SitesBLAST
Comparing WP_013537761.1 NCBI__GCF_000185805.1:WP_013537761.1 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)
50% identity, 96% coverage: 12:506/517 of query aligns to 19:505/505 of P0A8N5
- K114 (= K112) modified: N6-acetyllysine
- K156 (= K155) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1bbuA Lysyl-tRNA synthetase (lyss) complexed with lysine (see paper)
50% identity, 95% coverage: 12:504/517 of query aligns to 8:486/486 of 1bbuA
- active site: R246 (= R262), E248 (= E264), R253 (= R269), H254 (= H270), E405 (= E423), N408 (= N426), R464 (= R482)
- binding lysine: G200 (= G216), E224 (= E240), E262 (= E278), Y264 (= Y280), F410 (≠ Y428), E412 (= E430), G457 (= G475), G459 (= G477)
1e24A Lysyl-tRNA synthetase (lysu) hexagonal form complexed with lysine and atp and mn2+ (see paper)
49% identity, 95% coverage: 12:504/517 of query aligns to 8:485/485 of 1e24A
- active site: R245 (= R262), E247 (= E264), R252 (= R269), H253 (= H270), E404 (= E423), N407 (= N426), R463 (= R482)
- binding adenosine-5'-triphosphate: R245 (= R262), R252 (= R269), H253 (= H270), N254 (= N271), F257 (= F274), M259 (= M276), E404 (= E423), I405 (≠ V424), G460 (= G479), R463 (= R482)
- binding lysine: G199 (= G216), E223 (= E240), E261 (= E278), Y263 (= Y280), N407 (= N426), F409 (≠ Y428), E411 (= E430), G456 (= G475), G458 (= G477)
- binding manganese (ii) ion: E397 (= E416), E404 (= E423)
1e22A Lysyl-tRNA synthetase (lysu) hexagonal form complexed with lysine and the non-hydrolysable atp analogue amp-pcp (see paper)
49% identity, 95% coverage: 12:504/517 of query aligns to 8:485/485 of 1e22A
- active site: R245 (= R262), E247 (= E264), R252 (= R269), H253 (= H270), E404 (= E423), N407 (= N426), R463 (= R482)
- binding phosphomethylphosphonic acid adenylate ester: R245 (= R262), R252 (= R269), H253 (= H270), N254 (= N271), F257 (= F274), E404 (= E423), I405 (≠ V424), G460 (= G479), R463 (= R482)
- binding lysine: G199 (= G216), E223 (= E240), M259 (= M276), E261 (= E278), Y263 (= Y280), N407 (= N426), F409 (≠ Y428), E411 (= E430), G456 (= G475), G458 (= G477)
- binding magnesium ion: E397 (= E416), E404 (= E423)
1e1tA Lysyl-tRNA synthetase (lysu) hexagonal form complexed with the lysyl_adenylate intermediate (see paper)
49% identity, 95% coverage: 12:504/517 of query aligns to 8:485/485 of 1e1tA
- active site: R245 (= R262), E247 (= E264), R252 (= R269), H253 (= H270), E404 (= E423), N407 (= N426), R463 (= R482)
- binding adenosine-5'-[lysyl-phosphate]: G199 (= G216), E223 (= E240), R245 (= R262), R252 (= R269), H253 (= H270), N254 (= N271), F257 (= F274), M259 (= M276), E261 (= E278), Y263 (= Y280), E404 (= E423), I405 (≠ V424), N407 (= N426), F409 (≠ Y428), E411 (= E430), G456 (= G475), G458 (= G477), G460 (= G479)
- binding magnesium ion: E397 (= E416), E404 (= E423)
- binding pyrophosphate 2-: H253 (= H270), E404 (= E423), R463 (= R482)
3e9iA Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with l-lysine hydroxamate-amp (see paper)
51% identity, 95% coverage: 15:503/517 of query aligns to 9:483/484 of 3e9iA
- active site: R245 (= R262), E247 (= E264), R252 (= R269), H253 (= H270), E403 (= E423), N406 (= N426), R462 (= R482)
- binding 5'-O-{(R)-hydroxy[(L-lysylamino)oxy]phosphoryl}adenosine: G199 (= G216), E223 (= E240), R245 (= R262), H253 (= H270), N254 (= N271), F257 (= F274), M259 (= M276), E261 (= E278), Y263 (= Y280), E403 (= E423), H404 (≠ V424), N406 (= N426), F408 (≠ Y428), E410 (= E430), G459 (= G479)
3e9hA Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with l-lysylsulfamoyl adenosine (see paper)
51% identity, 95% coverage: 15:503/517 of query aligns to 9:483/484 of 3e9hA
- active site: R245 (= R262), E247 (= E264), R252 (= R269), H253 (= H270), E403 (= E423), N406 (= N426), R462 (= R482)
- binding 5'-o-[(l-lysylamino)sulfonyl]adenosine: E223 (= E240), R245 (= R262), H253 (= H270), N254 (= N271), F257 (= F274), M259 (= M276), E261 (= E278), Y263 (= Y280), E403 (= E423), H404 (≠ V424), N406 (= N426), F408 (≠ Y428), E410 (= E430), G455 (= G475), G459 (= G479), R462 (= R482)
- binding magnesium ion: E396 (= E416), E403 (= E423), N406 (= N426)
3a74A Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with diadenosine tetraphosphate (ap4a)
51% identity, 95% coverage: 15:503/517 of query aligns to 9:483/484 of 3a74A
- active site: R245 (= R262), E247 (= E264), R252 (= R269), H253 (= H270), E403 (= E423), N406 (= N426), R462 (= R482)
- binding bis(adenosine)-5'-tetraphosphate: R245 (= R262), E247 (= E264), R252 (= R269), H253 (= H270), N254 (= N271), F257 (= F274), M259 (= M276), E358 (= E378), E362 (= E382), E403 (= E423), N406 (= N426), G459 (= G479), R462 (= R482)
- binding 2,6-diamino-hexanoic acid amide: G199 (= G216), E223 (= E240), M259 (= M276), E261 (= E278), Y263 (= Y280), N406 (= N426), F408 (≠ Y428), E410 (= E430)
- binding magnesium ion: E396 (= E416), E396 (= E416), E403 (= E423), E403 (= E423)
5yzxA Crystal structure of e.Coli lysu t146d mutant
49% identity, 95% coverage: 12:504/517 of query aligns to 7:484/484 of 5yzxA
- binding bis(adenosine)-5'-tetraphosphate: R244 (= R262), E246 (= E264), H252 (= H270), N253 (= N271), F256 (= F274), M258 (= M276), D358 (≠ E378), E403 (= E423), I404 (≠ V424), G459 (= G479), R462 (= R482)
- binding calcium ion: D358 (≠ E378), E396 (= E416), E396 (= E416), E403 (= E423), N406 (= N426)
1e1oA Lysyl-tRNA synthetase (lysu) hexagonal form, complexed with lysine (see paper)
49% identity, 95% coverage: 12:504/517 of query aligns to 8:484/484 of 1e1oA
- active site: R245 (= R262), E247 (= E264), H252 (= H270), E403 (= E423), N406 (= N426), R462 (= R482)
- binding lysine: G199 (= G216), E223 (= E240), E260 (= E278), Y262 (= Y280), N406 (= N426), F408 (≠ Y428), E410 (= E430), G455 (= G475), G457 (= G477)
4ex5A Crystal structure of lysyl-tRNA synthetase lysrs from burkholderia thailandensis bound to lysine (see paper)
49% identity, 96% coverage: 8:503/517 of query aligns to 1:485/486 of 4ex5A
- active site: R242 (= R262), E244 (= E264), R249 (= R269), H250 (= H270), E405 (= E423), N408 (= N426), R464 (= R482)
- binding lysine: E220 (= E240), E258 (= E278), Y260 (= Y280), F410 (≠ Y428), E412 (= E430), G457 (= G475), G459 (= G477)
6wbdB Crystal structure of lysyl-tRNA synthetase from stenotrophomonas maltophilia with bound l-lysine
48% identity, 96% coverage: 8:504/517 of query aligns to 2:485/485 of 6wbdB
4up7A Crystal structure of entamoeba histolytica lysyl-tRNA synthetase in complex with lysyl-adenylate (see paper)
46% identity, 98% coverage: 7:511/517 of query aligns to 8:514/529 of 4up7A
- active site: R258 (= R262), E260 (= E264), T265 (≠ R269), H266 (= H270), E426 (= E423), N429 (= N426), R485 (= R482)
- binding adenosine-5'-[lysyl-phosphate]: E236 (= E240), R258 (= R262), H266 (= H270), F270 (= F274), E274 (= E278), Y276 (= Y280), E426 (= E423), I427 (≠ V424), Y431 (= Y428), E433 (= E430), G478 (= G475), R485 (= R482)
4up9A Crystal structure of entamoeba histolytica lysyl-tRNA synthetase in complex with atp (see paper)
45% identity, 98% coverage: 7:511/517 of query aligns to 5:499/514 of 4up9A
- active site: R255 (= R262), E257 (= E264), T262 (≠ R269), H263 (= H270), E418 (= E423), N421 (= N426), R470 (= R482)
- binding adenosine-5'-triphosphate: R255 (= R262), T262 (≠ R269), H263 (= H270), N264 (= N271), F267 (= F274), R470 (= R482)
4upaA Crystal structure of entamoeba histolytica lysyl-tRNA synthetase in complex with amppnp (see paper)
45% identity, 98% coverage: 7:511/517 of query aligns to 5:500/515 of 4upaA
- active site: R255 (= R262), E257 (= E264), T262 (≠ R269), H263 (= H270), E419 (= E423), N422 (= N426), R471 (= R482)
- binding phosphoaminophosphonic acid-adenylate ester: R255 (= R262), H263 (= H270), N264 (= N271), F267 (= F274), R471 (= R482)
Q15046 Lysine--tRNA ligase; Lysyl-tRNA synthetase; LysRS; EC 2.7.7.-; EC 6.1.1.6 from Homo sapiens (Human) (see 16 papers)
44% identity, 96% coverage: 15:510/517 of query aligns to 80:581/597 of Q15046
- R80 (= R15) to H: in DEAPLE; uncertain significance; dbSNP:rs369114426
- V101 (= V36) mutation V->D,R,W: Disrupts interaction with AIMP2 and the multisynthase complex.
- L105 (≠ A40) to H: in CMTRIB; severely affects enzyme activity; dbSNP:rs267607194
- G189 (≠ F128) to D: in LEPID; does not rescue the developmental defects caused by KARS1 depletion in xenopus
- P200 (≠ V139) to L: in DEAPLE and LEPID; reduces interaction with AIMP2. Reduces tRNA-lysine aminoacylation
- S207 (≠ T146) 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 (= F202) to V: in DEAPLE; reduces interaction with AIMP2. Reduces tRNA-lysine aminoacylation; dbSNP:rs772410450
- G277 (= G216) binding substrate
- E301 (= E240) binding substrate
- RNE 323:325 (= RNE 262:264) binding ATP
- HN 331:332 (= HN 270:271) binding ATP
- E339 (= E278) binding substrate
- Y341 (= Y280) binding substrate
- D346 (= D285) mutation to R: Induces protein aggregation. Releases from the subunit complex.
- L350 (= L289) to H: found in a patient with hypertrophic cardiomyopathy and mild intellectual disability together with proximal muscle weakness; uncertain significance
- P390 (= P324) to R: found in a patient with hypertrophic cardiomyopathy and mild intellectual disability together with proximal muscle weakness; uncertain significance
- R438 (≠ K371) to W: in LEPID; uncertain significance; dbSNP:rs761527468
- V448 (= V381) to F: in DEAPLE; uncertain significance
- R477 (= R406) 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 (≠ EV 423:424) binding ATP
- N497 (= N426) binding substrate
- E501 (= E430) binding substrate
- P505 (= P434) to S: in DEAPLE; decreases tRNA-lysine aminoacylation; slightly induces protein aggregation; no effect on cytoplasmic location; no effect on oligomerization; dbSNP:rs1555512658
- E525 (= E454) to K: in LEPID; uncertain significance; dbSNP:rs770522582
- G540 (= G469) 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 479:482) binding ATP
- L568 (= L497) 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)
44% identity, 95% coverage: 15:505/517 of query aligns to 9:505/505 of 4ycuA
- active site: R252 (= R262), E254 (= E264), T259 (≠ R269), H260 (= H270), E423 (= E423), N426 (= N426), R482 (= R482)
- binding cladosporin: E254 (= E264), H260 (= H270), N261 (= N271), F264 (= F274), N426 (= N426), G479 (= G479), R482 (= R482)
- binding lysine: G206 (= G216), E230 (= E240), E268 (= E278), Y270 (= Y280), N426 (= N426), Y428 (= Y428), E430 (= E430), G475 (= G475)
6chdA Crystal structure of human lysyl-tRNA synthetase complexed with l- lysylsulfamoyl adenosine
44% identity, 95% coverage: 15:505/517 of query aligns to 10:506/506 of 6chdA
- binding 5'-o-[(l-lysylamino)sulfonyl]adenosine: G207 (= G216), A229 (= A238), E231 (= E240), R253 (= R262), H261 (= H270), N262 (= N271), F265 (= F274), E269 (= E278), Y271 (= Y280), E424 (= E423), I425 (≠ V424), N427 (= N426), Y429 (= Y428), E431 (= E430), G476 (= G475), G478 (= G477), G480 (= G479), R483 (= R482)
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)
44% identity, 97% coverage: 13:513/517 of query aligns to 75:589/591 of P15180
- R488 (= R414) 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
3bjuA Crystal structure of tetrameric form of human lysyl-tRNA synthetase (see paper)
44% identity, 95% coverage: 15:505/517 of query aligns to 11:503/503 of 3bjuA
- active site: R250 (= R262), E252 (= E264), T257 (≠ R269), H258 (= H270), E421 (= E423), N424 (= N426), R480 (= R482)
- binding adenosine-5'-triphosphate: R250 (= R262), H258 (= H270), N259 (= N271), F262 (= F274), E421 (= E423), G477 (= G479), R480 (= R482)
- binding calcium ion: E414 (= E416), E421 (= E423)
- binding lysine: G204 (= G216), E228 (= E240), E266 (= E278), Y268 (= Y280), N424 (= N426), Y426 (= Y428), E428 (= E430), G473 (= G475)
Query Sequence
>WP_013537761.1 NCBI__GCF_000185805.1:WP_013537761.1
MAEEKSLEHKIVEQRKEKVEKLKELGYEPYAYKFDVNAKAGELIARFGRVKSQEEREGEE
LPSQEFSLAGRIVSMRVMGKAAFFHIQDESGRLQCYIRRDTVGEEFYNKVFKRLIDIGDI
VGVKGTLFRTRTGELTLEVKELTPLTKSLRPLPEKWHGLKDTEKRYRQRYLDLIVNPEVR
EVFRTRTEVIKAIREFLDSRGFLEVETPILQPIASGAAAKPFITHYNALDIDVYLRIAPE
LYLKRLLVGGFERVYELGKNFRNEGISTRHNPEFTMVEWYMAYADYYDLMEMTEELFEFL
LDRLYGPGVREIEYQGTKISFKRPFRRISYLEELSKKTGLTPDELLHNEEKVLQKAKELE
IENAEKLSHFKRVQELFEKLVEPELIQPTFVVDFPKAISPLAKEKRGNPELVERFELFIY
GREVANAYSELNNPEEQARRFKQQLQEKARGDEEAMEYDADFVTALEYGMPPTAGEGIGI
DRLVMLFTDKDSIREVLLFPQLRPERREEKKEEVKES
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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