SitesBLAST
Comparing PP_4694 FitnessBrowser__Putida:PP_4694 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)
51% identity, 96% coverage: 6:294/300 of query aligns to 11:299/308 of P27305
- E55 (= E50) binding L-glutamate
- Y182 (= Y177) binding L-glutamate
- R200 (= R195) binding L-glutamate
4a91A Crystal structure of the glutamyl-queuosine trnaasp synthetase from e. Coli complexed with l-glutamate (see paper)
50% identity, 96% coverage: 8:294/300 of query aligns to 1:285/290 of 4a91A
- active site: S11 (≠ T18), K229 (= K236)
- binding glutamic acid: R7 (= R14), A9 (= A16), S11 (≠ T18), E43 (= E50), Y170 (= Y177), R188 (= R195), L192 (= L199)
- binding zinc ion: C99 (= C106), C101 (= C108), Y113 (= Y120), C117 (= C124)
8i9iA Glutamyl-tRNA synthetase from escherichia coli bound to glutamate and zinc
37% identity, 75% coverage: 14:238/300 of query aligns to 6:242/468 of 8i9iA
P04805 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Escherichia coli (strain K12) (see 4 papers)
37% identity, 75% coverage: 14:238/300 of query aligns to 6:242/471 of P04805
- C98 (= C106) mutation to S: 10-fold decrease in activity. Strong decrease in zinc content.
- C100 (= C108) 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 (= C124) mutation to S: Loss of activity. Strong decrease in zinc content.
- H127 (≠ N126) mutation to Q: 10-fold decrease in activity. Strong decrease in zinc content.
- H129 (vs. gap) mutation to Q: No change in activity or in zinc content.
- H131 (≠ G128) mutation to Q: No change in activity or in zinc content.
- H132 (= H129) mutation to Q: No change in activity or in zinc content.
- C138 (≠ A134) mutation to S: No change in activity or in zinc content.
- S239 (≠ G235) modified: Phosphoserine; mutation to D: Does not aminoacylate tRNA(Glu), not phosphorylated by HipA.
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, 74% coverage: 14:236/300 of query aligns to 6:251/485 of Q8DLI5
- R6 (= R14) binding L-glutamate
- Y192 (= Y177) binding L-glutamate
2cfoA Non-discriminating glutamyl-tRNA synthetase from thermosynechococcus elongatus in complex with glu (see paper)
37% identity, 74% coverage: 14:236/300 of query aligns to 5:250/484 of 2cfoA
4g6zA Crystal structure of a glutamyl-tRNA synthetase glurs from burkholderia thailandensis bound to l-glutamate (see paper)
35% identity, 75% coverage: 14:238/300 of query aligns to 6:227/380 of 4g6zA
3al0C Crystal structure of the glutamine transamidosome from thermotoga maritima in the glutamylation state. (see paper)
32% identity, 81% coverage: 14:256/300 of query aligns to 106:355/564 of 3al0C
- active site: S110 (≠ T18), K335 (= K236)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R106 (= R14), A108 (= A16), P109 (= P17), G118 (= G26), T122 (≠ A30), E142 (= E50), Y276 (= Y177), R294 (= R195), G295 (= G196), D297 (= D198), H298 (≠ L199), L324 (= L225), I325 (= I226), L333 (= L234)
- binding : T144 (= T52), D145 (= D53), R148 (= R56), Y208 (≠ C108), P213 (vs. gap), K252 (≠ Q152), M255 (≠ Q156), I266 (≠ V167), K269 (≠ R170), S270 (≠ R171), Y276 (= Y177), D297 (= D198), H298 (≠ L199), L299 (= L200), S300 (≠ D201), N301 (= N202), K304 (≠ R205), R330 (≠ G231), P332 (≠ K233)
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: 12:257/300 of query aligns to 3:267/468 of 1g59A
- binding : D44 (= D53), R45 (≠ P54), A46 (≠ P55), R47 (= R56), P109 (≠ R110), V145 (≠ A135), R163 (≠ Q152), V166 (≠ Q156), E172 (= E162), V177 (= V167), K180 (≠ R170), S181 (≠ R171), D182 (= D172), E207 (≠ A197), E208 (≠ D198), R237 (≠ V227), K241 (≠ G231), T242 (≠ H232), K243 (= K233)
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)
34% identity, 82% coverage: 12:257/300 of query aligns to 3:267/468 of 2cv2A
- active site: K246 (= K236)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R5 (= R14), A7 (= A16), S9 (≠ T18), G17 (= G26), I21 (≠ A30), E41 (= E50), Y187 (= Y177), R205 (= R195), A206 (≠ G196), E208 (≠ D198), W209 (≠ L199), L235 (= L225), L236 (≠ I226)
- binding : S9 (≠ T18), T43 (= T52), D44 (= D53), R47 (= R56), V145 (≠ A135), R163 (≠ Q152), Y168 (≠ H158), E172 (= E162), V177 (= V167), K180 (≠ R170), S181 (≠ R171), Y187 (= Y177), E207 (≠ A197), E208 (≠ D198), W209 (≠ L199), V211 (≠ D201), R237 (≠ V227), K241 (≠ G231)
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
34% identity, 82% coverage: 12:257/300 of query aligns to 3:267/468 of 2cv1A
- active site: K246 (= K236)
- binding adenosine-5'-triphosphate: P8 (= P17), S9 (≠ T18), G17 (= G26), T18 (≠ S27), I21 (≠ A30), R47 (= R56), A206 (≠ G196), W209 (≠ L199), L235 (= L225), L236 (≠ I226)
- binding (4s)-4-amino-5-hydroxypentanoic acid: R5 (= R14), A7 (= A16), E41 (= E50), Y187 (= Y177), R205 (= R195), W209 (≠ L199)
- binding : S9 (≠ T18), E41 (= E50), T43 (= T52), D44 (= D53), R47 (= R56), V145 (≠ A135), R163 (≠ Q152), V166 (≠ Q156), E172 (= E162), V177 (= V167), K180 (≠ R170), S181 (≠ R171), Y187 (= Y177), E207 (≠ A197), E208 (≠ D198), W209 (≠ L199), V211 (≠ D201), R237 (≠ V227), K241 (≠ G231), K243 (= K233)
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)
34% identity, 82% coverage: 12:257/300 of query aligns to 3:267/468 of 2cuzA
1n78A Crystal structure of thermus thermophilus glutamyl-tRNA synthetase complexed with tRNA(glu) and glutamol-amp. (see paper)
34% identity, 82% coverage: 12:257/300 of query aligns to 3:267/468 of 1n78A
- active site: K246 (= K236)
- binding glutamol-amp: R5 (= R14), A7 (= A16), P8 (= P17), S9 (≠ T18), G17 (= G26), T18 (≠ S27), I21 (≠ A30), E41 (= E50), Y187 (= Y177), N191 (≠ V181), R205 (= R195), A206 (≠ G196), E208 (≠ D198), W209 (≠ L199), L235 (= L225), L236 (≠ I226)
- binding : S9 (≠ T18), T43 (= T52), D44 (= D53), R47 (= R56), V145 (≠ A135), R163 (≠ Q152), V166 (≠ Q156), Y168 (≠ H158), E172 (= E162), V177 (= V167), K180 (≠ R170), S181 (≠ R171), Y187 (= Y177), E207 (≠ A197), E208 (≠ D198), W209 (≠ L199), L210 (= L200), V211 (≠ D201), R237 (≠ V227), K241 (≠ G231)
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)
34% identity, 82% coverage: 12:257/300 of query aligns to 3:267/468 of 1j09A
- active site: K246 (= K236)
- binding adenosine-5'-triphosphate: H15 (= H24), E208 (≠ D198), L235 (= L225), L236 (≠ I226), K243 (= K233), I244 (≠ L234), S245 (≠ G235), K246 (= K236), R247 (≠ S237)
- binding glutamic acid: R5 (= R14), A7 (= A16), S9 (≠ T18), E41 (= E50), Y187 (= Y177), N191 (≠ V181), R205 (= R195), W209 (≠ L199)
P27000 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
34% identity, 82% coverage: 12:257/300 of query aligns to 3:267/468 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).
4griB Crystal structure of a glutamyl-tRNA synthetase glurs from borrelia burgdorferi bound to glutamic acid and zinc (see paper)
32% identity, 77% coverage: 14:244/300 of query aligns to 5:261/485 of 4griB
- active site: S9 (≠ T18), K253 (= K236)
- binding glutamic acid: R5 (= R14), A7 (= A16), S9 (≠ T18), E41 (= E50), Y194 (= Y177), R212 (= R195), W216 (≠ L199)
- binding zinc ion: C105 (= C106), C107 (= C108), Y128 (≠ F123), C132 (= C124)
8vc5A Crystal structure of glutamyl-tRNA synthetase glurs from pseudomonas aeruginosa (zinc bound)
31% identity, 74% coverage: 14:236/300 of query aligns to 7:254/488 of 8vc5A
6brlA Crystal structure of a glutamate tRNA ligase from elizabethkingia meningosepticum ccug26117 in complex with its amino acid (see paper)
27% identity, 74% coverage: 14:236/300 of query aligns to 6:261/502 of 6brlA
3aiiA Archaeal non-discriminating glutamyl-tRNA synthetase from methanothermobacter thermautotrophicus (see paper)
33% identity, 73% coverage: 3:222/300 of query aligns to 3:228/455 of 3aiiA
Sites not aligning to the query:
2re8A Glutaminyl-tRNA synthetase mutant c229r with bound analog 5'-o-[n-(l- glutamyl)-sulfamoyl]adenosine (see paper)
26% identity, 65% coverage: 14:208/300 of query aligns to 23:233/529 of 2re8A
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: P25 (≠ A16), P26 (= P17), E27 (≠ T18), G35 (= G26), H36 (≠ S27), D59 (≠ E50), Y204 (= Y177), H208 (≠ V181), R222 (= R195), T223 (≠ G196)
- binding : E27 (≠ T18), T61 (= T52), N62 (≠ D53), L117 (≠ C108), P119 (≠ R110), R123 (≠ E114), R126 (≠ N117), T128 (≠ I119), L129 (≠ Y120), G161 (= G133), P174 (= P141), F175 (≠ E142), I176 (≠ L143), V182 (≠ D149), R185 (≠ Q152), M203 (≠ A176), Y204 (= Y177), F226 (≠ L199), D228 (= D201)
Sites not aligning to the query:
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: 253, 254, 263
- binding : 6, 306, 309, 310, 311, 313, 314, 316, 319, 322, 329, 334, 362, 363, 392, 394, 395, 403, 405, 406, 435, 499, 501, 502, 527
Query Sequence
>PP_4694 FitnessBrowser__Putida:PP_4694
MPSLTMTDSSYIGRFAPTPSGFLHFGSLVAALASWLDARAVNGRWLLRMEDTDPPREMPG
ARDAILQTLERYGLHWDGEVVFQSQRHDAYAAVVDRLFNMGLAYACTCSRKQLESYNGIY
PGFCRNAGHAREGAAIRLRVPELIYRFTDRVQGEYQQHLGREVGDFVIQRRDGLYAYQLA
VVLDDAWQGVTDIVRGADLLDNTPRQLYLQELLGFSQPRYLHIPLIVQPDGHKLGKSYRS
PPLQAEHATPLLLRALRALGQETDPELLLATPAEVLAVARAQWRPEAIAQRTTVPEADLR
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