SitesBLAST
Comparing HSERO_RS15460 FitnessBrowser__HerbieS:HSERO_RS15460 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
4g6zA Crystal structure of a glutamyl-tRNA synthetase glurs from burkholderia thailandensis bound to l-glutamate (see paper)
66% identity, 80% coverage: 6:376/466 of query aligns to 3:357/380 of 4g6zA
P04805 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Escherichia coli (strain K12) (see 4 papers)
52% identity, 99% coverage: 5:466/466 of query aligns to 2:461/471 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 (≠ W128) mutation to S: Loss of activity. Strong decrease in zinc content.
- H127 (≠ P130) mutation to Q: 10-fold decrease in activity. Strong decrease in zinc content.
- H129 (≠ P132) mutation to Q: No change in activity or in zinc content.
- H131 (≠ K134) mutation to Q: No change in activity or in zinc content.
- H132 (≠ T135) mutation to Q: No change in activity or in zinc content.
- C138 (≠ P145) mutation to S: No change in activity or in zinc content.
- S239 (= S246) 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
52% identity, 99% coverage: 5:466/466 of query aligns to 2:461/468 of 8i9iA
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)
42% identity, 96% coverage: 6:453/466 of query aligns to 3:464/485 of Q8DLI5
- R6 (= R9) binding
- Y192 (= Y188) binding
2cfoA Non-discriminating glutamyl-tRNA synthetase from thermosynechococcus elongatus in complex with glu (see paper)
42% identity, 96% coverage: 6:453/466 of query aligns to 2:463/484 of 2cfoA
4griB Crystal structure of a glutamyl-tRNA synthetase glurs from borrelia burgdorferi bound to glutamic acid and zinc (see paper)
35% identity, 98% coverage: 5:462/466 of query aligns to 1:475/485 of 4griB
- active site: S9 (= S13), K253 (= K247)
- binding glutamic acid: R5 (= R9), A7 (= A11), S9 (= S13), E41 (= E45), Y194 (= Y188), R212 (= R206), W216 (≠ H210)
- binding zinc ion: C105 (= C101), C107 (= C103), Y128 (= Y124), C132 (≠ W128)
6brlA Crystal structure of a glutamate tRNA ligase from elizabethkingia meningosepticum ccug26117 in complex with its amino acid
34% identity, 98% coverage: 5:463/466 of query aligns to 2:495/502 of 6brlA
1g59A Glutamyl-tRNA synthetase complexed with tRNA(glu). (see paper)
35% identity, 98% coverage: 6:463/466 of query aligns to 2:464/468 of 1g59A
- binding : D44 (= D48), R45 (≠ V49), A46 (≠ E50), R47 (= R51), P109 (= P105), V145 (= V146), R163 (≠ K164), V166 (≠ I167), E172 (= E173), V177 (= V178), K180 (≠ R181), S181 (≠ P182), D182 (= D183), E207 (≠ D208), E208 (≠ D209), R237 (≠ L238), K241 (≠ G242), T242 (≠ E243), K243 (= K244), M273 (≠ L274), G274 (= G275), E282 (= E282), S299 (≠ T299), L300 (≠ K300), P303 (≠ A303), V304 (≠ Q304), K309 (= K309), W312 (= W312), R319 (≠ K319), P357 (≠ D356), R358 (= R357), R417 (≠ K416), K426 (= K425), L427 (≠ M426), Q432 (≠ M431), R435 (= R434), L442 (= L441), E443 (≠ Q442), T444 (= T443), P445 (= P444), G446 (≠ A445), L447 (≠ I446), F448 (≠ D447)
3al0C Crystal structure of the glutamine transamidosome from thermotoga maritima in the glutamylation state. (see paper)
35% identity, 99% coverage: 6:466/466 of query aligns to 103:559/564 of 3al0C
- active site: S110 (= S13), K335 (= K247)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R106 (= R9), A108 (= A11), P109 (= P12), G118 (= G21), T122 (= T25), E142 (= E45), Y276 (= Y188), R294 (= R206), G295 (= G207), D297 (= D209), H298 (= H210), L324 (≠ M236), I325 (= I237), L333 (= L245)
- binding : T144 (= T47), D145 (= D48), R148 (= R51), Y208 (= Y124), P213 (= P132), K252 (= K164), M255 (≠ I167), I266 (≠ V178), K269 (≠ R181), S270 (≠ P182), Y276 (= Y188), D297 (= D209), H298 (= H210), L299 (≠ V211), S300 (≠ N212), N301 (= N213), K304 (≠ R216), R330 (≠ G242), P332 (≠ K244), G363 (= G275), W364 (= W276), R365 (≠ S277), E370 (= E282), S387 (≠ T299), K389 (≠ A301), V391 (≠ A303), I392 (≠ Q304), K397 (= K309), W400 (= W312), R407 (≠ K319), E446 (≠ D356), K447 (≠ R357), Q453 (≠ E363), I457 (≠ A367), R509 (≠ K416), K520 (≠ Q428), Q524 (≠ P432), R527 (= R434), V535 (≠ Q442), T536 (= T443), G538 (≠ A445), L539 (≠ I446)
2cv2A Glutamyl-tRNA synthetase from thermus thermophilus in complex with tRNA(glu) and an enzyme inhibitor, glu-ams (see paper)
35% identity, 98% coverage: 6:463/466 of query aligns to 2:464/468 of 2cv2A
- active site: K246 (= K247)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R5 (= R9), A7 (= A11), S9 (= S13), G17 (= G21), I21 (≠ T25), E41 (= E45), Y187 (= Y188), R205 (= R206), A206 (≠ G207), E208 (≠ D209), W209 (≠ H210), L235 (≠ M236), L236 (≠ I237)
- binding : S9 (= S13), T43 (= T47), D44 (= D48), R47 (= R51), V145 (= V146), R163 (≠ K164), Y168 (≠ I169), E172 (= E173), V177 (= V178), K180 (≠ R181), S181 (≠ P182), Y187 (= Y188), E207 (≠ D208), E208 (≠ D209), W209 (≠ H210), V211 (≠ N212), R237 (≠ L238), K241 (≠ G242), L272 (≠ R273), M273 (≠ L274), G274 (= G275), E282 (= E282), S299 (≠ T299), P303 (≠ A303), V304 (≠ Q304), K309 (= K309), W312 (= W312), R319 (≠ K319), P357 (≠ D356), R358 (= R357), R417 (≠ K416), Q432 (≠ M431), R435 (= R434), L442 (= L441), E443 (≠ Q442), T444 (= T443), G446 (≠ A445), L447 (≠ I446), F448 (≠ D447)
2cv1A Glutamyl-tRNA synthetase from thermus thermophilus in complex with tRNA(glu), atp, and an analog of l-glutamate: a quaternary complex
35% identity, 98% coverage: 6:463/466 of query aligns to 2:464/468 of 2cv1A
- active site: K246 (= K247)
- binding adenosine-5'-triphosphate: P8 (= P12), S9 (= S13), G17 (= G21), T18 (≠ G22), I21 (≠ T25), R47 (= R51), A206 (≠ G207), W209 (≠ H210), L235 (≠ M236), L236 (≠ I237)
- binding (4s)-4-amino-5-hydroxypentanoic acid: R5 (= R9), A7 (= A11), E41 (= E45), Y187 (= Y188), R205 (= R206), W209 (≠ H210)
- binding : S9 (= S13), E41 (= E45), T43 (= T47), D44 (= D48), R47 (= R51), V145 (= V146), R163 (≠ K164), V166 (≠ I167), E172 (= E173), V177 (= V178), K180 (≠ R181), S181 (≠ P182), Y187 (= Y188), E207 (≠ D208), E208 (≠ D209), W209 (≠ H210), V211 (≠ N212), R237 (≠ L238), K241 (≠ G242), K243 (= K244), M273 (≠ L274), G274 (= G275), S276 (= S277), E282 (= E282), S299 (≠ T299), P303 (≠ A303), V304 (≠ Q304), K309 (= K309), W312 (= W312), R319 (≠ K319), P357 (≠ D356), R358 (= R357), R417 (≠ K416), L427 (≠ M426), Q432 (≠ M431), R435 (= R434), L442 (= L441), E443 (≠ Q442), T444 (= T443), G446 (≠ A445), L447 (≠ I446), F448 (≠ D447)
2cuzA Glutamyl-tRNA synthetase from thermus thermophilus in complex with l-glutamate (see paper)
35% identity, 98% coverage: 6:463/466 of query aligns to 2:464/468 of 2cuzA
1n78A Crystal structure of thermus thermophilus glutamyl-tRNA synthetase complexed with tRNA(glu) and glutamol-amp. (see paper)
35% identity, 98% coverage: 6:463/466 of query aligns to 2:464/468 of 1n78A
- active site: K246 (= K247)
- binding glutamol-amp: R5 (= R9), A7 (= A11), P8 (= P12), S9 (= S13), G17 (= G21), T18 (≠ G22), I21 (≠ T25), E41 (= E45), Y187 (= Y188), N191 (≠ V192), R205 (= R206), A206 (≠ G207), E208 (≠ D209), W209 (≠ H210), L235 (≠ M236), L236 (≠ I237)
- binding : S9 (= S13), T43 (= T47), D44 (= D48), R47 (= R51), V145 (= V146), R163 (≠ K164), V166 (≠ I167), Y168 (≠ I169), E172 (= E173), V177 (= V178), K180 (≠ R181), S181 (≠ P182), Y187 (= Y188), E207 (≠ D208), E208 (≠ D209), W209 (≠ H210), L210 (≠ V211), V211 (≠ N212), R237 (≠ L238), K241 (≠ G242), M273 (≠ L274), G274 (= G275), E282 (= E282), R297 (≠ H297), P303 (≠ A303), V304 (≠ Q304), K309 (= K309), W312 (= W312), R319 (≠ K319), P357 (≠ D356), R358 (= R357), R417 (≠ K416), L427 (≠ M426), Q432 (≠ M431), R435 (= R434), L442 (= L441), E443 (≠ Q442), T444 (= T443), G446 (≠ A445), L447 (≠ I446), F448 (≠ D447)
1j09A Crystal structure of thermus thermophilus glutamyl-tRNA synthetase complexed with atp and glu (see paper)
35% identity, 98% coverage: 6:463/466 of query aligns to 2:464/468 of 1j09A
- active site: K246 (= K247)
- binding adenosine-5'-triphosphate: H15 (= H19), E208 (≠ D209), L235 (≠ M236), L236 (≠ I237), K243 (= K244), I244 (≠ L245), S245 (= S246), K246 (= K247), R247 (= R248)
- binding glutamic acid: R5 (= R9), A7 (= A11), S9 (= S13), E41 (= E45), Y187 (= Y188), N191 (≠ V192), R205 (= R206), W209 (≠ H210)
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, 98% coverage: 6:463/466 of query aligns to 2:464/468 of P27000
- R358 (= R357) mutation to Q: Reduces affinity for tRNA and abolishes the ability to discriminate between tRNA(Glu) and tRNA(Gln).
8vc5A Crystal structure of glutamyl-tRNA synthetase glurs from pseudomonas aeruginosa (zinc bound)
33% identity, 98% coverage: 4:462/466 of query aligns to 2:462/488 of 8vc5A
P27305 Glutamyl-Q tRNA(Asp) synthetase; Glu-Q-RSs; EC 6.1.1.- from Escherichia coli (strain K12) (see paper)
35% identity, 62% coverage: 1:289/466 of query aligns to 11:280/308 of P27305
- E55 (= E45) binding
- Y182 (= Y188) binding
- R200 (= R206) binding
4a91A Crystal structure of the glutamyl-queuosine trnaasp synthetase from e. Coli complexed with l-glutamate (see paper)
34% identity, 61% coverage: 4:289/466 of query aligns to 2:266/290 of 4a91A
- active site: S11 (= S13), K229 (= K247)
- binding glutamic acid: R7 (= R9), A9 (= A11), S11 (= S13), E43 (= E45), Y170 (= Y188), R188 (= R206), L192 (≠ H210)
- binding zinc ion: C99 (= C101), C101 (= C103), Y113 (= Y124), C117 (≠ W128)
3aiiA Archaeal non-discriminating glutamyl-tRNA synthetase from methanothermobacter thermautotrophicus (see paper)
33% identity, 58% coverage: 5:275/466 of query aligns to 10:278/455 of 3aiiA
4h3sA The structure of glutaminyl-tRNA synthetase from saccharomyces cerevisiae (see paper)
34% identity, 26% coverage: 1:121/466 of query aligns to 33:152/585 of 4h3sA
Sites not aligning to the query:
Query Sequence
>HSERO_RS15460 FitnessBrowser__HerbieS:HSERO_RS15460
MTATQVRTRFAPSPTGYLHLGGARTALFSWAYARRFGGTFVLRIEDTDVERSTPEAVQAI
IEGMQWLGLEHDEGPFYQMKRMDRYREVIAQMLEQGTAYYCYCTPEEVEAMRERQRAAGE
KPRYDGTWRPEPGKTLPAIPEGRKPVVRFKNPQDGEVSWNDVVKGPITISNRELDDLVIA
RPDGTPTYNFCVVVDDWDMKITHVIRGDDHVNNTPRQINILKALGGTLPEYGHVPMILGA
DGEKLSKRHGAVSVMDYPAQGYLPEAMLNYLARLGWSHGDDEIFSMQQFCAWFDLDHLTK
APAQFNPEKLNWLNNHYIKLADNARLAGLVRPLLEAQGAVFEGAPDLAAVIALLKDRANT
VNEIAAAALMFYRQPAPDAALVAQHITEAIKPALADFAQRVATVEWTKEAIAPMIKEVLA
AHGIKMPQLAMPLRLIVAGQLQTPAIDAVLQLFGREAVQARLSGYL
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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