SitesBLAST
Comparing GFF789 FitnessBrowser__Marino:GFF789 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)
P0A8N5 Lysine--tRNA ligase, heat inducible; Lysyl-tRNA synthetase; LysRS; EC 6.1.1.6 from Escherichia coli (strain K12) (see 2 papers)
61% identity, 95% coverage: 14:501/511 of query aligns to 16:504/505 of P0A8N5
- K114 (= K102) modified: N6-acetyllysine
- K156 (= K144) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1bbuA Lysyl-tRNA synthetase (lyss) complexed with lysine (see paper)
61% identity, 95% coverage: 14:500/511 of query aligns to 5:486/486 of 1bbuA
- active site: R246 (= R251), E248 (= E253), R253 (= R258), H254 (= H259), E405 (= E419), N408 (= N422), R464 (= R478)
- binding lysine: G200 (= G205), E224 (= E229), E262 (= E267), Y264 (= Y269), F410 (= F424), E412 (= E426), G457 (= G471), G459 (= G473)
1e24A Lysyl-tRNA synthetase (lysu) hexagonal form complexed with lysine and atp and mn2+ (see paper)
61% identity, 95% coverage: 14:500/511 of query aligns to 5:485/485 of 1e24A
- active site: R245 (= R251), E247 (= E253), R252 (= R258), H253 (= H259), E404 (= E419), N407 (= N422), R463 (= R478)
- binding adenosine-5'-triphosphate: R245 (= R251), R252 (= R258), H253 (= H259), N254 (= N260), F257 (= F263), M259 (= M265), E404 (= E419), I405 (= I420), G460 (= G475), R463 (= R478)
- binding lysine: G199 (= G205), E223 (= E229), E261 (= E267), Y263 (= Y269), N407 (= N422), F409 (= F424), E411 (= E426), G456 (= G471), G458 (= G473)
- binding manganese (ii) ion: E397 (= E412), E404 (= E419)
1e22A Lysyl-tRNA synthetase (lysu) hexagonal form complexed with lysine and the non-hydrolysable atp analogue amp-pcp (see paper)
61% identity, 95% coverage: 14:500/511 of query aligns to 5:485/485 of 1e22A
- active site: R245 (= R251), E247 (= E253), R252 (= R258), H253 (= H259), E404 (= E419), N407 (= N422), R463 (= R478)
- binding phosphomethylphosphonic acid adenylate ester: R245 (= R251), R252 (= R258), H253 (= H259), N254 (= N260), F257 (= F263), E404 (= E419), I405 (= I420), G460 (= G475), R463 (= R478)
- binding lysine: G199 (= G205), E223 (= E229), M259 (= M265), E261 (= E267), Y263 (= Y269), N407 (= N422), F409 (= F424), E411 (= E426), G456 (= G471), G458 (= G473)
- binding magnesium ion: E397 (= E412), E404 (= E419)
1e1tA Lysyl-tRNA synthetase (lysu) hexagonal form complexed with the lysyl_adenylate intermediate (see paper)
61% identity, 95% coverage: 14:500/511 of query aligns to 5:485/485 of 1e1tA
- active site: R245 (= R251), E247 (= E253), R252 (= R258), H253 (= H259), E404 (= E419), N407 (= N422), R463 (= R478)
- binding adenosine-5'-[lysyl-phosphate]: G199 (= G205), E223 (= E229), R245 (= R251), R252 (= R258), H253 (= H259), N254 (= N260), F257 (= F263), M259 (= M265), E261 (= E267), Y263 (= Y269), E404 (= E419), I405 (= I420), N407 (= N422), F409 (= F424), E411 (= E426), G456 (= G471), G458 (= G473), G460 (= G475)
- binding magnesium ion: E397 (= E412), E404 (= E419)
- binding pyrophosphate 2-: H253 (= H259), E404 (= E419), R463 (= R478)
5yzxA Crystal structure of e.Coli lysu t146d mutant
61% identity, 95% coverage: 14:500/511 of query aligns to 4:484/484 of 5yzxA
- binding bis(adenosine)-5'-tetraphosphate: R244 (= R251), E246 (= E253), H252 (= H259), N253 (= N260), F256 (= F263), M258 (= M265), D358 (≠ E374), E403 (= E419), I404 (= I420), G459 (= G475), R462 (= R478)
- binding calcium ion: D358 (≠ E374), E396 (= E412), E396 (= E412), E403 (= E419), N406 (= N422)
1e1oA Lysyl-tRNA synthetase (lysu) hexagonal form, complexed with lysine (see paper)
61% identity, 95% coverage: 14:500/511 of query aligns to 5:484/484 of 1e1oA
- active site: R245 (= R251), E247 (= E253), H252 (= H259), E403 (= E419), N406 (= N422), R462 (= R478)
- binding lysine: G199 (= G205), E223 (= E229), E260 (= E267), Y262 (= Y269), N406 (= N422), F408 (= F424), E410 (= E426), G455 (= G471), G457 (= G473)
4ex5A Crystal structure of lysyl-tRNA synthetase lysrs from burkholderia thailandensis bound to lysine (see paper)
56% identity, 95% coverage: 13:499/511 of query aligns to 1:485/486 of 4ex5A
- active site: R242 (= R251), E244 (= E253), R249 (= R258), H250 (= H259), E405 (= E419), N408 (= N422), R464 (= R478)
- binding lysine: E220 (= E229), E258 (= E267), Y260 (= Y269), F410 (= F424), E412 (= E426), G457 (= G471), G459 (= G473)
6wbdB Crystal structure of lysyl-tRNA synthetase from stenotrophomonas maltophilia with bound l-lysine
55% identity, 96% coverage: 12:500/511 of query aligns to 1:485/485 of 6wbdB
3e9iA Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with l-lysine hydroxamate-amp (see paper)
49% identity, 95% coverage: 12:499/511 of query aligns to 1:483/484 of 3e9iA
- active site: R245 (= R251), E247 (= E253), R252 (= R258), H253 (= H259), E403 (= E419), N406 (= N422), R462 (= R478)
- binding 5'-O-{(R)-hydroxy[(L-lysylamino)oxy]phosphoryl}adenosine: G199 (= G205), E223 (= E229), R245 (= R251), H253 (= H259), N254 (= N260), F257 (= F263), M259 (= M265), E261 (= E267), Y263 (= Y269), E403 (= E419), H404 (≠ I420), N406 (= N422), F408 (= F424), E410 (= E426), G459 (= G475)
3e9hA Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with l-lysylsulfamoyl adenosine (see paper)
49% identity, 95% coverage: 12:499/511 of query aligns to 1:483/484 of 3e9hA
- active site: R245 (= R251), E247 (= E253), R252 (= R258), H253 (= H259), E403 (= E419), N406 (= N422), R462 (= R478)
- binding 5'-o-[(l-lysylamino)sulfonyl]adenosine: E223 (= E229), R245 (= R251), H253 (= H259), N254 (= N260), F257 (= F263), M259 (= M265), E261 (= E267), Y263 (= Y269), E403 (= E419), H404 (≠ I420), N406 (= N422), F408 (= F424), E410 (= E426), G455 (= G471), G459 (= G475), R462 (= R478)
- binding magnesium ion: E396 (= E412), E403 (= E419), N406 (= N422)
3a74A Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with diadenosine tetraphosphate (ap4a)
49% identity, 95% coverage: 12:499/511 of query aligns to 1:483/484 of 3a74A
- active site: R245 (= R251), E247 (= E253), R252 (= R258), H253 (= H259), E403 (= E419), N406 (= N422), R462 (= R478)
- binding bis(adenosine)-5'-tetraphosphate: R245 (= R251), E247 (= E253), R252 (= R258), H253 (= H259), N254 (= N260), F257 (= F263), M259 (= M265), E358 (= E374), E362 (= E378), E403 (= E419), N406 (= N422), G459 (= G475), R462 (= R478)
- binding 2,6-diamino-hexanoic acid amide: G199 (= G205), E223 (= E229), M259 (= M265), E261 (= E267), Y263 (= Y269), N406 (= N422), F408 (= F424), E410 (= E426)
- binding magnesium ion: E396 (= E412), E396 (= E412), E403 (= E419), E403 (= E419)
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)
42% identity, 96% coverage: 20:511/511 of query aligns to 77:589/591 of P15180
- R488 (= R410) 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
4up7A Crystal structure of entamoeba histolytica lysyl-tRNA synthetase in complex with lysyl-adenylate (see paper)
41% identity, 97% coverage: 15:510/511 of query aligns to 11:517/529 of 4up7A
- active site: R258 (= R251), E260 (= E253), T265 (≠ R258), H266 (= H259), E426 (= E419), N429 (= N422), R485 (= R478)
- binding adenosine-5'-[lysyl-phosphate]: E236 (= E229), R258 (= R251), H266 (= H259), F270 (= F263), E274 (= E267), Y276 (= Y269), E426 (= E419), I427 (= I420), Y431 (≠ F424), E433 (= E426), G478 (= G471), R485 (= R478)
Q15046 Lysine--tRNA ligase; Lysyl-tRNA synthetase; LysRS; EC 2.7.7.-; EC 6.1.1.6 from Homo sapiens (Human) (see 16 papers)
40% identity, 96% coverage: 14:506/511 of query aligns to 74:581/597 of Q15046
- R80 (= R20) to H: in DEAPLE; uncertain significance; dbSNP:rs369114426
- V101 (≠ R40) mutation V->D,R,W: Disrupts interaction with AIMP2 and the multisynthase complex.
- L105 (≠ A44) to H: in CMTRIB; severely affects enzyme activity; dbSNP:rs267607194
- G189 (≠ S117) to D: in LEPID; does not rescue the developmental defects caused by KARS1 depletion in xenopus
- P200 (≠ M128) to L: in DEAPLE and LEPID; reduces interaction with AIMP2. Reduces tRNA-lysine aminoacylation
- S207 (≠ T135) 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 (= F191) to V: in DEAPLE; reduces interaction with AIMP2. Reduces tRNA-lysine aminoacylation; dbSNP:rs772410450
- G277 (= G205) binding
- E301 (= E229) binding
- RNE 323:325 (= RNE 251:253) binding
- HN 331:332 (= HN 259:260) binding
- E339 (= E267) binding
- Y341 (= Y269) binding
- D346 (= D274) mutation to R: Induces protein aggregation. Releases from the subunit complex.
- L350 (= L278) to H: found in a patient with hypertrophic cardiomyopathy and mild intellectual disability together with proximal muscle weakness; uncertain significance
- P390 (≠ T320) to R: found in a patient with hypertrophic cardiomyopathy and mild intellectual disability together with proximal muscle weakness; uncertain significance
- R438 (≠ L359) to W: in LEPID; uncertain significance; dbSNP:rs761527468
- V448 (≠ Q369) to F: in DEAPLE; uncertain significance
- R477 (≠ D402) 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 419:420) binding
- N497 (= N422) binding
- E501 (= E426) binding
- P505 (≠ A430) to S: in DEAPLE; decreases tRNA-lysine aminoacylation; slightly induces protein aggregation; no effect on cytoplasmic location; no effect on oligomerization; dbSNP:rs1555512658
- E525 (= E450) to K: in LEPID; uncertain significance; dbSNP:rs770522582
- G540 (= G465) 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 475:478) binding
- L568 (≠ I493) 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
4ycuA Crystal structure of cladosporin in complex with human lysyl-tRNA synthetase (see paper)
40% identity, 95% coverage: 14:501/511 of query aligns to 3:505/505 of 4ycuA
- active site: R252 (= R251), E254 (= E253), T259 (≠ R258), H260 (= H259), E423 (= E419), N426 (= N422), R482 (= R478)
- binding cladosporin: E254 (= E253), H260 (= H259), N261 (= N260), F264 (= F263), N426 (= N422), G479 (= G475), R482 (= R478)
- binding lysine: G206 (= G205), E230 (= E229), E268 (= E267), Y270 (= Y269), N426 (= N422), Y428 (≠ F424), E430 (= E426), G475 (= G471)
6chdA Crystal structure of human lysyl-tRNA synthetase complexed with l- lysylsulfamoyl adenosine
40% identity, 95% coverage: 14:501/511 of query aligns to 4:506/506 of 6chdA
- binding 5'-o-[(l-lysylamino)sulfonyl]adenosine: G207 (= G205), A229 (= A227), E231 (= E229), R253 (= R251), H261 (= H259), N262 (= N260), F265 (= F263), E269 (= E267), Y271 (= Y269), E424 (= E419), I425 (= I420), N427 (= N422), Y429 (≠ F424), E431 (= E426), G476 (= G471), G478 (= G473), G480 (= G475), R483 (= R478)
7f6wA Crystal structure of saccharomyces cerevisiae lysyl-tRNA synthetase (see paper)
41% identity, 94% coverage: 20:500/511 of query aligns to 9:506/506 of 7f6wA
- binding 5'-o-[(l-lysylamino)sulfonyl]adenosine: E232 (= E229), R254 (= R251), H262 (= H259), N263 (= N260), F266 (= F263), E270 (= E267), E425 (= E419), I426 (= I420), N428 (= N422), Y430 (≠ F424), E432 (= E426), G477 (= G471), G481 (= G475), R484 (= R478)
6kctA Crystal structure of plasmodium lysyl-tRNA synthetase in complex with a cladosporin derivative 5 (see paper)
40% identity, 95% coverage: 13:500/511 of query aligns to 2:504/506 of 6kctA
- active site: R253 (= R251), E255 (= E253), T260 (≠ R258), H261 (= H259), E423 (= E419), N426 (= N422), R482 (= R478)
- binding 3-(cyclohexylmethyl)-6,8-bis(oxidanyl)isochromen-1-one: E255 (= E253), H261 (= H259), N262 (= N260), F265 (= F263), E423 (= E419), V424 (≠ I420), L425 (≠ A421), G477 (= G473), R482 (= R478)
- binding lysine: E231 (= E229), E269 (= E267), Y271 (= Y269), N426 (= N422), Y428 (≠ F424), E430 (= E426), G475 (= G471), L476 (≠ E472), G477 (= G473)
6kabA Crystal structure of plasmodium lysyl-tRNA synthetase in complex with a cladosporin derivative 2 (see paper)
40% identity, 95% coverage: 13:500/511 of query aligns to 2:504/506 of 6kabA
- active site: R253 (= R251), E255 (= E253), T260 (≠ R258), H261 (= H259), E423 (= E419), N426 (= N422), R482 (= R478)
- binding (3~{S})-3-(cyclohexylmethyl)-6,8-bis(oxidanyl)-3,4-dihydroisochromen-1-one: E255 (= E253), H261 (= H259), N262 (= N260), F265 (= F263), E423 (= E419), V424 (≠ I420), L425 (≠ A421), N426 (= N422), G477 (= G473), R482 (= R478)
- binding lysine: E231 (= E229), E269 (= E267), Y271 (= Y269), N426 (= N422), Y428 (≠ F424), E430 (= E426), G475 (= G471), G477 (= G473)
Query Sequence
>GFF789 FitnessBrowser__Marino:GFF789
MTDQTQNAAPHEDNKLIAERRAKLSEMRDQGNAFPNDFRRDATAAELQAKYGEKTKEELE
SLGIKVAIAGRMMLDRKAFKVVQDMTGRIQIYASKDVQKDTKHWDLGDIVGVRGTLSKSG
KGDLYVTMDEYVLLTKSLRPLPEKHKGLTDTEARYRHRYVDLMVNEDSRRVFYARSKIIS
AMRQYFTDRDFMEVETPMLQVIPGGATARPFVTHHNALGIDMYLRIAPELFLKRLVVGGF
ERVFEINRNFRNEGLSTRHNPEFTMVEFYQAYADYNDLMDLTEDMLRTITQKVLGTTTVV
NSRTLADGSEETVEYDFGKTFERLTVVDAILRYNPDIKPEQLADDASARQVAKDLGIHLK
EGWGLGKVQIEIFEATAEHRLMQPTFITEYPKEVSPLARCKDSNPFVTERFEFFVGGREI
ANGFSELNDAEDQAERFQAQVAEKDAGDDEAMFYDEDYVMALEYGLPPTAGEGIGIDRLA
MLLTNSPSIRDVILFPAMRPEHKAESRKDED
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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