SitesBLAST
Comparing BWI76_RS05010 FitnessBrowser__Koxy:BWI76_RS05010 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)
74% identity, 100% coverage: 1:293/293 of query aligns to 11:303/308 of P27305
- E55 (= E45) binding
- Y182 (= Y172) binding
- R200 (= R190) binding
4a91A Crystal structure of the glutamyl-queuosine trnaasp synthetase from e. Coli complexed with l-glutamate (see paper)
74% identity, 99% coverage: 3:293/293 of query aligns to 1:289/290 of 4a91A
- active site: S11 (= S13), K229 (= K231)
- binding glutamic acid: R7 (= R9), A9 (= A11), S11 (= S13), E43 (= E45), Y170 (= Y172), R188 (= R190), L192 (= L194)
- binding zinc ion: C99 (= C101), C101 (= C103), Y113 (= Y115), C117 (= C119)
2cfoA Non-discriminating glutamyl-tRNA synthetase from thermosynechococcus elongatus in complex with glu (see paper)
34% identity, 84% coverage: 9:255/293 of query aligns to 5:278/484 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)
34% identity, 84% coverage: 9:255/293 of query aligns to 6:279/485 of Q8DLI5
- R6 (= R9) binding
- Y192 (= Y172) binding
4griB Crystal structure of a glutamyl-tRNA synthetase glurs from borrelia burgdorferi bound to glutamic acid and zinc (see paper)
31% identity, 90% coverage: 9:273/293 of query aligns to 5:299/485 of 4griB
- active site: S9 (= S13), K253 (= K231)
- binding glutamic acid: R5 (= R9), A7 (= A11), S9 (= S13), E41 (= E45), Y194 (= Y172), R212 (= R190), W216 (≠ L194)
- binding zinc ion: C105 (= C101), C107 (= C103), Y128 (= Y115), C132 (= C119)
4g6zA Crystal structure of a glutamyl-tRNA synthetase glurs from burkholderia thailandensis bound to l-glutamate (see paper)
36% identity, 77% coverage: 9:235/293 of query aligns to 6:229/380 of 4g6zA
3al0C Crystal structure of the glutamine transamidosome from thermotoga maritima in the glutamylation state. (see paper)
34% identity, 78% coverage: 9:238/293 of query aligns to 106:342/564 of 3al0C
- active site: S110 (= S13), K335 (= K231)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R106 (= R9), A108 (= A11), P109 (= P12), G118 (= G21), T122 (≠ A25), E142 (= E45), Y276 (= Y172), R294 (= R190), G295 (= G191), D297 (= D193), H298 (≠ L194), L324 (= L220), I325 (≠ A221), L333 (= L229)
- binding : T144 (≠ I47), D145 (= D48), R148 (= R51), Y208 (≠ C103), P213 (≠ I108), K252 (≠ R147), M255 (≠ I150), I266 (= I162), K269 (≠ R165), S270 (≠ R166), Y276 (= Y172), D297 (= D193), H298 (≠ L194), L299 (≠ I195), S300 (≠ E196), N301 (≠ P197), K304 (≠ R200), 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
1g59A Glutamyl-tRNA synthetase complexed with tRNA(glu). (see paper)
35% identity, 79% coverage: 7:238/293 of query aligns to 3:253/468 of 1g59A
- binding : D44 (= D48), R45 (≠ P49), A46 (≠ P50), R47 (= R51), P109 (≠ R105), V145 (≠ A130), R163 (= R147), V166 (≠ I150), E172 (≠ L156), V177 (≠ I162), K180 (≠ R165), S181 (≠ R166), D182 (= D167), E207 (≠ A192), E208 (≠ D193), R237 (≠ L222), K241 (≠ G226), T242 (≠ N227), 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
P04805 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Escherichia coli (strain K12) (see 4 papers)
34% identity, 78% coverage: 9:238/293 of query aligns to 6:247/471 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 (= C119) 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 (≠ L122) mutation to Q: No change in activity or in zinc content.
- H131 (≠ L124) mutation to Q: No change in activity or in zinc content.
- H132 (≠ G125) mutation to Q: No change in activity or in zinc content.
- C138 (≠ L131) 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.
2cv2A Glutamyl-tRNA synthetase from thermus thermophilus in complex with tRNA(glu) and an enzyme inhibitor, glu-ams (see paper)
35% identity, 79% coverage: 7:238/293 of query aligns to 3:253/468 of 2cv2A
- active site: K246 (= K231)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R5 (= R9), A7 (= A11), S9 (= S13), G17 (= G21), I21 (≠ A25), E41 (= E45), Y187 (= Y172), R205 (= R190), A206 (≠ G191), E208 (≠ D193), W209 (≠ L194), L235 (= L220), L236 (≠ A221)
- binding : S9 (= S13), T43 (≠ I47), D44 (= D48), R47 (= R51), V145 (≠ A130), R163 (= R147), Y168 (≠ A152), E172 (≠ L156), V177 (≠ I162), K180 (≠ R165), S181 (≠ R166), Y187 (= Y172), E207 (≠ A192), E208 (≠ D193), W209 (≠ L194), V211 (≠ E196), R237 (≠ L222), 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
35% identity, 79% coverage: 7:238/293 of query aligns to 3:253/468 of 2cv1A
- active site: K246 (= K231)
- binding adenosine-5'-triphosphate: P8 (= P12), S9 (= S13), G17 (= G21), T18 (≠ S22), I21 (≠ A25), R47 (= R51), A206 (≠ G191), W209 (≠ L194), L235 (= L220), L236 (≠ A221)
- binding (4s)-4-amino-5-hydroxypentanoic acid: R5 (= R9), A7 (= A11), E41 (= E45), Y187 (= Y172), R205 (= R190), W209 (≠ L194)
- binding : S9 (= S13), E41 (= E45), T43 (≠ I47), D44 (= D48), R47 (= R51), V145 (≠ A130), R163 (= R147), V166 (≠ I150), E172 (≠ L156), V177 (≠ I162), K180 (≠ R165), S181 (≠ R166), Y187 (= Y172), E207 (≠ A192), E208 (≠ D193), W209 (≠ L194), V211 (≠ E196), R237 (≠ L222), 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)
35% identity, 79% coverage: 7:238/293 of query aligns to 3:253/468 of 2cuzA
1n78A Crystal structure of thermus thermophilus glutamyl-tRNA synthetase complexed with tRNA(glu) and glutamol-amp. (see paper)
35% identity, 79% coverage: 7:238/293 of query aligns to 3:253/468 of 1n78A
- active site: K246 (= K231)
- binding glutamol-amp: R5 (= R9), A7 (= A11), P8 (= P12), S9 (= S13), G17 (= G21), T18 (≠ S22), I21 (≠ A25), E41 (= E45), Y187 (= Y172), N191 (≠ V176), R205 (= R190), A206 (≠ G191), E208 (≠ D193), W209 (≠ L194), L235 (= L220), L236 (≠ A221)
- binding : S9 (= S13), T43 (≠ I47), D44 (= D48), R47 (= R51), V145 (≠ A130), R163 (= R147), V166 (≠ I150), Y168 (≠ A152), E172 (≠ L156), V177 (≠ I162), K180 (≠ R165), S181 (≠ R166), Y187 (= Y172), E207 (≠ A192), E208 (≠ D193), W209 (≠ L194), L210 (≠ I195), V211 (≠ E196), R237 (≠ L222), 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)
35% identity, 79% coverage: 7:238/293 of query aligns to 3:253/468 of 1j09A
- active site: K246 (= K231)
- binding adenosine-5'-triphosphate: H15 (= H19), E208 (≠ D193), L235 (= L220), L236 (≠ A221), K243 (= K228), I244 (≠ L229), S245 (= S230), K246 (= K231), R247 (≠ Q232)
- binding glutamic acid: R5 (= R9), A7 (= A11), S9 (= S13), E41 (= E45), 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)
35% identity, 79% coverage: 7:238/293 of query aligns to 3:253/468 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).
8i9iA Glutamyl-tRNA synthetase from escherichia coli bound to glutamate and zinc
34% identity, 78% coverage: 9:238/293 of query aligns to 6:247/468 of 8i9iA
8vc5A Crystal structure of glutamyl-tRNA synthetase glurs from pseudomonas aeruginosa (zinc bound)
32% identity, 79% coverage: 9:239/293 of query aligns to 7:262/488 of 8vc5A
6brlA Crystal structure of a glutamate tRNA ligase from elizabethkingia meningosepticum ccug26117 in complex with its amino acid
29% identity, 77% coverage: 9:233/293 of query aligns to 6:263/502 of 6brlA
3aiiA Archaeal non-discriminating glutamyl-tRNA synthetase from methanothermobacter thermautotrophicus (see paper)
34% identity, 71% coverage: 9:217/293 of query aligns to 14:228/455 of 3aiiA
Sites not aligning to the query:
4h3sA The structure of glutaminyl-tRNA synthetase from saccharomyces cerevisiae (see paper)
31% identity, 35% coverage: 9:112/293 of query aligns to 41:146/585 of 4h3sA
Sites not aligning to the query:
Query Sequence
>BWI76_RS05010 FitnessBrowser__Koxy:BWI76_RS05010
MKDSHYIGRFAPSPSGELHFGSLIAALGSYLQARAQNGIWRVRIEDIDPPREVPGAADTI
LRQLERYGLHWDGEVLWQSKRHEAYREHLAWLREQDLCYYCTCTRARIHGIGGIYDGHCR
DLRLGAENAALRLRQTRPVLEFYDRLRGTIVADEPLAREDFIIHRRDGLFAYNLAVVVDD
HFQGVSEIVRGADLIEPTVRQISLYQHFGWQAPDYIHLPLALNAQGNKLSKQNHAPALSE
GDPRPEIVRALTFLNQDVIQEWQTLSIEDLLEYAIANWRPEQIQHSQMRSAEL
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