SitesBLAST
Comparing 200059 FitnessBrowser__MR1:200059 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)
56% identity, 93% coverage: 15:291/299 of query aligns to 16:295/308 of P27305
- E55 (= E54) 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)
55% identity, 93% coverage: 15:291/299 of query aligns to 4:281/290 of 4a91A
- active site: S11 (= S22), K229 (= K240)
- binding glutamic acid: R7 (= R18), A9 (= A20), S11 (= S22), E43 (= E54), Y170 (= Y181), R188 (= R199), L192 (= L203)
- binding zinc ion: C99 (= C110), C101 (= C112), Y113 (= Y124), C117 (= C128)
P04805 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Escherichia coli (strain K12) (see 4 papers)
33% identity, 92% coverage: 18:291/299 of query aligns to 6:293/471 of P04805
- C98 (= C110) mutation to S: 10-fold decrease in activity. Strong decrease in zinc content.
- C100 (= C112) 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 (= C128) 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 (= H129) mutation to Q: No change in activity or in zinc content.
- H131 (≠ L131) mutation to Q: No change in activity or in zinc content.
- H132 (≠ A132) mutation to Q: No change in activity or in zinc content.
- C138 (≠ G138) 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.
8i9iA Glutamyl-tRNA synthetase from escherichia coli bound to glutamate and zinc
33% identity, 92% coverage: 18:291/299 of query aligns to 6:293/468 of 8i9iA
2cfoA Non-discriminating glutamyl-tRNA synthetase from thermosynechococcus elongatus in complex with glu (see paper)
32% identity, 92% coverage: 18:291/299 of query aligns to 5:305/484 of 2cfoA
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)
32% identity, 92% coverage: 18:291/299 of query aligns to 6:306/485 of Q8DLI5
- R6 (= R18) binding
- Y192 (= Y181) binding
4griB Crystal structure of a glutamyl-tRNA synthetase glurs from borrelia burgdorferi bound to glutamic acid and zinc (see paper)
31% identity, 83% coverage: 18:266/299 of query aligns to 5:283/485 of 4griB
- active site: S9 (= S22), K253 (= K240)
- binding glutamic acid: R5 (= R18), A7 (= A20), S9 (= S22), E41 (= E54), Y194 (= Y181), R212 (= R199), W216 (≠ L203)
- binding zinc ion: C105 (= C110), C107 (= C112), Y128 (= Y124), C132 (= C128)
3al0C Crystal structure of the glutamine transamidosome from thermotoga maritima in the glutamylation state. (see paper)
31% identity, 81% coverage: 18:260/299 of query aligns to 106:355/564 of 3al0C
- active site: S110 (= S22), K335 (= K240)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R106 (= R18), A108 (= A20), P109 (= P21), G118 (= G30), T122 (≠ A34), E142 (= E54), Y276 (= Y181), R294 (= R199), G295 (= G200), D297 (= D202), H298 (≠ L203), L324 (= L229), I325 (≠ A230), L333 (= L238)
- binding : T144 (≠ I56), D145 (= D57), R148 (= R60), Y208 (≠ C112), P213 (vs. gap), K252 (≠ M156), M255 (≠ V159), I266 (= I171), K269 (≠ R174), S270 (= S175), Y276 (= Y181), D297 (= D202), H298 (≠ L203), L299 (≠ I204), S300 (≠ E205), N301 (≠ A206), 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
1g59A Glutamyl-tRNA synthetase complexed with tRNA(glu). (see paper)
34% identity, 82% coverage: 16:260/299 of query aligns to 3:266/468 of 1g59A
- binding : D44 (= D57), R45 (≠ P58), A46 (≠ P59), R47 (= R60), P109 (≠ Q111), V145 (≠ A139), R163 (≠ M156), V166 (= V159), E172 (≠ A166), V177 (≠ I171), K180 (≠ R174), S181 (= S175), D182 (= D176), E207 (≠ C201), E208 (≠ D202), R237 (≠ C231), K241 (≠ G235), T242 (≠ F236), K243 (= K237)
Sites not aligning to the query:
- binding : 273, 274, 282, 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)
33% identity, 82% coverage: 16:260/299 of query aligns to 3:266/468 of 2cv2A
- active site: K246 (= K240)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R5 (= R18), A7 (= A20), S9 (= S22), G17 (= G30), I21 (≠ A34), E41 (= E54), Y187 (= Y181), R205 (= R199), A206 (≠ G200), E208 (≠ D202), W209 (≠ L203), L235 (= L229), L236 (≠ A230)
- binding : S9 (= S22), T43 (≠ I56), D44 (= D57), R47 (= R60), V145 (≠ A139), R163 (≠ M156), Y168 (≠ V161), E172 (≠ A166), V177 (≠ I171), K180 (≠ R174), S181 (= S175), Y187 (= Y181), E207 (≠ C201), E208 (≠ D202), W209 (≠ L203), V211 (≠ E205), R237 (≠ C231), K241 (≠ G235)
Sites not aligning to the query:
- binding : 272, 273, 274, 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
33% identity, 82% coverage: 16:260/299 of query aligns to 3:266/468 of 2cv1A
- active site: K246 (= K240)
- binding adenosine-5'-triphosphate: P8 (= P21), S9 (= S22), G17 (= G30), T18 (≠ S31), I21 (≠ A34), R47 (= R60), A206 (≠ G200), W209 (≠ L203), L235 (= L229), L236 (≠ A230)
- binding (4s)-4-amino-5-hydroxypentanoic acid: R5 (= R18), A7 (= A20), E41 (= E54), Y187 (= Y181), R205 (= R199), W209 (≠ L203)
- binding : S9 (= S22), E41 (= E54), T43 (≠ I56), D44 (= D57), R47 (= R60), V145 (≠ A139), R163 (≠ M156), V166 (= V159), E172 (≠ A166), V177 (≠ I171), K180 (≠ R174), S181 (= S175), Y187 (= Y181), E207 (≠ C201), E208 (≠ D202), W209 (≠ L203), V211 (≠ E205), R237 (≠ C231), K241 (≠ G235), K243 (= K237)
Sites not aligning to the query:
- binding : 273, 274, 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)
33% identity, 82% coverage: 16:260/299 of query aligns to 3:266/468 of 2cuzA
1n78A Crystal structure of thermus thermophilus glutamyl-tRNA synthetase complexed with tRNA(glu) and glutamol-amp. (see paper)
33% identity, 82% coverage: 16:260/299 of query aligns to 3:266/468 of 1n78A
- active site: K246 (= K240)
- binding glutamol-amp: R5 (= R18), A7 (= A20), P8 (= P21), S9 (= S22), G17 (= G30), T18 (≠ S31), I21 (≠ A34), E41 (= E54), Y187 (= Y181), N191 (≠ V185), R205 (= R199), A206 (≠ G200), E208 (≠ D202), W209 (≠ L203), L235 (= L229), L236 (≠ A230)
- binding : S9 (= S22), T43 (≠ I56), D44 (= D57), R47 (= R60), V145 (≠ A139), R163 (≠ M156), V166 (= V159), Y168 (≠ V161), E172 (≠ A166), V177 (≠ I171), K180 (≠ R174), S181 (= S175), Y187 (= Y181), E207 (≠ C201), E208 (≠ D202), W209 (≠ L203), L210 (≠ I204), V211 (≠ E205), R237 (≠ C231), K241 (≠ G235)
Sites not aligning to the query:
- binding : 273, 274, 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)
33% identity, 82% coverage: 16:260/299 of query aligns to 3:266/468 of 1j09A
- active site: K246 (= K240)
- binding adenosine-5'-triphosphate: H15 (= H28), E208 (≠ D202), L235 (= L229), L236 (≠ A230), K243 (= K237), I244 (≠ L238), S245 (= S239), K246 (= K240), R247 (≠ Q241)
- binding glutamic acid: R5 (= R18), A7 (= A20), S9 (= S22), E41 (= E54), 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)
33% identity, 82% coverage: 16:260/299 of query aligns to 3:266/468 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, 85% coverage: 14:266/299 of query aligns to 2:255/380 of 4g6zA
8vc5A Crystal structure of glutamyl-tRNA synthetase glurs from pseudomonas aeruginosa (zinc bound)
29% identity, 91% coverage: 18:289/299 of query aligns to 7:301/488 of 8vc5A
6brlA Crystal structure of a glutamate tRNA ligase from elizabethkingia meningosepticum ccug26117 in complex with its amino acid
28% identity, 75% coverage: 18:242/299 of query aligns to 6:263/502 of 6brlA
3aiiA Archaeal non-discriminating glutamyl-tRNA synthetase from methanothermobacter thermautotrophicus (see paper)
29% identity, 72% coverage: 12:226/299 of query aligns to 8:228/455 of 3aiiA
Sites not aligning to the query:
4h3sA The structure of glutaminyl-tRNA synthetase from saccharomyces cerevisiae (see paper)
27% identity, 47% coverage: 18:158/299 of query aligns to 41:176/585 of 4h3sA
Sites not aligning to the query:
Query Sequence
>200059 FitnessBrowser__MR1:200059
MMATLTTAISPQGPYVGRFAPSPSGALHFGSLVAALGSYLRARSLGGKWLIRIEDIDPPR
EVKGAADDILRTLEAYGFEWDDTVLYQSARTDAYQAKLDQLLAQDDAYFCQCSRKQIQAM
GGIYDGRCHQLATPHQSGAIRLVNRAQVAEFTDNLMGKVVVDHDFATEDFIIKRSDGLYA
YQLAVVLDDAHQGISEVVRGCDLIEASCRQLSLYQSLGLTAPQWLHLPLACLTPGFKLSK
QNHAQAIDKQHPQASLNAALTFLGQSTVEPTSAAQMLAQAVAQFELTAVPKQREIILTA
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