicus (see paper)
31% identity, 98% coverage: 3:281/286 of query aligns to 10:273/455 of 3aiiA
P00962 Glutamine--tRNA ligase; Glutaminyl-tRNA synthetase; GlnRS; EC 6.1.1.18 from Escherichia coli (strain K12) (see 7 papers)
38% identity, 32% coverage: 6:97/286 of query aligns to 30:121/554 of P00962
- R31 (= R7) mutation R->A,K: Decreased affinity for glutamine and catalytic activity.
- EPN 35:37 (≠ SPT 11:13) binding ATP
- 41:47 (vs. 17:23, 71% identical) binding ATP
- D67 (≠ E43) binding L-glutamine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 212 binding L-glutamine
- 230 C→R: Decreases catalytic activity 1000-fold, but has no effect on affinity for glutamine. Loss of catalytic activity; when associated with I-256.
- 231 binding ATP
- 256 Q→I: Loss of catalytic activity; when associated with R-230.
- 261:262 binding ATP
- 269:271 binding ATP
- 317:324 Interaction with tRNA
Query Sequence
>WP_012975077.1 NCBI__GCF_000010725.1:WP_012975077.1
MSDLVTRFAPSPTGHLHLGHAHSALFGWTTARGAAGRFLLRIEDIDPNRCRPEFERDLIE
DLGWLGLDWDGPVRRQSDHFDDYRAALARLESLGVLYPCFCTRKDIAAEIARAAAAPHGP
GPTSSDGPLYPGTCRHRSPQERAERIGDGESWALRLDVEAARRLTGPLRWHDRARGWQQA
TPELLGDVVLARKDTPTSYHLSVTVDDHLQGVTLVTRGEDLFFATHLHRLLQALLGYDPP
DYHHHGLLRNAAGERLAKRDRAQSLRSLREEGRGPAEVRALAGFPG
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