SitesBLAST
Comparing 5210702 FitnessBrowser__PV4:5210702 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, 87% coverage: 30:308/319 of query aligns to 13:294/308 of P27305
- E55 (= E72) binding
- Y182 (= Y199) binding
- R200 (= R217) binding
4a91A Crystal structure of the glutamyl-queuosine trnaasp synthetase from e. Coli complexed with l-glutamate (see paper)
55% identity, 87% coverage: 30:308/319 of query aligns to 1:280/290 of 4a91A
- active site: S11 (= S40), K229 (= K258)
- binding glutamic acid: R7 (= R36), A9 (= A38), S11 (= S40), E43 (= E72), Y170 (= Y199), R188 (= R217), L192 (= L221)
- binding zinc ion: C99 (= C128), C101 (= C130), Y113 (= Y142), C117 (= C146)
P04805 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Escherichia coli (strain K12) (see 4 papers)
33% identity, 79% coverage: 36:287/319 of query aligns to 6:273/471 of P04805
- C98 (= C128) mutation to S: 10-fold decrease in activity. Strong decrease in zinc content.
- C100 (= C130) 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 (= C146) mutation to S: Loss of activity. Strong decrease in zinc content.
- H127 (≠ I148) mutation to Q: 10-fold decrease in activity. Strong decrease in zinc content.
- H129 (≠ T150) mutation to Q: No change in activity or in zinc content.
- H131 (≠ K152) mutation to Q: No change in activity or in zinc content.
- H132 (= H153) mutation to Q: No change in activity or in zinc content.
- C138 (vs. gap) mutation to S: No change in activity or in zinc content.
- S239 (= S257) 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, 79% coverage: 36:287/319 of query aligns to 6:273/468 of 8i9iA
2cfoA Non-discriminating glutamyl-tRNA synthetase from thermosynechococcus elongatus in complex with glu (see paper)
30% identity, 86% coverage: 36:309/319 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)
30% identity, 86% coverage: 36:309/319 of query aligns to 6:306/485 of Q8DLI5
- R6 (= R36) binding
- Y192 (= Y199) binding
4g6zA Crystal structure of a glutamyl-tRNA synthetase glurs from burkholderia thailandensis bound to l-glutamate (see paper)
31% identity, 87% coverage: 31:307/319 of query aligns to 1:276/380 of 4g6zA
3al0C Crystal structure of the glutamine transamidosome from thermotoga maritima in the glutamylation state. (see paper)
31% identity, 76% coverage: 36:278/319 of query aligns to 106:355/564 of 3al0C
- active site: S110 (= S40), K335 (= K258)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R106 (= R36), A108 (= A38), P109 (= P39), G118 (= G48), T122 (≠ A52), E142 (= E72), Y276 (= Y199), R294 (= R217), G295 (= G218), D297 (= D220), H298 (≠ L221), L324 (= L247), I325 (≠ A248), L333 (= L256)
- binding : T144 (≠ I74), D145 (= D75), R148 (= R78), Y208 (≠ C130), P213 (vs. gap), K252 (≠ L174), M255 (≠ I177), I266 (= I189), K269 (≠ R192), S270 (≠ R193), Y276 (= Y199), D297 (= D220), H298 (≠ L221), L299 (= L222), S300 (≠ T223), N301 (≠ S224), K304 (≠ R227), R330 (≠ G253), P332 (≠ K255)
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, 75% coverage: 36:275/319 of query aligns to 5:275/485 of 4griB
- active site: S9 (= S40), K253 (= K258)
- binding glutamic acid: R5 (= R36), A7 (= A38), S9 (= S40), E41 (= E72), Y194 (= Y199), R212 (= R217), W216 (≠ L221)
- binding zinc ion: C105 (= C128), C107 (= C130), Y128 (= Y142), C132 (= C146)
1g59A Glutamyl-tRNA synthetase complexed with tRNA(glu). (see paper)
32% identity, 77% coverage: 34:278/319 of query aligns to 3:266/468 of 1g59A
- binding : D44 (= D75), R45 (≠ P76), A46 (≠ P77), R47 (= R78), P109 (vs. gap), V145 (≠ A157), R163 (≠ L174), V166 (≠ I177), E172 (≠ A184), V177 (≠ I189), K180 (≠ R192), S181 (≠ R193), D182 (= D194), E207 (≠ A219), E208 (≠ D220), R237 (≠ C249), K241 (≠ G253), T242 (≠ M254), K243 (= K255)
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)
32% identity, 77% coverage: 34:278/319 of query aligns to 3:266/468 of 2cv2A
- active site: K246 (= K258)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R5 (= R36), A7 (= A38), S9 (= S40), G17 (= G48), I21 (≠ A52), E41 (= E72), Y187 (= Y199), R205 (= R217), A206 (≠ G218), E208 (≠ D220), W209 (≠ L221), L235 (= L247), L236 (≠ A248)
- binding : S9 (= S40), T43 (≠ I74), D44 (= D75), R47 (= R78), V145 (≠ A157), R163 (≠ L174), Y168 (≠ V179), E172 (≠ A184), V177 (≠ I189), K180 (≠ R192), S181 (≠ R193), Y187 (= Y199), E207 (≠ A219), E208 (≠ D220), W209 (≠ L221), V211 (≠ T223), R237 (≠ C249), K241 (≠ G253)
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
32% identity, 77% coverage: 34:278/319 of query aligns to 3:266/468 of 2cv1A
- active site: K246 (= K258)
- binding adenosine-5'-triphosphate: P8 (= P39), S9 (= S40), G17 (= G48), T18 (≠ S49), I21 (≠ A52), R47 (= R78), A206 (≠ G218), W209 (≠ L221), L235 (= L247), L236 (≠ A248)
- binding (4s)-4-amino-5-hydroxypentanoic acid: R5 (= R36), A7 (= A38), E41 (= E72), Y187 (= Y199), R205 (= R217), W209 (≠ L221)
- binding : S9 (= S40), E41 (= E72), T43 (≠ I74), D44 (= D75), R47 (= R78), V145 (≠ A157), R163 (≠ L174), V166 (≠ I177), E172 (≠ A184), V177 (≠ I189), K180 (≠ R192), S181 (≠ R193), Y187 (= Y199), E207 (≠ A219), E208 (≠ D220), W209 (≠ L221), V211 (≠ T223), R237 (≠ C249), K241 (≠ G253), K243 (= K255)
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)
32% identity, 77% coverage: 34:278/319 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)
32% identity, 77% coverage: 34:278/319 of query aligns to 3:266/468 of 1n78A
- active site: K246 (= K258)
- binding glutamol-amp: R5 (= R36), A7 (= A38), P8 (= P39), S9 (= S40), G17 (= G48), T18 (≠ S49), I21 (≠ A52), E41 (= E72), Y187 (= Y199), N191 (≠ V203), R205 (= R217), A206 (≠ G218), E208 (≠ D220), W209 (≠ L221), L235 (= L247), L236 (≠ A248)
- binding : S9 (= S40), T43 (≠ I74), D44 (= D75), R47 (= R78), V145 (≠ A157), R163 (≠ L174), V166 (≠ I177), Y168 (≠ V179), E172 (≠ A184), V177 (≠ I189), K180 (≠ R192), S181 (≠ R193), Y187 (= Y199), E207 (≠ A219), E208 (≠ D220), W209 (≠ L221), L210 (= L222), V211 (≠ T223), R237 (≠ C249), K241 (≠ G253)
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)
32% identity, 77% coverage: 34:278/319 of query aligns to 3:266/468 of 1j09A
- active site: K246 (= K258)
- binding adenosine-5'-triphosphate: H15 (= H46), E208 (≠ D220), L235 (= L247), L236 (≠ A248), K243 (= K255), I244 (≠ L256), S245 (= S257), K246 (= K258), R247 (≠ Q259)
- binding glutamic acid: R5 (= R36), A7 (= A38), S9 (= S40), E41 (= E72), 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)
32% identity, 77% coverage: 34:278/319 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).
6brlA Crystal structure of a glutamate tRNA ligase from elizabethkingia meningosepticum ccug26117 in complex with its amino acid
29% identity, 86% coverage: 36:309/319 of query aligns to 6:332/502 of 6brlA
8vc5A Crystal structure of glutamyl-tRNA synthetase glurs from pseudomonas aeruginosa (zinc bound)
29% identity, 85% coverage: 36:307/319 of query aligns to 7:301/488 of 8vc5A
3aiiA Archaeal non-discriminating glutamyl-tRNA synthetase from methanothermobacter thermautotrophicus (see paper)
29% identity, 66% coverage: 34:244/319 of query aligns to 12:228/455 of 3aiiA
Sites not aligning to the query:
1o0cA Crystal structure of l-glutamate and ampcpp bound to glutamine aminoacyl tRNA synthetase (see paper)
32% identity, 33% coverage: 36:141/319 of query aligns to 23:128/529 of 1o0cA
- binding adenosine monophosphate: F24 (= F37), P26 (= P39), H33 (= H46), G35 (= G48), H36 (≠ S49), S39 (≠ A52)
- binding glutamic acid: R23 (= R36)
- binding : E27 (≠ S40), T61 (≠ I74), N62 (≠ D75), P119 (≠ R132), R123 (≠ Q136), R126 (≠ G139), T128 (= T141)
Sites not aligning to the query:
- binding adenosine monophosphate: 223, 253, 254, 263
- binding glutamic acid: 204, 208, 222
- binding : 6, 129, 130, 161, 174, 175, 176, 185, 187, 203, 204, 226, 227, 228, 231, 306, 309, 310, 311, 313, 314, 316, 318, 319, 322, 329, 334, 362, 392, 394, 395, 403, 405, 406, 435, 499, 501, 502, 527
Query Sequence
>5210702 FitnessBrowser__PV4:5210702
MSDIESVNKGFAVIPQADPSLSPDNPMQIDKPYVGRFAPSPSGPLHFGSLIAALGSYLRA
RAEQGQWLVRIEDIDPPREVKGASDLILKTLEAYGLHWDGAVLYQSSRLDDYQARLNSLL
AEDKAYYCQCTRKQIQAMGGTYDGRCAIRTAKHTAGAIRIRNTLAIDHFDDELLGPIRVE
PEFAAEDFIIKRRDGLYAYQLAVVMDDAFQGITEVVRGADLLTSSARQATLFNLFDDNAP
KWLHLPLACAEPGMKLSKQNHAPAIDLKAPQASINAALAFLGQAPCDIDSVKTMLAQAVS
QFELSRIPRQQEIILAPGA
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