SitesBLAST
Comparing WP_057508000.1 NCBI__GCF_001431535.1:WP_057508000.1 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)
46% identity, 96% coverage: 1:283/296 of query aligns to 11:294/308 of P27305
- E55 (= E45) binding
- Y182 (= Y171) binding
- R200 (= R189) binding
4a91A Crystal structure of the glutamyl-queuosine trnaasp synthetase from e. Coli complexed with l-glutamate (see paper)
46% identity, 94% coverage: 6:283/296 of query aligns to 4:280/290 of 4a91A
- active site: S11 (= S13), K229 (= K230)
- binding glutamic acid: R7 (= R9), A9 (= A11), S11 (= S13), E43 (= E45), Y170 (= Y171), R188 (= R189), L192 (= L193)
- binding zinc ion: C99 (= C101), C101 (= C103), Y113 (≠ H115), C117 (≠ Q117)
P04805 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Escherichia coli (strain K12) (see 4 papers)
39% identity, 82% coverage: 9:252/296 of query aligns to 6:267/471 of P04805
- C98 (= C101) mutation to S: 10-fold decrease in activity. Strong decrease in zinc content.
- C100 (= C103) 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 (≠ I114) mutation to S: Loss of activity. Strong decrease in zinc content.
- H127 (= H116) 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 (vs. gap) mutation to Q: No change in activity or in zinc content.
- H132 (vs. gap) mutation to Q: No change in activity or in zinc content.
- C138 (= C118) mutation to S: No change in activity or in zinc content.
- S239 (= S229) 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
39% identity, 82% coverage: 9:252/296 of query aligns to 6:267/468 of 8i9iA
2cfoA Non-discriminating glutamyl-tRNA synthetase from thermosynechococcus elongatus in complex with glu (see paper)
37% identity, 80% coverage: 9:246/296 of query aligns to 5:266/484 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)
37% identity, 80% coverage: 9:246/296 of query aligns to 6:267/485 of Q8DLI5
- R6 (= R9) binding
- Y192 (= Y171) binding
4g6zA Crystal structure of a glutamyl-tRNA synthetase glurs from burkholderia thailandensis bound to l-glutamate (see paper)
37% identity, 82% coverage: 9:252/296 of query aligns to 6:252/380 of 4g6zA
3al0C Crystal structure of the glutamine transamidosome from thermotoga maritima in the glutamylation state. (see paper)
34% identity, 78% coverage: 9:238/296 of query aligns to 106:343/564 of 3al0C
- active site: S110 (= S13), K335 (= K230)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R106 (= R9), A108 (= A11), P109 (= P12), G118 (= G21), T122 (≠ A25), E142 (= E45), Y276 (= Y171), R294 (= R189), G295 (= G190), D297 (= D192), H298 (≠ L193), L324 (= L219), I325 (≠ L220), L333 (= L228)
- binding : T144 (≠ V47), D145 (= D48), R148 (= R51), Y208 (≠ C103), P213 (vs. gap), K252 (≠ R146), M255 (≠ Q149), I266 (≠ V161), K269 (≠ R164), S270 (≠ A165), Y276 (= Y171), D297 (= D192), H298 (≠ L193), L299 (= L194), S300 (≠ D195), N301 (≠ S196), K304 (≠ R199), R330 (≠ G225), P332 (≠ K227)
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
6brlA Crystal structure of a glutamate tRNA ligase from elizabethkingia meningosepticum ccug26117 in complex with its amino acid
32% identity, 75% coverage: 9:230/296 of query aligns to 6:261/502 of 6brlA
1g59A Glutamyl-tRNA synthetase complexed with tRNA(glu). (see paper)
37% identity, 78% coverage: 9:238/296 of query aligns to 5:254/468 of 1g59A
- binding : D44 (= D48), R45 (≠ P49), A46 (≠ P50), R47 (= R51), P109 (≠ R105), V145 (≠ A128), R163 (= R146), V166 (≠ Q149), E172 (≠ D156), V177 (= V161), K180 (≠ R164), S181 (≠ A165), D182 (= D166), E207 (≠ A191), E208 (≠ D192), R237 (≠ L221), K241 (≠ G225), T242 (≠ R226), K243 (= K227)
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)
37% identity, 78% coverage: 9:238/296 of query aligns to 5:254/468 of 2cv2A
- active site: K246 (= K230)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R5 (= R9), A7 (= A11), S9 (= S13), G17 (= G21), I21 (≠ A25), E41 (= E45), Y187 (= Y171), R205 (= R189), A206 (≠ G190), E208 (≠ D192), W209 (≠ L193), L235 (= L219), L236 (= L220)
- binding : S9 (= S13), T43 (≠ V47), D44 (= D48), R47 (= R51), V145 (≠ A128), R163 (= R146), Y168 (≠ Q151), E172 (≠ D156), V177 (= V161), K180 (≠ R164), S181 (≠ A165), Y187 (= Y171), E207 (≠ A191), E208 (≠ D192), W209 (≠ L193), V211 (≠ D195), R237 (≠ L221), K241 (≠ G225)
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
37% identity, 78% coverage: 9:238/296 of query aligns to 5:254/468 of 2cv1A
- active site: K246 (= K230)
- binding adenosine-5'-triphosphate: P8 (= P12), S9 (= S13), G17 (= G21), T18 (≠ S22), I21 (≠ A25), R47 (= R51), A206 (≠ G190), W209 (≠ L193), L235 (= L219), L236 (= L220)
- binding (4s)-4-amino-5-hydroxypentanoic acid: R5 (= R9), A7 (= A11), E41 (= E45), Y187 (= Y171), R205 (= R189), W209 (≠ L193)
- binding : S9 (= S13), E41 (= E45), T43 (≠ V47), D44 (= D48), R47 (= R51), V145 (≠ A128), R163 (= R146), V166 (≠ Q149), E172 (≠ D156), V177 (= V161), K180 (≠ R164), S181 (≠ A165), Y187 (= Y171), E207 (≠ A191), E208 (≠ D192), W209 (≠ L193), V211 (≠ D195), R237 (≠ L221), K241 (≠ G225), K243 (= K227)
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)
37% identity, 78% coverage: 9:238/296 of query aligns to 5:254/468 of 2cuzA
1n78A Crystal structure of thermus thermophilus glutamyl-tRNA synthetase complexed with tRNA(glu) and glutamol-amp. (see paper)
37% identity, 78% coverage: 9:238/296 of query aligns to 5:254/468 of 1n78A
- active site: K246 (= K230)
- binding glutamol-amp: R5 (= R9), A7 (= A11), P8 (= P12), S9 (= S13), G17 (= G21), T18 (≠ S22), I21 (≠ A25), E41 (= E45), Y187 (= Y171), N191 (≠ V175), R205 (= R189), A206 (≠ G190), E208 (≠ D192), W209 (≠ L193), L235 (= L219), L236 (= L220)
- binding : S9 (= S13), T43 (≠ V47), D44 (= D48), R47 (= R51), V145 (≠ A128), R163 (= R146), V166 (≠ Q149), Y168 (≠ Q151), E172 (≠ D156), V177 (= V161), K180 (≠ R164), S181 (≠ A165), Y187 (= Y171), E207 (≠ A191), E208 (≠ D192), W209 (≠ L193), L210 (= L194), V211 (≠ D195), R237 (≠ L221), K241 (≠ G225)
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)
37% identity, 78% coverage: 9:238/296 of query aligns to 5:254/468 of 1j09A
- active site: K246 (= K230)
- binding adenosine-5'-triphosphate: H15 (= H19), E208 (≠ D192), L235 (= L219), L236 (= L220), K243 (= K227), I244 (≠ L228), S245 (= S229), K246 (= K230), R247 (≠ S231)
- binding glutamic acid: R5 (= R9), A7 (= A11), S9 (= S13), E41 (= E45), Y187 (= Y171), N191 (≠ V175), R205 (= R189), W209 (≠ L193)
P27000 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
37% identity, 78% coverage: 9:238/296 of query aligns to 5:254/468 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).
4griB Crystal structure of a glutamyl-tRNA synthetase glurs from borrelia burgdorferi bound to glutamic acid and zinc (see paper)
30% identity, 94% coverage: 9:286/296 of query aligns to 5:321/485 of 4griB
- active site: S9 (= S13), K253 (= K230)
- binding glutamic acid: R5 (= R9), A7 (= A11), S9 (= S13), E41 (= E45), Y194 (= Y171), R212 (= R189), W216 (≠ L193)
- binding zinc ion: C105 (= C101), C107 (= C103), Y128 (vs. gap), C132 (≠ H116)
8vc5A Crystal structure of glutamyl-tRNA synthetase glurs from pseudomonas aeruginosa (zinc bound)
32% identity, 93% coverage: 9:284/296 of query aligns to 7:303/488 of 8vc5A
3aiiA Archaeal non-discriminating glutamyl-tRNA synthetase from methanothermobacter thermautotrophicus (see paper)
29% identity, 74% coverage: 9:227/296 of query aligns to 14:239/455 of 3aiiA
4h3sA The structure of glutaminyl-tRNA synthetase from saccharomyces cerevisiae (see paper)
29% identity, 36% coverage: 9:114/296 of query aligns to 41:145/585 of 4h3sA
Sites not aligning to the query:
Query Sequence
>WP_057508000.1 NCBI__GCF_001431535.1:WP_057508000.1
MTSPIHCGRFAPSPTGPLHAGSLLAAFASWLFAHHQGGRWLLRVEDVDPPRTVPGAAQSQ
LDLLHYLGLQPDGPVLWQSRRSDVYQHALDALLASGRAFACHCSRSELAASGGIHHQCVA
RQARPDPAIRLRVAPGSVVTFDDALRGPQRQDVHADVGDFVLRRADGCWAYQLAVVVDDA
AQGITDVVRGADLLDSTARQILLQRALGLPTPRYAHLPLLLAGDGRKLSKSEAAPTVDGG
DPMAVLRQLWRLLGQPAAALAGASTQADLLQRAAAAFDRTRVPLHDISSRQAHSGP
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