SitesBLAST
Comparing WP_019865507.1 NCBI__GCF_000384075.1:WP_019865507.1 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, 97% coverage: 1:283/292 of query aligns to 11:293/308 of P27305
- E55 (≠ D46) binding L-glutamate
- Y182 (= Y172) binding L-glutamate
- R200 (= R190) binding L-glutamate
4a91A Crystal structure of the glutamyl-queuosine trnaasp synthetase from e. Coli complexed with l-glutamate (see paper)
43% identity, 95% coverage: 8:283/292 of query aligns to 5:279/290 of 4a91A
- active site: S11 (= S14), K229 (= K231)
- binding glutamic acid: R7 (= R10), A9 (= A12), S11 (= S14), E43 (≠ D46), Y170 (= Y172), R188 (= R190), L192 (= L194)
- binding zinc ion: C99 (= C102), C101 (= C104), Y113 (= Y114), C117 (= C118)
8i9iA Glutamyl-tRNA synthetase from escherichia coli bound to glutamate and zinc
36% identity, 85% coverage: 7:253/292 of query aligns to 3:267/468 of 8i9iA
P04805 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Escherichia coli (strain K12) (see 4 papers)
36% identity, 85% coverage: 7:253/292 of query aligns to 3:267/471 of P04805
- C98 (= C102) mutation to S: 10-fold decrease in activity. Strong decrease in zinc content.
- C100 (= C104) 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 (= C118) 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 (≠ N120) mutation to Q: No change in activity or in zinc content.
- H131 (≠ D122) mutation to Q: No change in activity or in zinc content.
- H132 (≠ I123) mutation to Q: No change in activity or in zinc content.
- C138 (≠ H129) mutation to S: No change in activity or in zinc content.
- S239 (= S230) modified: Phosphoserine; mutation to D: Does not aminoacylate tRNA(Glu), not phosphorylated by HipA.
3al0C Crystal structure of the glutamine transamidosome from thermotoga maritima in the glutamylation state. (see paper)
33% identity, 84% coverage: 10:254/292 of query aligns to 106:362/564 of 3al0C
- active site: S110 (= S14), K335 (= K231)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R106 (= R10), A108 (= A12), P109 (= P13), G118 (= G22), T122 (= T26), E142 (≠ D46), Y276 (= Y172), R294 (= R190), G295 (= G191), D297 (= D193), H298 (≠ L194), L324 (≠ V220), I325 (= I221), L333 (= L229)
- binding : T144 (≠ L48), D145 (= D49), R148 (= R52), Y208 (vs. gap), P213 (≠ C104), K252 (≠ Q147), M255 (≠ I150), I266 (= I162), K269 (≠ R165), S270 (≠ K166), Y276 (= Y172), D297 (= D193), H298 (≠ L194), L299 (= L195), S300 (≠ T196), N301 (≠ S197), K304 (= K200), R330 (≠ G226), P332 (≠ K228)
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
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)
31% identity, 91% coverage: 6:271/292 of query aligns to 2:290/485 of Q8DLI5
- R6 (= R10) binding L-glutamate
- Y192 (= Y172) binding L-glutamate
2cfoA Non-discriminating glutamyl-tRNA synthetase from thermosynechococcus elongatus in complex with glu (see paper)
31% identity, 91% coverage: 6:271/292 of query aligns to 1:289/484 of 2cfoA
4g6zA Crystal structure of a glutamyl-tRNA synthetase glurs from burkholderia thailandensis bound to l-glutamate (see paper)
33% identity, 78% coverage: 10:238/292 of query aligns to 6:232/380 of 4g6zA
1g59A Glutamyl-tRNA synthetase complexed with tRNA(glu). (see paper)
31% identity, 80% coverage: 7:239/292 of query aligns to 2:254/468 of 1g59A
- binding : D44 (= D49), R45 (≠ T50), A46 (≠ P51), R47 (= R52), P109 (≠ R106), V145 (≠ A130), R163 (≠ Q147), V166 (≠ I150), E172 (≠ Q153), V177 (≠ I162), K180 (≠ R165), S181 (≠ K166), D182 (= D167), E207 (≠ C192), E208 (≠ D193), R237 (≠ I222), K241 (≠ G226), T242 (≠ Y227), K243 (= K228)
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
4griB Crystal structure of a glutamyl-tRNA synthetase glurs from borrelia burgdorferi bound to glutamic acid and zinc (see paper)
31% identity, 82% coverage: 10:247/292 of query aligns to 5:274/485 of 4griB
- active site: S9 (= S14), K253 (= K231)
- binding glutamic acid: R5 (= R10), A7 (= A12), S9 (= S14), E41 (≠ D46), Y194 (= Y172), R212 (= R190), W216 (≠ L194)
- binding zinc ion: C105 (= C102), C107 (= C104), Y128 (= Y114), C132 (= C118)
2cv2A Glutamyl-tRNA synthetase from thermus thermophilus in complex with tRNA(glu) and an enzyme inhibitor, glu-ams (see paper)
31% identity, 80% coverage: 7:239/292 of query aligns to 2:254/468 of 2cv2A
- active site: K246 (= K231)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R5 (= R10), A7 (= A12), S9 (= S14), G17 (= G22), I21 (≠ T26), E41 (≠ D46), Y187 (= Y172), R205 (= R190), A206 (≠ G191), E208 (≠ D193), W209 (≠ L194), L235 (≠ V220), L236 (≠ I221)
- binding : S9 (= S14), T43 (≠ L48), D44 (= D49), R47 (= R52), V145 (≠ A130), R163 (≠ Q147), Y168 (vs. gap), E172 (≠ Q153), V177 (≠ I162), K180 (≠ R165), S181 (≠ K166), Y187 (= Y172), E207 (≠ C192), E208 (≠ D193), W209 (≠ L194), V211 (≠ T196), R237 (≠ I222), K241 (≠ G226)
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
31% identity, 80% coverage: 7:239/292 of query aligns to 2:254/468 of 2cv1A
- active site: K246 (= K231)
- binding adenosine-5'-triphosphate: P8 (= P13), S9 (= S14), G17 (= G22), T18 (≠ S23), I21 (≠ T26), R47 (= R52), A206 (≠ G191), W209 (≠ L194), L235 (≠ V220), L236 (≠ I221)
- binding (4s)-4-amino-5-hydroxypentanoic acid: R5 (= R10), A7 (= A12), E41 (≠ D46), Y187 (= Y172), R205 (= R190), W209 (≠ L194)
- binding : S9 (= S14), E41 (≠ D46), T43 (≠ L48), D44 (= D49), R47 (= R52), V145 (≠ A130), R163 (≠ Q147), V166 (≠ I150), E172 (≠ Q153), V177 (≠ I162), K180 (≠ R165), S181 (≠ K166), Y187 (= Y172), E207 (≠ C192), E208 (≠ D193), W209 (≠ L194), V211 (≠ T196), R237 (≠ I222), K241 (≠ G226), K243 (= K228)
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)
31% identity, 80% coverage: 7:239/292 of query aligns to 2:254/468 of 2cuzA
1n78A Crystal structure of thermus thermophilus glutamyl-tRNA synthetase complexed with tRNA(glu) and glutamol-amp. (see paper)
31% identity, 80% coverage: 7:239/292 of query aligns to 2:254/468 of 1n78A
- active site: K246 (= K231)
- binding glutamol-amp: R5 (= R10), A7 (= A12), P8 (= P13), S9 (= S14), G17 (= G22), T18 (≠ S23), I21 (≠ T26), E41 (≠ D46), Y187 (= Y172), N191 (≠ V176), R205 (= R190), A206 (≠ G191), E208 (≠ D193), W209 (≠ L194), L235 (≠ V220), L236 (≠ I221)
- binding : S9 (= S14), T43 (≠ L48), D44 (= D49), R47 (= R52), V145 (≠ A130), R163 (≠ Q147), V166 (≠ I150), Y168 (vs. gap), E172 (≠ Q153), V177 (≠ I162), K180 (≠ R165), S181 (≠ K166), Y187 (= Y172), E207 (≠ C192), E208 (≠ D193), W209 (≠ L194), L210 (= L195), V211 (≠ T196), R237 (≠ I222), K241 (≠ G226)
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)
31% identity, 80% coverage: 7:239/292 of query aligns to 2:254/468 of 1j09A
- active site: K246 (= K231)
- binding adenosine-5'-triphosphate: H15 (= H20), E208 (≠ D193), L235 (≠ V220), L236 (≠ I221), K243 (= K228), I244 (≠ L229), S245 (= S230), K246 (= K231), R247 (≠ Q232)
- binding glutamic acid: R5 (= R10), A7 (= A12), S9 (= S14), E41 (≠ D46), Y187 (= Y172), N191 (≠ V176), R205 (= R190), W209 (≠ L194)
P27000 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
31% identity, 80% coverage: 7:239/292 of query aligns to 2:254/468 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 (see paper)
29% identity, 76% coverage: 10:232/292 of query aligns to 6:262/502 of 6brlA
8vc5A Crystal structure of glutamyl-tRNA synthetase glurs from pseudomonas aeruginosa (zinc bound)
27% identity, 80% coverage: 6:238/292 of query aligns to 3:261/488 of 8vc5A
3aiiA Archaeal non-discriminating glutamyl-tRNA synthetase from methanothermobacter thermautotrophicus (see paper)
28% identity, 73% coverage: 4:217/292 of query aligns to 8:228/455 of 3aiiA
Sites not aligning to the query:
1o0cA Crystal structure of l-glutamate and ampcpp bound to glutamine aminoacyl tRNA synthetase (see paper)
36% identity, 28% coverage: 6:86/292 of query aligns to 19:102/529 of 1o0cA
Sites not aligning to the query:
- binding adenosine monophosphate: 223, 253, 254, 263
- binding glutamic acid: 204, 208, 222
- binding : 6, 119, 123, 126, 128, 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
>WP_019865507.1 NCBI__GCF_000384075.1:WP_019865507.1
MPDKQTIIGRFAPSPTGPLHLGSLYTALASFLQARSQQGRWLLRLDDLDTPRNRPGSVTS
ILNTLDSLSLHWDGEVAYQSQQLSVYRDILNQLIQNQYLYRCDCSRKLLASDSYSGRCRN
RDISPDTPHALRIKTGIREIAFDDYLQGPINEQLNGPHSDFIVKRKDGIIAYQFAVVIDD
YLQQVNEIVRGCDLLTSTPKQIYLQQLLGYPTPRYLHVPVIIDHDGYKLSKQTLATAVDT
SIPSAVIFGLLVLLKQQPPLELKAASVGELLAWGISHWNPAALRNQQSLAIV
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