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Comparing Dsui_2863 FitnessBrowser__PS:Dsui_2863 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)
4ex5A Crystal structure of lysyl-tRNA synthetase lysrs from burkholderia thailandensis bound to lysine (see paper)
65% identity, 98% coverage: 11:498/500 of query aligns to 1:486/486 of 4ex5A
- active site: R242 (= R258), E244 (= E260), R249 (= R265), H250 (= H266), E405 (= E417), N408 (= N420), R464 (= R476)
- binding lysine: E220 (= E236), E258 (= E274), Y260 (= Y276), F410 (= F422), E412 (= E424), G457 (= G469), G459 (= G471)
P0A8N5 Lysine--tRNA ligase, heat inducible; Lysyl-tRNA synthetase; LysRS; EC 6.1.1.6 from Escherichia coli (strain K12) (see 2 papers)
60% identity, 100% coverage: 1:499/500 of query aligns to 1:504/505 of P0A8N5
- M1 (= M1) modified: Initiator methionine, Removed
- K114 (= K109) modified: N6-acetyllysine
- K156 (= K151) modified: N6-acetyllysine
1e24A Lysyl-tRNA synthetase (lysu) hexagonal form complexed with lysine and atp and mn2+ (see paper)
60% identity, 98% coverage: 10:497/500 of query aligns to 3:484/485 of 1e24A
- active site: R245 (= R258), E247 (= E260), R252 (= R265), H253 (= H266), E404 (= E417), N407 (= N420), R463 (= R476)
- binding adenosine-5'-triphosphate: R245 (= R258), R252 (= R265), H253 (= H266), N254 (= N267), F257 (= F270), M259 (= M272), E404 (= E417), I405 (= I418), G460 (= G473), R463 (= R476)
- binding lysine: G199 (= G212), E223 (= E236), E261 (= E274), Y263 (= Y276), N407 (= N420), F409 (= F422), E411 (= E424), G456 (= G469), G458 (= G471)
- binding manganese (ii) ion: E397 (= E410), E404 (= E417)
1e22A Lysyl-tRNA synthetase (lysu) hexagonal form complexed with lysine and the non-hydrolysable atp analogue amp-pcp (see paper)
60% identity, 98% coverage: 10:497/500 of query aligns to 3:484/485 of 1e22A
- active site: R245 (= R258), E247 (= E260), R252 (= R265), H253 (= H266), E404 (= E417), N407 (= N420), R463 (= R476)
- binding phosphomethylphosphonic acid adenylate ester: R245 (= R258), R252 (= R265), H253 (= H266), N254 (= N267), F257 (= F270), E404 (= E417), I405 (= I418), G460 (= G473), R463 (= R476)
- binding lysine: G199 (= G212), E223 (= E236), M259 (= M272), E261 (= E274), Y263 (= Y276), N407 (= N420), F409 (= F422), E411 (= E424), G456 (= G469), G458 (= G471)
- binding magnesium ion: E397 (= E410), E404 (= E417)
1e1tA Lysyl-tRNA synthetase (lysu) hexagonal form complexed with the lysyl_adenylate intermediate (see paper)
60% identity, 98% coverage: 10:497/500 of query aligns to 3:484/485 of 1e1tA
- active site: R245 (= R258), E247 (= E260), R252 (= R265), H253 (= H266), E404 (= E417), N407 (= N420), R463 (= R476)
- binding adenosine-5'-[lysyl-phosphate]: G199 (= G212), E223 (= E236), R245 (= R258), R252 (= R265), H253 (= H266), N254 (= N267), F257 (= F270), M259 (= M272), E261 (= E274), Y263 (= Y276), E404 (= E417), I405 (= I418), N407 (= N420), F409 (= F422), E411 (= E424), G456 (= G469), G458 (= G471), G460 (= G473)
- binding magnesium ion: E397 (= E410), E404 (= E417)
- binding pyrophosphate 2-: H253 (= H266), E404 (= E417), R463 (= R476)
1bbuA Lysyl-tRNA synthetase (lyss) complexed with lysine (see paper)
61% identity, 98% coverage: 10:497/500 of query aligns to 3:485/486 of 1bbuA
- active site: R246 (= R258), E248 (= E260), R253 (= R265), H254 (= H266), E405 (= E417), N408 (= N420), R464 (= R476)
- binding lysine: G200 (= G212), E224 (= E236), E262 (= E274), Y264 (= Y276), F410 (= F422), E412 (= E424), G457 (= G469), G459 (= G471)
5yzxA Crystal structure of e.Coli lysu t146d mutant
60% identity, 98% coverage: 10:497/500 of query aligns to 2:483/484 of 5yzxA
- binding bis(adenosine)-5'-tetraphosphate: R244 (= R258), E246 (= E260), H252 (= H266), N253 (= N267), F256 (= F270), M258 (= M272), D358 (≠ E372), E403 (= E417), I404 (= I418), G459 (= G473), R462 (= R476)
- binding calcium ion: D358 (≠ E372), E396 (= E410), E396 (= E410), E403 (= E417), N406 (= N420)
1e1oA Lysyl-tRNA synthetase (lysu) hexagonal form, complexed with lysine (see paper)
60% identity, 98% coverage: 10:497/500 of query aligns to 3:483/484 of 1e1oA
- active site: R245 (= R258), E247 (= E260), H252 (= H266), E403 (= E417), N406 (= N420), R462 (= R476)
- binding lysine: G199 (= G212), E223 (= E236), E260 (= E274), Y262 (= Y276), N406 (= N420), F408 (= F422), E410 (= E424), G455 (= G469), G457 (= G471)
6wbdB Crystal structure of lysyl-tRNA synthetase from stenotrophomonas maltophilia with bound l-lysine
59% identity, 98% coverage: 10:497/500 of query aligns to 1:484/485 of 6wbdB
3e9iA Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with l-lysine hydroxamate-amp (see paper)
55% identity, 97% coverage: 12:497/500 of query aligns to 3:483/484 of 3e9iA
- active site: R245 (= R258), E247 (= E260), R252 (= R265), H253 (= H266), E403 (= E417), N406 (= N420), R462 (= R476)
- binding 5'-O-{(R)-hydroxy[(L-lysylamino)oxy]phosphoryl}adenosine: G199 (= G212), E223 (= E236), R245 (= R258), H253 (= H266), N254 (= N267), F257 (= F270), M259 (= M272), E261 (= E274), Y263 (= Y276), E403 (= E417), H404 (≠ I418), N406 (= N420), F408 (= F422), E410 (= E424), G459 (= G473)
3e9hA Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with l-lysylsulfamoyl adenosine (see paper)
55% identity, 97% coverage: 12:497/500 of query aligns to 3:483/484 of 3e9hA
- active site: R245 (= R258), E247 (= E260), R252 (= R265), H253 (= H266), E403 (= E417), N406 (= N420), R462 (= R476)
- binding 5'-o-[(l-lysylamino)sulfonyl]adenosine: E223 (= E236), R245 (= R258), H253 (= H266), N254 (= N267), F257 (= F270), M259 (= M272), E261 (= E274), Y263 (= Y276), E403 (= E417), H404 (≠ I418), N406 (= N420), F408 (= F422), E410 (= E424), G455 (= G469), G459 (= G473), R462 (= R476)
- binding magnesium ion: E396 (= E410), E403 (= E417), N406 (= N420)
3a74A Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with diadenosine tetraphosphate (ap4a)
55% identity, 97% coverage: 12:497/500 of query aligns to 3:483/484 of 3a74A
- active site: R245 (= R258), E247 (= E260), R252 (= R265), H253 (= H266), E403 (= E417), N406 (= N420), R462 (= R476)
- binding bis(adenosine)-5'-tetraphosphate: R245 (= R258), E247 (= E260), R252 (= R265), H253 (= H266), N254 (= N267), F257 (= F270), M259 (= M272), E358 (= E372), E362 (= E376), E403 (= E417), N406 (= N420), G459 (= G473), R462 (= R476)
- binding 2,6-diamino-hexanoic acid amide: G199 (= G212), E223 (= E236), M259 (= M272), E261 (= E274), Y263 (= Y276), N406 (= N420), F408 (= F422), E410 (= E424)
- binding magnesium ion: E396 (= E410), E396 (= E410), E403 (= E417), E403 (= E417)
Q15046 Lysine--tRNA ligase; Lysyl-tRNA synthetase; LysRS; EC 2.7.7.-; EC 6.1.1.6 from Homo sapiens (Human) (see 16 papers)
43% identity, 98% coverage: 10:500/500 of query aligns to 72:577/597 of Q15046
- R80 (= R18) to H: in DEAPLE; uncertain significance; dbSNP:rs369114426
- V101 (≠ R38) mutation V->D,R,W: Disrupts interaction with AIMP2 and the multisynthase complex.
- L105 (≠ A42) to H: in CMTRIB; severely affects enzyme activity; dbSNP:rs267607194
- G189 (≠ F124) to D: in LEPID; does not rescue the developmental defects caused by KARS1 depletion in xenopus
- P200 (≠ V135) to L: in DEAPLE and LEPID; reduces interaction with AIMP2. Reduces tRNA-lysine aminoacylation
- S207 (= S142) modified: Phosphoserine; mutation to A: Strongly reduced production of diadenosine tetraphosphate (Ap4A). Reduced protein phosphorylation.; mutation to D: Phosphomimetic mutant that strongly enhances translocation into the nucleus and production of diadenosine tetraphosphate (Ap4A). Almost complete loss of tRNA ligase activity.; mutation to R: Strongly decreased tRNA ligase activity.; mutation to Y: Almost complete loss of tRNA ligase activity.
- F263 (= F198) to V: in DEAPLE; reduces interaction with AIMP2. Reduces tRNA-lysine aminoacylation; dbSNP:rs772410450
- G277 (= G212) binding
- E301 (= E236) binding
- RNE 323:325 (= RNE 258:260) binding
- HN 331:332 (= HN 266:267) binding
- E339 (= E274) binding
- Y341 (= Y276) binding
- D346 (= D281) mutation to R: Induces protein aggregation. Releases from the subunit complex.
- L350 (= L285) to H: found in a patient with hypertrophic cardiomyopathy and mild intellectual disability together with proximal muscle weakness; uncertain significance
- P390 (= P318) to R: found in a patient with hypertrophic cardiomyopathy and mild intellectual disability together with proximal muscle weakness; uncertain significance
- R438 (≠ M361) to W: in LEPID; uncertain significance; dbSNP:rs761527468
- V448 (≠ F371) to F: in DEAPLE; uncertain significance
- R477 (≠ D400) to H: in DEAPLE and LEPID; decreases tRNA-lysine aminoacylation; induces protein aggregation; releases from the subunit complex; no effect on cytoplasmic location; no effect on oligomerization; dbSNP:rs778748895
- EI 494:495 (= EI 417:418) binding
- N497 (= N420) binding
- E501 (= E424) binding
- P505 (= P428) to S: in DEAPLE; decreases tRNA-lysine aminoacylation; slightly induces protein aggregation; no effect on cytoplasmic location; no effect on oligomerization; dbSNP:rs1555512658
- E525 (= E448) to K: in LEPID; uncertain significance; dbSNP:rs770522582
- G540 (= G463) mutation to Y: Disrupts interaction with AIMP2 and the multisynthase complex. Increases production of diadenosine tetraphosphate (Ap4A). Almost complete loss of tRNA ligase activity.
- GIDR 550:553 (= GIDR 473:476) binding
- L568 (≠ I491) to F: in LEPID; decreases tRNA-lysine aminoacylation activity of both the mitochondrial and cytosolic forms. Does not rescue the developmental defects caused by KARS1 depletion in xenopus
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 1:65 mutation Missing: Loss of nuclear localization, but no effect on packaging into HIV-1.
- 2 modified: N-acetylalanine
- 595 T → S: in dbSNP:rs6834
6chdA Crystal structure of human lysyl-tRNA synthetase complexed with l- lysylsulfamoyl adenosine
43% identity, 98% coverage: 10:499/500 of query aligns to 2:506/506 of 6chdA
- binding 5'-o-[(l-lysylamino)sulfonyl]adenosine: G207 (= G212), A229 (= A234), E231 (= E236), R253 (= R258), H261 (= H266), N262 (= N267), F265 (= F270), E269 (= E274), Y271 (= Y276), E424 (= E417), I425 (= I418), N427 (= N420), Y429 (≠ F422), E431 (= E424), G476 (= G469), G478 (= G471), G480 (= G473), R483 (= R476)
4ycuA Crystal structure of cladosporin in complex with human lysyl-tRNA synthetase (see paper)
43% identity, 98% coverage: 10:499/500 of query aligns to 1:505/505 of 4ycuA
- active site: R252 (= R258), E254 (= E260), T259 (≠ R265), H260 (= H266), E423 (= E417), N426 (= N420), R482 (= R476)
- binding cladosporin: E254 (= E260), H260 (= H266), N261 (= N267), F264 (= F270), N426 (= N420), G479 (= G473), R482 (= R476)
- binding lysine: G206 (= G212), E230 (= E236), E268 (= E274), Y270 (= Y276), N426 (= N420), Y428 (≠ F422), E430 (= E424), G475 (= G469)
3bjuA Crystal structure of tetrameric form of human lysyl-tRNA synthetase (see paper)
43% identity, 98% coverage: 10:499/500 of query aligns to 3:503/503 of 3bjuA
- active site: R250 (= R258), E252 (= E260), T257 (≠ R265), H258 (= H266), E421 (= E417), N424 (= N420), R480 (= R476)
- binding adenosine-5'-triphosphate: R250 (= R258), H258 (= H266), N259 (= N267), F262 (= F270), E421 (= E417), G477 (= G473), R480 (= R476)
- binding calcium ion: E414 (= E410), E421 (= E417)
- binding lysine: G204 (= G212), E228 (= E236), E266 (= E274), Y268 (= Y276), N424 (= N420), Y426 (≠ F422), E428 (= E424), G473 (= G469)
4dpgA Crystal structure of human lysrs: p38/aimp2 complex i (see paper)
43% identity, 98% coverage: 10:497/500 of query aligns to 2:500/501 of 4dpgA
- active site: R249 (= R258), E251 (= E260), T256 (≠ R265), H257 (= H266), E420 (= E417), N423 (= N420), R479 (= R476)
- binding diphosphomethylphosphonic acid adenosyl ester: R249 (= R258), T256 (≠ R265), H257 (= H266), N258 (= N267), F261 (= F270), R479 (= R476)
- binding lysine: E227 (= E236), E265 (= E274), Y267 (= Y276), N423 (= N420), Y425 (≠ F422), E427 (= E424), G472 (= G469)
- binding magnesium ion: E413 (= E410), E420 (= E417)
P15180 Lysine--tRNA ligase, cytoplasmic; Lysyl-tRNA synthetase; LysRS; EC 6.1.1.6 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
41% identity, 98% coverage: 10:497/500 of query aligns to 69:577/591 of P15180
- R488 (= R408) mutation to L: In GCD5-1; defects in lysine-binding.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
6ildB Crystal structure of human lysrs: p38/aimp2 complex ii (see paper)
42% identity, 98% coverage: 10:497/500 of query aligns to 1:498/499 of 6ildB
- active site: R247 (= R258), E249 (= E260), T254 (≠ R265), H255 (= H266), E418 (= E417), N421 (= N420), R477 (= R476)
- binding 5'-O-[(S)-hydroxy(methyl)phosphoryl]adenosine: T254 (≠ R265), H255 (= H266), F259 (= F270), E418 (= E417), R477 (= R476)
- binding lysine: G201 (= G212), E225 (= E236), E263 (= E274), Y265 (= Y276), Y423 (≠ F422), E425 (= E424), G470 (= G469), W471 (≠ C470)
- binding magnesium ion: E411 (= E410), E418 (= E417)
4ycwA Crystal structure of cladosporin in complex with plasmodium like human lysyl-tRNA synthetase mutant
43% identity, 98% coverage: 10:497/500 of query aligns to 1:500/501 of 4ycwA
- active site: R249 (= R258), E251 (= E260), T256 (≠ R265), H257 (= H266), E420 (= E417), N423 (= N420), R479 (= R476)
- binding cladosporin: R249 (= R258), E251 (= E260), H257 (= H266), N258 (= N267), F261 (= F270), E420 (= E417), I421 (= I418), C422 (≠ A419), N423 (= N420), G476 (= G473), R479 (= R476)
- binding lysine: E227 (= E236), E265 (= E274), Y267 (= Y276), N423 (= N420), Y425 (≠ F422), E427 (= E424), G472 (= G469), W473 (≠ C470)
- binding : V30 (≠ R38), S33 (≠ T41), I171 (≠ V180), S174 (= S183), T178 (≠ Q187), D185 (≠ I194), E186 (≠ S195), G188 (≠ H197), F189 (= F198), R240 (≠ K249), M268 (≠ E277), Y270 (= Y279), A271 (= A280), D275 (≠ L284)
Query Sequence
>Dsui_2863 FitnessBrowser__PS:Dsui_2863
MTEQTAQPQDENQLIAERRAKLAKWRESGKAYPNDFRRENTAGRLDELYSEKTAEELEAA
PISVKVAGRIMLRRLMGKASFATIQDVSGRIQLYVKVDLVGAEAYDDFKHWDIGDIVGAE
GTLFKTRTGELTIQVSEIRLLSKALRPLPEKFHGLTDMEQRHRQRYLDLIMNESSRFTFV
ARSRMIQSIRNYMISHHFLEVETPMMHPIPGGASAKPFITHHNALDMELFLRIAPELYLK
RLVVGGFEKVFEVNRNFRNEGLSTRHNPEFTMMEFYEAYADYKLLMDFTEGLLRHAARDA
LGTEVFQYQGRELDLSKPFARLTMVQAVRAQCPGYSEAELNDAEWLKKKLGEMKVAVKPG
MGLGALQLLMFEEVAEANLWDPTFIIDYPVEVSPLARASDSNPEITERFELFIVGREIAN
GFSELNDPEDQAARFLEQAKAKDAGDEEAMFYDADYIKALEFGLPPTGGCGIGIDRLVML
LTDTANIRDVILFPQMRKED
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