SitesBLAST
Comparing WP_012101848.1 NCBI__GCF_000016505.1:WP_012101848.1 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)
4griB Crystal structure of a glutamyl-tRNA synthetase glurs from borrelia burgdorferi bound to glutamic acid and zinc (see paper)
40% identity, 98% coverage: 4:482/487 of query aligns to 2:484/485 of 4griB
- active site: S9 (= S11), K253 (= K254)
- binding glutamic acid: R5 (= R7), A7 (= A9), S9 (= S11), E41 (= E43), Y194 (= Y195), R212 (= R213), W216 (≠ Y217)
- binding zinc ion: C105 (= C107), C107 (= C109), Y128 (= Y130), C132 (= C134)
2cv2A Glutamyl-tRNA synthetase from thermus thermophilus in complex with tRNA(glu) and an enzyme inhibitor, glu-ams (see paper)
39% identity, 97% coverage: 4:477/487 of query aligns to 2:467/468 of 2cv2A
- active site: K246 (= K254)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R5 (= R7), A7 (= A9), S9 (= S11), G17 (= G19), I21 (≠ T23), E41 (= E43), Y187 (= Y195), R205 (= R213), A206 (≠ G214), E208 (= E216), W209 (≠ Y217), L235 (≠ P243), L236 (≠ I244)
- binding : S9 (= S11), T43 (= T45), D44 (= D46), R47 (= R49), V145 (= V153), R163 (≠ Y171), Y168 (≠ V176), E172 (= E180), V177 (≠ I185), K180 (= K188), S181 (= S189), Y187 (= Y195), E207 (≠ S215), E208 (= E216), W209 (≠ Y217), V211 (≠ S219), R237 (≠ M245), K241 (≠ H249), L272 (= L280), M273 (≠ L281), G274 (= G282), E282 (= E290), S299 (≠ N307), P303 (≠ A311), V304 (≠ I312), K309 (= K317), W312 (= W320), R319 (≠ K327), P357 (≠ I361), R358 (= R362), R417 (≠ M426), Q432 (≠ W441), R435 (= R444), L442 (≠ K451), E443 (≠ S452), T444 (= T453), G446 (= G456), L447 (≠ A457), F448 (= F458)
2cv1A Glutamyl-tRNA synthetase from thermus thermophilus in complex with tRNA(glu), atp, and an analog of l-glutamate: a quaternary complex
39% identity, 97% coverage: 4:477/487 of query aligns to 2:467/468 of 2cv1A
- active site: K246 (= K254)
- binding adenosine-5'-triphosphate: P8 (= P10), S9 (= S11), G17 (= G19), T18 (≠ N20), I21 (≠ T23), R47 (= R49), A206 (≠ G214), W209 (≠ Y217), L235 (≠ P243), L236 (≠ I244)
- binding (4s)-4-amino-5-hydroxypentanoic acid: R5 (= R7), A7 (= A9), E41 (= E43), Y187 (= Y195), R205 (= R213), W209 (≠ Y217)
- binding : S9 (= S11), E41 (= E43), T43 (= T45), D44 (= D46), R47 (= R49), V145 (= V153), R163 (≠ Y171), V166 (≠ I174), E172 (= E180), V177 (≠ I185), K180 (= K188), S181 (= S189), Y187 (= Y195), E207 (≠ S215), E208 (= E216), W209 (≠ Y217), V211 (≠ S219), R237 (≠ M245), K241 (≠ H249), K243 (= K251), M273 (≠ L281), G274 (= G282), S276 (≠ N284), E282 (= E290), S299 (≠ N307), P303 (≠ A311), V304 (≠ I312), K309 (= K317), W312 (= W320), R319 (≠ K327), P357 (≠ I361), R358 (= R362), R417 (≠ M426), L427 (≠ N436), Q432 (≠ W441), R435 (= R444), L442 (≠ K451), E443 (≠ S452), T444 (= T453), G446 (= G456), L447 (≠ A457), F448 (= F458)
2cuzA Glutamyl-tRNA synthetase from thermus thermophilus in complex with l- glutamate (see paper)
39% identity, 97% coverage: 4:477/487 of query aligns to 2:467/468 of 2cuzA
1n78A Crystal structure of thermus thermophilus glutamyl-tRNA synthetase complexed with tRNA(glu) and glutamol-amp. (see paper)
39% identity, 97% coverage: 4:477/487 of query aligns to 2:467/468 of 1n78A
- active site: K246 (= K254)
- binding glutamol-amp: R5 (= R7), A7 (= A9), P8 (= P10), S9 (= S11), G17 (= G19), T18 (≠ N20), I21 (≠ T23), E41 (= E43), Y187 (= Y195), N191 (= N199), R205 (= R213), A206 (≠ G214), E208 (= E216), W209 (≠ Y217), L235 (≠ P243), L236 (≠ I244)
- binding : S9 (= S11), T43 (= T45), D44 (= D46), R47 (= R49), V145 (= V153), R163 (≠ Y171), V166 (≠ I174), Y168 (≠ V176), E172 (= E180), V177 (≠ I185), K180 (= K188), S181 (= S189), Y187 (= Y195), E207 (≠ S215), E208 (= E216), W209 (≠ Y217), L210 (= L218), V211 (≠ S219), R237 (≠ M245), K241 (≠ H249), M273 (≠ L281), G274 (= G282), E282 (= E290), R297 (≠ N305), P303 (≠ A311), V304 (≠ I312), K309 (= K317), W312 (= W320), R319 (≠ K327), P357 (≠ I361), R358 (= R362), R417 (≠ M426), L427 (≠ N436), Q432 (≠ W441), R435 (= R444), L442 (≠ K451), E443 (≠ S452), T444 (= T453), G446 (= G456), L447 (≠ A457), F448 (= F458)
1j09A Crystal structure of thermus thermophilus glutamyl-tRNA synthetase complexed with atp and glu (see paper)
39% identity, 97% coverage: 4:477/487 of query aligns to 2:467/468 of 1j09A
- active site: K246 (= K254)
- binding adenosine-5'-triphosphate: H15 (= H17), E208 (= E216), L235 (≠ P243), L236 (≠ I244), K243 (= K251), I244 (≠ L252), S245 (= S253), K246 (= K254), R247 (= R255)
- binding glutamic acid: R5 (= R7), A7 (= A9), S9 (= S11), E41 (= E43), Y187 (= Y195), N191 (= N199), R205 (= R213), W209 (≠ Y217)
P27000 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
39% identity, 97% coverage: 4:477/487 of query aligns to 2:467/468 of P27000
- R358 (= R362) mutation to Q: Reduces affinity for tRNA and abolishes the ability to discriminate between tRNA(Glu) and tRNA(Gln).
1g59A Glutamyl-tRNA synthetase complexed with tRNA(glu). (see paper)
38% identity, 97% coverage: 4:477/487 of query aligns to 2:467/468 of 1g59A
- binding : D44 (= D46), R45 (≠ Q47), A46 (≠ E48), R47 (= R49), P109 (≠ K111), V145 (= V153), R163 (≠ Y171), V166 (≠ I174), E172 (= E180), V177 (≠ I185), K180 (= K188), S181 (= S189), D182 (= D190), E207 (≠ S215), E208 (= E216), R237 (≠ M245), K241 (≠ H249), T242 (≠ Q250), K243 (= K251), M273 (≠ L281), G274 (= G282), E282 (= E290), S299 (≠ N307), L300 (≠ K308), P303 (≠ A311), V304 (≠ I312), K309 (= K317), W312 (= W320), R319 (≠ K327), P357 (≠ I361), R358 (= R362), R417 (≠ M426), K426 (= K435), L427 (≠ N436), Q432 (≠ W441), R435 (= R444), L442 (≠ K451), E443 (≠ S452), T444 (= T453), P445 (= P454), G446 (= G456), L447 (≠ A457), F448 (= F458)
8vc5A Crystal structure of glutamyl-tRNA synthetase glurs from pseudomonas aeruginosa (zinc bound)
39% identity, 99% coverage: 1:480/487 of query aligns to 1:469/488 of 8vc5A
3al0C Crystal structure of the glutamine transamidosome from thermotoga maritima in the glutamylation state. (see paper)
40% identity, 98% coverage: 4:481/487 of query aligns to 103:563/564 of 3al0C
- active site: S110 (= S11), K335 (= K254)
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: R106 (= R7), A108 (= A9), P109 (= P10), G118 (= G19), T122 (= T23), E142 (= E43), Y276 (= Y195), R294 (= R213), G295 (= G214), D297 (≠ E216), H298 (≠ Y217), L324 (≠ P243), I325 (= I244), L333 (= L252)
- binding : T144 (= T45), D145 (= D46), R148 (= R49), Y208 (≠ K118), P213 (≠ E123), K252 (≠ Y171), M255 (≠ I174), I266 (= I185), K269 (= K188), S270 (= S189), Y276 (= Y195), D297 (≠ E216), H298 (≠ Y217), L299 (= L218), S300 (= S219), N301 (≠ S220), K304 (= K223), R330 (≠ H249), P332 (≠ K251), G363 (= G282), W364 (= W283), R365 (≠ N284), E370 (= E290), S387 (≠ N307), K389 (≠ S309), V391 (≠ A311), I392 (= I312), K397 (= K317), W400 (= W320), R407 (≠ K327), E446 (vs. gap), K447 (≠ R362), Q453 (≠ E368), I457 (vs. gap), R509 (≠ M426), K520 (≠ G437), Q524 (≠ W441), R527 (= R444), V535 (≠ S452), T536 (= T453), G538 (= G456), L539 (≠ A457)
6brlA Crystal structure of a glutamate tRNA ligase from elizabethkingia meningosepticum ccug26117 in complex with its amino acid (see paper)
37% identity, 98% coverage: 3:481/487 of query aligns to 2:502/502 of 6brlA
8i9iA Glutamyl-tRNA synthetase from escherichia coli bound to glutamate and zinc
36% identity, 97% coverage: 3:473/487 of query aligns to 2:457/468 of 8i9iA
P04805 Glutamate--tRNA ligase; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Escherichia coli (strain K12) (see 4 papers)
36% identity, 97% coverage: 3:473/487 of query aligns to 2:457/471 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 (= C134) mutation to S: Loss of activity. Strong decrease in zinc content.
- H127 (≠ E141) mutation to Q: 10-fold decrease in activity. Strong decrease in zinc content.
- H129 (≠ N143) mutation to Q: No change in activity or in zinc content.
- H131 (≠ K145) mutation to Q: No change in activity or in zinc content.
- H132 (≠ L146) mutation to Q: No change in activity or in zinc content.
- C138 (≠ Y152) mutation to S: No change in activity or in zinc content.
- S239 (= S253) modified: Phosphoserine; mutation to D: Does not aminoacylate tRNA(Glu), not phosphorylated by HipA.
4g6zA Crystal structure of a glutamyl-tRNA synthetase glurs from burkholderia thailandensis bound to l-glutamate (see paper)
37% identity, 79% coverage: 4:386/487 of query aligns to 3:362/380 of 4g6zA
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, 99% coverage: 4:484/487 of query aligns to 3:485/485 of Q8DLI5
- R6 (= R7) binding L-glutamate
- Y192 (= Y195) binding L-glutamate
2cfoA Non-discriminating glutamyl-tRNA synthetase from thermosynechococcus elongatus in complex with glu (see paper)
34% identity, 99% coverage: 4:484/487 of query aligns to 2:484/484 of 2cfoA
P27305 Glutamyl-Q tRNA(Asp) synthetase; Glu-Q-RSs; EC 6.1.1.- from Escherichia coli (strain K12) (see paper)
35% identity, 61% coverage: 2:299/487 of query aligns to 14:282/308 of P27305
- E55 (= E43) binding L-glutamate
- Y182 (= Y195) binding L-glutamate
- R200 (= R213) binding L-glutamate
4a91A Crystal structure of the glutamyl-queuosine trnaasp synthetase from e. Coli complexed with l-glutamate (see paper)
34% identity, 61% coverage: 2:299/487 of query aligns to 2:268/290 of 4a91A
- active site: S11 (= S11), K229 (= K254)
- binding glutamic acid: R7 (= R7), A9 (= A9), S11 (= S11), E43 (= E43), Y170 (= Y195), R188 (= R213), L192 (≠ Y217)
- binding zinc ion: C99 (= C107), C101 (= C109), Y113 (= Y130), C117 (= C134)
3aiiA Archaeal non-discriminating glutamyl-tRNA synthetase from methanothermobacter thermautotrophicus (see paper)
33% identity, 49% coverage: 3:240/487 of query aligns to 10:228/455 of 3aiiA
Sites not aligning to the query:
Q8CGC7 Bifunctional glutamate/proline--tRNA ligase; Bifunctional aminoacyl-tRNA synthetase; EC 6.1.1.17; EC 6.1.1.15 from Mus musculus (Mouse) (see 2 papers)
24% identity, 48% coverage: 1:236/487 of query aligns to 195:418/1512 of Q8CGC7
Sites not aligning to the query:
- 999 modified: Phosphoserine; by RPS6KB1; S→A: Loss of function in translation inhibition. Loss of interaction with SLC27A1. Mutant mice have no apparent developmental defect but display reduced adiposity associated with decreased insulin levels and adipocytes size. They also display increased lipolysis and fatty acid beta-oxidation and an extended lifespan. Adipocytes display decreased insulin-stimulated long-chain fatty acid uptake.; S→D: Constitutively active in translation inhibition (phosphomimetic). Mutant mice have no apparent developmental defect and do not display overt phenotype related to adiposity or lifespan.
Query Sequence
>WP_012101848.1 NCBI__GCF_000016505.1:WP_012101848.1
MTKVRTRFAPSPTGYMHVGNLRTALYTYLIAKHDGGDFILRIEDTDQERFVEGALDIIYH
TLEITGLKHDEGPDIGGPVGPYIQSQRTDIYLEYAKELIDKGKAYYCFCTKERMDSLKNK
DDEEKEFYKYDKHCLKLSKEEINEKLASNIPYVIRQNNPESGFTTFHDEIYGDISVDNSE
LDDMILIKSDGYPTYNFANVVDDHLMGITHVVRGSEYLSSAPKYNRLYDAFGWEVPIYIH
CPPIMKDAHQKLSKRNGDASFQDLIEKGYLKEAVLNYIALLGWNPGNEKEIFDLDELVEL
FNYKNINKSPAIFDNVKLKWMNGEYMKKLPLEEFNKMALPYYKKVISKNLDFLKISELLK
IRVEILSEIPDMLDFFNELPEYSTEIYIHKKMKTNLENSLFTLEKILPKFKELSPWTLEN
IEKCCMDLISELQVKNGIVLWPVRIALSGKKSTPGGAFEIADIIGKDESLKRIEYGIKKL
KLESGDN
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