SitesBLAST
Comparing WP_011444212.1 NCBI__GCF_000013325.1:WP_011444212.1 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)
35% identity, 86% coverage: 3:245/281 of query aligns to 17:248/308 of P27305
- E55 (= E41) binding L-glutamate
- Y182 (= Y179) binding L-glutamate
- R200 (= R197) binding L-glutamate
4a91A Crystal structure of the glutamyl-queuosine trnaasp synthetase from e. Coli complexed with l-glutamate (see paper)
35% identity, 86% coverage: 3:245/281 of query aligns to 5:234/290 of 4a91A
- active site: S11 (= S9), K229 (= K238)
- binding glutamic acid: R7 (= R5), A9 (= A7), S11 (= S9), E43 (= E41), Y170 (= Y179), R188 (= R197), L192 (= L201)
- binding zinc ion: C99 (= C96), C101 (= C98), Y113 (= Y117), C117 (= C121)
4g6zA Crystal structure of a glutamyl-tRNA synthetase glurs from burkholderia thailandensis bound to l-glutamate (see paper)
34% identity, 89% coverage: 4:252/281 of query aligns to 5:239/380 of 4g6zA
1g59A Glutamyl-tRNA synthetase complexed with tRNA(glu). (see paper)
35% identity, 87% coverage: 1:245/281 of query aligns to 1:253/468 of 1g59A
- binding : D44 (= D44), R45 (≠ G45), A46 (= A46), R47 (= R47), P109 (≠ R100), V145 (≠ Q140), R163 (≠ H155), V166 (≠ Q158), E172 (≠ M164), V177 (= V169), K180 (≠ R172), S181 (≠ K173), D182 (= D174), E207 (≠ V199), E208 (≠ D200), R237 (≠ V229), K241 (≠ G233), T242 (≠ R234), K243 (= K235)
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, 87% coverage: 1:245/281 of query aligns to 1:253/468 of 2cv2A
- active site: K246 (= K238)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R5 (= R5), A7 (= A7), S9 (= S9), G17 (= G17), I21 (≠ S21), E41 (= E41), Y187 (= Y179), R205 (= R197), A206 (≠ G198), E208 (≠ D200), W209 (≠ L201), L235 (≠ V227), L236 (= L228)
- binding : S9 (= S9), T43 (≠ I43), D44 (= D44), R47 (= R47), V145 (≠ Q140), R163 (≠ H155), Y168 (≠ A160), E172 (≠ M164), V177 (= V169), K180 (≠ R172), S181 (≠ K173), Y187 (= Y179), E207 (≠ V199), E208 (≠ D200), W209 (≠ L201), V211 (≠ R203), R237 (≠ V229), K241 (≠ G233)
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, 87% coverage: 1:245/281 of query aligns to 1:253/468 of 2cv1A
- active site: K246 (= K238)
- binding adenosine-5'-triphosphate: P8 (= P8), S9 (= S9), G17 (= G17), T18 (≠ H18), I21 (≠ S21), R47 (= R47), A206 (≠ G198), W209 (≠ L201), L235 (≠ V227), L236 (= L228)
- binding (4s)-4-amino-5-hydroxypentanoic acid: R5 (= R5), A7 (= A7), E41 (= E41), Y187 (= Y179), R205 (= R197), W209 (≠ L201)
- binding : S9 (= S9), E41 (= E41), T43 (≠ I43), D44 (= D44), R47 (= R47), V145 (≠ Q140), R163 (≠ H155), V166 (≠ Q158), E172 (≠ M164), V177 (= V169), K180 (≠ R172), S181 (≠ K173), Y187 (= Y179), E207 (≠ V199), E208 (≠ D200), W209 (≠ L201), V211 (≠ R203), R237 (≠ V229), K241 (≠ G233), K243 (= K235)
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, 87% coverage: 1:245/281 of query aligns to 1:253/468 of 2cuzA
1n78A Crystal structure of thermus thermophilus glutamyl-tRNA synthetase complexed with tRNA(glu) and glutamol-amp. (see paper)
34% identity, 87% coverage: 1:245/281 of query aligns to 1:253/468 of 1n78A
- active site: K246 (= K238)
- binding glutamol-amp: R5 (= R5), A7 (= A7), P8 (= P8), S9 (= S9), G17 (= G17), T18 (≠ H18), I21 (≠ S21), E41 (= E41), Y187 (= Y179), N191 (≠ A183), R205 (= R197), A206 (≠ G198), E208 (≠ D200), W209 (≠ L201), L235 (≠ V227), L236 (= L228)
- binding : S9 (= S9), T43 (≠ I43), D44 (= D44), R47 (= R47), V145 (≠ Q140), R163 (≠ H155), V166 (≠ Q158), Y168 (≠ A160), E172 (≠ M164), V177 (= V169), K180 (≠ R172), S181 (≠ K173), Y187 (= Y179), E207 (≠ V199), E208 (≠ D200), W209 (≠ L201), L210 (≠ F202), V211 (≠ R203), R237 (≠ V229), K241 (≠ G233)
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, 87% coverage: 1:245/281 of query aligns to 1:253/468 of 1j09A
- active site: K246 (= K238)
- binding adenosine-5'-triphosphate: H15 (= H15), E208 (≠ D200), L235 (≠ V227), L236 (= L228), K243 (= K235), I244 (≠ L236), S245 (≠ A237), K246 (= K238), R247 (= R239)
- binding glutamic acid: R5 (= R5), A7 (= A7), S9 (= S9), E41 (= E41), Y187 (= Y179), N191 (≠ A183), R205 (= R197), W209 (≠ L201)
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, 87% coverage: 1:245/281 of query aligns to 1:253/468 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).
P04805 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Escherichia coli (strain K12) (see 4 papers)
31% identity, 89% coverage: 4:252/281 of query aligns to 5:254/471 of P04805
- C98 (= C96) mutation to S: 10-fold decrease in activity. Strong decrease in zinc content.
- C100 (= C98) 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 (= C121) mutation to S: Loss of activity. Strong decrease in zinc content.
- H127 (≠ R123) mutation to Q: 10-fold decrease in activity. Strong decrease in zinc content.
- H129 (≠ G125) mutation to Q: No change in activity or in zinc content.
- H131 (≠ V127) mutation to Q: No change in activity or in zinc content.
- H132 (≠ P128) mutation to Q: No change in activity or in zinc content.
- C138 (≠ W134) mutation to S: No change in activity or in zinc content.
- S239 (≠ A237) 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)
35% identity, 92% coverage: 1:259/281 of query aligns to 1:272/485 of Q8DLI5
- R6 (= R5) binding L-glutamate
- Y192 (= Y179) binding L-glutamate
8i9iA Glutamyl-tRNA synthetase from escherichia coli bound to glutamate and zinc
31% identity, 89% coverage: 4:252/281 of query aligns to 5:254/468 of 8i9iA
2cfoA Non-discriminating glutamyl-tRNA synthetase from thermosynechococcus elongatus in complex with glu (see paper)
34% identity, 91% coverage: 4:259/281 of query aligns to 4:271/484 of 2cfoA
4griB Crystal structure of a glutamyl-tRNA synthetase glurs from borrelia burgdorferi bound to glutamic acid and zinc (see paper)
31% identity, 90% coverage: 2:255/281 of query aligns to 2:267/485 of 4griB
- active site: S9 (= S9), K253 (= K238)
- binding glutamic acid: R5 (= R5), A7 (= A7), S9 (= S9), E41 (= E41), Y194 (= Y179), R212 (= R197), W216 (≠ L201)
- binding zinc ion: C105 (= C96), C107 (= C98), Y128 (= Y117), C132 (= C121)
8vc5A Crystal structure of glutamyl-tRNA synthetase glurs from pseudomonas aeruginosa (zinc bound)
29% identity, 98% coverage: 4:278/281 of query aligns to 6:294/488 of 8vc5A
3al0C Crystal structure of the glutamine transamidosome from thermotoga maritima in the glutamylation state. (see paper)
28% identity, 91% coverage: 4:258/281 of query aligns to 105:355/564 of 3al0C
- active site: S110 (= S9), K335 (= K238)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R106 (= R5), A108 (= A7), P109 (= P8), G118 (= G17), T122 (≠ S21), E142 (= E41), Y276 (= Y179), R294 (= R197), G295 (= G198), D297 (= D200), H298 (≠ L201), L324 (≠ V227), I325 (≠ L228), L333 (= L236)
- binding : T144 (≠ I43), D145 (= D44), R148 (= R47), Y208 (= Y94), P213 (≠ T99), K252 (≠ H155), M255 (≠ Q158), I266 (≠ V169), K269 (≠ R172), S270 (≠ K173), Y276 (= Y179), D297 (= D200), H298 (≠ L201), L299 (≠ F202), S300 (≠ R203), N301 (≠ A204), K304 (≠ V207), R330 (≠ G233), P332 (≠ K235)
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
3aiiA Archaeal non-discriminating glutamyl-tRNA synthetase from methanothermobacter thermautotrophicus (see paper)
43% identity, 36% coverage: 2:103/281 of query aligns to 11:112/455 of 3aiiA
Sites not aligning to the query:
6brlA Crystal structure of a glutamate tRNA ligase from elizabethkingia meningosepticum ccug26117 in complex with its amino acid (see paper)
30% identity, 84% coverage: 4:239/281 of query aligns to 5:262/502 of 6brlA
4h3sA The structure of glutaminyl-tRNA synthetase from saccharomyces cerevisiae (see paper)
31% identity, 41% coverage: 4:117/281 of query aligns to 40:153/585 of 4h3sA
Sites not aligning to the query:
Query Sequence
>WP_011444212.1 NCBI__GCF_000013325.1:WP_011444212.1
MTVTRFAPSPNGPLHLGHAYSAIVAHDRAKRDNGEFLLRIEDIDGARSRPDLADEFRADL
QWLRLDYREVAPQSQRIASYRTAANELRAMGILYPCTCTRAEIAAAAVAQGPDGPLYPGT
CLRRGPVPGPDVAWRLDMEQATLIAGPLEWTDERHGVQQARPEMFGDVVLWRKDAPASYH
LAATLDDATDGITHVTRGVDLFRATHVHRLLQHLLGLPVPVWYHHPVLVEADGRKLAKRR
DAPALADRRRAGEDGRAVAAEVRATLFDTGISLSDTIDQSA
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