SitesBLAST
Comparing GFF971 FitnessBrowser__psRCH2:GFF971 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)
50% identity, 94% coverage: 11:292/301 of query aligns to 15:296/308 of P27305
- E55 (= E51) binding
- Y182 (= Y178) binding
- R200 (= R196) binding
4a91A Crystal structure of the glutamyl-queuosine trnaasp synthetase from e. Coli complexed with l-glutamate (see paper)
50% identity, 94% coverage: 11:292/301 of query aligns to 3:282/290 of 4a91A
- active site: S11 (≠ T19), K229 (= K237)
- binding glutamic acid: R7 (= R15), A9 (= A17), S11 (≠ T19), E43 (= E51), Y170 (= Y178), R188 (= R196), L192 (= L200)
- binding zinc ion: C99 (= C107), C101 (= C109), Y113 (= Y121), C117 (= C125)
8i9iA Glutamyl-tRNA synthetase from escherichia coli bound to glutamate and zinc
37% identity, 75% coverage: 15:239/301 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: 15:239/301 of query aligns to 6:242/471 of P04805
- C98 (= C107) mutation to S: 10-fold decrease in activity. Strong decrease in zinc content.
- C100 (= C109) 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 (= C125) 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 (≠ A128) mutation to Q: No change in activity or in zinc content.
- H131 (≠ N130) mutation to Q: No change in activity or in zinc content.
- H132 (≠ G131) mutation to Q: No change in activity or in zinc content.
- C138 (≠ I137) mutation to S: No change in activity or in zinc content.
- S239 (≠ G236) 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)
33% identity, 92% coverage: 15:291/301 of query aligns to 6:306/485 of Q8DLI5
- R6 (= R15) binding
- Y192 (= Y178) binding
2cfoA Non-discriminating glutamyl-tRNA synthetase from thermosynechococcus elongatus in complex with glu (see paper)
33% identity, 92% coverage: 15:291/301 of query aligns to 5:305/484 of 2cfoA
3al0C Crystal structure of the glutamine transamidosome from thermotoga maritima in the glutamylation state. (see paper)
31% identity, 81% coverage: 15:257/301 of query aligns to 106:355/564 of 3al0C
- active site: S110 (≠ T19), K335 (= K237)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R106 (= R15), A108 (= A17), P109 (= P18), G118 (= G27), T122 (≠ A31), E142 (= E51), Y276 (= Y178), R294 (= R196), G295 (= G197), D297 (= D199), H298 (≠ L200), L324 (= L226), I325 (= I227), L333 (= L235)
- binding : T144 (≠ I53), D145 (= D54), R148 (= R57), Y208 (≠ C109), P213 (vs. gap), K252 (≠ Q153), M255 (≠ R157), I266 (≠ V168), K269 (≠ R171), S270 (≠ R172), Y276 (= Y178), D297 (= D199), H298 (≠ L200), L299 (= L201), S300 (≠ D202), N301 (≠ S203), K304 (≠ R206), R330 (≠ G232), P332 (≠ K234)
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)
33% identity, 82% coverage: 13:258/301 of query aligns to 3:267/468 of 1g59A
- binding : D44 (= D54), R45 (≠ P55), A46 (≠ P56), R47 (= R57), P109 (≠ R111), V145 (vs. gap), R163 (= R157), V166 (≠ L160), E172 (= E163), V177 (= V168), K180 (≠ R171), S181 (≠ R172), D182 (= D173), E207 (≠ A198), E208 (≠ D199), R237 (≠ I228), K241 (≠ G232), T242 (≠ H233), K243 (= K234)
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)
33% identity, 82% coverage: 13:258/301 of query aligns to 3:267/468 of 2cv2A
- active site: K246 (= K237)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R5 (= R15), A7 (= A17), S9 (≠ T19), G17 (= G27), I21 (≠ A31), E41 (= E51), Y187 (= Y178), R205 (= R196), A206 (≠ G197), E208 (≠ D199), W209 (≠ L200), L235 (= L226), L236 (≠ I227)
- binding : S9 (≠ T19), T43 (≠ I53), D44 (= D54), R47 (= R57), V145 (vs. gap), R163 (= R157), Y168 (vs. gap), E172 (= E163), V177 (= V168), K180 (≠ R171), S181 (≠ R172), Y187 (= Y178), E207 (≠ A198), E208 (≠ D199), W209 (≠ L200), V211 (≠ D202), R237 (≠ I228), K241 (≠ G232)
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
33% identity, 82% coverage: 13:258/301 of query aligns to 3:267/468 of 2cv1A
- active site: K246 (= K237)
- binding adenosine-5'-triphosphate: P8 (= P18), S9 (≠ T19), G17 (= G27), T18 (≠ S28), I21 (≠ A31), R47 (= R57), A206 (≠ G197), W209 (≠ L200), L235 (= L226), L236 (≠ I227)
- binding (4s)-4-amino-5-hydroxypentanoic acid: R5 (= R15), A7 (= A17), E41 (= E51), Y187 (= Y178), R205 (= R196), W209 (≠ L200)
- binding : S9 (≠ T19), E41 (= E51), T43 (≠ I53), D44 (= D54), R47 (= R57), V145 (vs. gap), R163 (= R157), V166 (≠ L160), E172 (= E163), V177 (= V168), K180 (≠ R171), S181 (≠ R172), Y187 (= Y178), E207 (≠ A198), E208 (≠ D199), W209 (≠ L200), V211 (≠ D202), R237 (≠ I228), K241 (≠ G232), K243 (= K234)
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)
33% identity, 82% coverage: 13:258/301 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)
33% identity, 82% coverage: 13:258/301 of query aligns to 3:267/468 of 1n78A
- active site: K246 (= K237)
- binding glutamol-amp: R5 (= R15), A7 (= A17), P8 (= P18), S9 (≠ T19), G17 (= G27), T18 (≠ S28), I21 (≠ A31), E41 (= E51), Y187 (= Y178), N191 (≠ V182), R205 (= R196), A206 (≠ G197), E208 (≠ D199), W209 (≠ L200), L235 (= L226), L236 (≠ I227)
- binding : S9 (≠ T19), T43 (≠ I53), D44 (= D54), R47 (= R57), V145 (vs. gap), R163 (= R157), V166 (≠ L160), Y168 (vs. gap), E172 (= E163), V177 (= V168), K180 (≠ R171), S181 (≠ R172), Y187 (= Y178), E207 (≠ A198), E208 (≠ D199), W209 (≠ L200), L210 (= L201), V211 (≠ D202), R237 (≠ I228), K241 (≠ G232)
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)
33% identity, 82% coverage: 13:258/301 of query aligns to 3:267/468 of 1j09A
- active site: K246 (= K237)
- binding adenosine-5'-triphosphate: H15 (= H25), E208 (≠ D199), L235 (= L226), L236 (≠ I227), K243 (= K234), I244 (≠ L235), S245 (≠ G236), K246 (= K237), R247 (≠ S238)
- binding glutamic acid: R5 (= R15), A7 (= A17), S9 (≠ T19), E41 (= E51), Y187 (= Y178), N191 (≠ V182), R205 (= R196), W209 (≠ L200)
P27000 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
33% identity, 82% coverage: 13:258/301 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).
4g6zA Crystal structure of a glutamyl-tRNA synthetase glurs from burkholderia thailandensis bound to l-glutamate (see paper)
32% identity, 75% coverage: 15:239/301 of query aligns to 6:227/380 of 4g6zA
4griB Crystal structure of a glutamyl-tRNA synthetase glurs from borrelia burgdorferi bound to glutamic acid and zinc (see paper)
31% identity, 77% coverage: 15:245/301 of query aligns to 5:261/485 of 4griB
- active site: S9 (≠ T19), K253 (= K237)
- binding glutamic acid: R5 (= R15), A7 (= A17), S9 (≠ T19), E41 (= E51), Y194 (= Y178), R212 (= R196), W216 (≠ L200)
- binding zinc ion: C105 (= C107), C107 (= C109), Y128 (= Y121), C132 (= C125)
8vc5A Crystal structure of glutamyl-tRNA synthetase glurs from pseudomonas aeruginosa (zinc bound)
31% identity, 81% coverage: 15:257/301 of query aligns to 7:274/488 of 8vc5A
6brlA Crystal structure of a glutamate tRNA ligase from elizabethkingia meningosepticum ccug26117 in complex with its amino acid
29% identity, 76% coverage: 10:237/301 of query aligns to 1:261/502 of 6brlA
3aiiA Archaeal non-discriminating glutamyl-tRNA synthetase from methanothermobacter thermautotrophicus (see paper)
33% identity, 70% coverage: 13:223/301 of query aligns to 12:228/455 of 3aiiA
Sites not aligning to the query:
4jyzA Crystal structure of e. Coli glutaminyl-tRNA synthetase bound to atp and native tRNA(gln) containing the cmnm5s2u34 anticodon wobble base (see paper)
28% identity, 39% coverage: 4:119/301 of query aligns to 14:128/542 of 4jyzA
Sites not aligning to the query:
- active site: 254, 264
- binding adenosine-5'-triphosphate: 224, 254, 255, 262, 264
- binding : 7, 129, 130, 162, 165, 175, 176, 177, 183, 186, 188, 204, 205, 227, 228, 229, 232, 307, 310, 311, 312, 313, 314, 315, 317, 319, 320, 323, 330, 335, 364, 393, 395, 396, 404, 406, 437, 438, 449, 511, 513, 514, 538, 539, 541, 542
Query Sequence
>GFF971 FitnessBrowser__psRCH2:GFF971
MPSATSAHTERYVGRFAPTPSGYLHFGSLVAALASYLDARAVGGRWLLRMEDIDPPREMP
GAQKAIIGTLISYGFEWDGEMLRQSERHDAYRDAIDRLLEQRLAYACTCSRKQLEAYPGP
YPGFCRTAGNGLDDAAIRLRVPDREYGFVDRVQGEFRQHLGREVGDFVIRRRDGLIAYQL
AVVLDDAWQGVTDVVRGADLLDSTPRQLYLQELLGLPQLRYLHLPLIIQPDGHKLGKSYR
SPPLQPHEASPLLLRALRALGQQPADELSDALPGEILTWAVRHWNADRIPRTRTLAEAQL
R
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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