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Comparing WP_010959665.1 NCBI__GCF_000008325.1:WP_010959665.1 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)
63% identity, 100% coverage: 2:495/496 of query aligns to 10:504/505 of P0A8N5
- K114 (= K105) modified: N6-acetyllysine
- K156 (= K147) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1bbuA Lysyl-tRNA synthetase (lyss) complexed with lysine (see paper)
63% identity, 99% coverage: 6:494/496 of query aligns to 3:486/486 of 1bbuA
- active site: R246 (= R254), E248 (= E256), R253 (= R261), H254 (= H262), E405 (= E413), N408 (= N416), R464 (= R472)
- binding lysine: G200 (= G208), E224 (= E232), E262 (= E270), Y264 (= Y272), F410 (= F418), E412 (= E420), G457 (= G465), G459 (= G467)
1e24A Lysyl-tRNA synthetase (lysu) hexagonal form complexed with lysine and atp and mn2+ (see paper)
62% identity, 99% coverage: 6:494/496 of query aligns to 3:485/485 of 1e24A
- active site: R245 (= R254), E247 (= E256), R252 (= R261), H253 (= H262), E404 (= E413), N407 (= N416), R463 (= R472)
- binding adenosine-5'-triphosphate: R245 (= R254), R252 (= R261), H253 (= H262), N254 (= N263), F257 (= F266), M259 (= M268), E404 (= E413), I405 (≠ L414), G460 (= G469), R463 (= R472)
- binding lysine: G199 (= G208), E223 (= E232), E261 (= E270), Y263 (= Y272), N407 (= N416), F409 (= F418), E411 (= E420), G456 (= G465), G458 (= G467)
- binding manganese (ii) ion: E397 (= E406), E404 (= E413)
1e22A Lysyl-tRNA synthetase (lysu) hexagonal form complexed with lysine and the non-hydrolysable atp analogue amp-pcp (see paper)
62% identity, 99% coverage: 6:494/496 of query aligns to 3:485/485 of 1e22A
- active site: R245 (= R254), E247 (= E256), R252 (= R261), H253 (= H262), E404 (= E413), N407 (= N416), R463 (= R472)
- binding phosphomethylphosphonic acid adenylate ester: R245 (= R254), R252 (= R261), H253 (= H262), N254 (= N263), F257 (= F266), E404 (= E413), I405 (≠ L414), G460 (= G469), R463 (= R472)
- binding lysine: G199 (= G208), E223 (= E232), M259 (= M268), E261 (= E270), Y263 (= Y272), N407 (= N416), F409 (= F418), E411 (= E420), G456 (= G465), G458 (= G467)
- binding magnesium ion: E397 (= E406), E404 (= E413)
1e1tA Lysyl-tRNA synthetase (lysu) hexagonal form complexed with the lysyl_adenylate intermediate (see paper)
62% identity, 99% coverage: 6:494/496 of query aligns to 3:485/485 of 1e1tA
- active site: R245 (= R254), E247 (= E256), R252 (= R261), H253 (= H262), E404 (= E413), N407 (= N416), R463 (= R472)
- binding adenosine-5'-[lysyl-phosphate]: G199 (= G208), E223 (= E232), R245 (= R254), R252 (= R261), H253 (= H262), N254 (= N263), F257 (= F266), M259 (= M268), E261 (= E270), Y263 (= Y272), E404 (= E413), I405 (≠ L414), N407 (= N416), F409 (= F418), E411 (= E420), G456 (= G465), G458 (= G467), G460 (= G469)
- binding magnesium ion: E397 (= E406), E404 (= E413)
- binding pyrophosphate 2-: H253 (= H262), E404 (= E413), R463 (= R472)
5yzxA Crystal structure of e.Coli lysu t146d mutant
62% identity, 99% coverage: 6:494/496 of query aligns to 2:484/484 of 5yzxA
- binding bis(adenosine)-5'-tetraphosphate: R244 (= R254), E246 (= E256), H252 (= H262), N253 (= N263), F256 (= F266), M258 (= M268), D358 (≠ E368), E403 (= E413), I404 (≠ L414), G459 (= G469), R462 (= R472)
- binding calcium ion: D358 (≠ E368), E396 (= E406), E396 (= E406), E403 (= E413), N406 (= N416)
1e1oA Lysyl-tRNA synthetase (lysu) hexagonal form, complexed with lysine (see paper)
62% identity, 99% coverage: 6:494/496 of query aligns to 3:484/484 of 1e1oA
- active site: R245 (= R254), E247 (= E256), H252 (= H262), E403 (= E413), N406 (= N416), R462 (= R472)
- binding lysine: G199 (= G208), E223 (= E232), E260 (= E270), Y262 (= Y272), N406 (= N416), F408 (= F418), E410 (= E420), G455 (= G465), G457 (= G467)
6wbdB Crystal structure of lysyl-tRNA synthetase from stenotrophomonas maltophilia with bound l-lysine
63% identity, 99% coverage: 6:494/496 of query aligns to 1:485/485 of 6wbdB
4ex5A Crystal structure of lysyl-tRNA synthetase lysrs from burkholderia thailandensis bound to lysine (see paper)
57% identity, 98% coverage: 7:493/496 of query aligns to 1:485/486 of 4ex5A
- active site: R242 (= R254), E244 (= E256), R249 (= R261), H250 (= H262), E405 (= E413), N408 (= N416), R464 (= R472)
- binding lysine: E220 (= E232), E258 (= E270), Y260 (= Y272), F410 (= F418), E412 (= E420), G457 (= G465), G459 (= G467)
3e9iA Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with l-lysine hydroxamate-amp (see paper)
53% identity, 98% coverage: 8:493/496 of query aligns to 3:483/484 of 3e9iA
- active site: R245 (= R254), E247 (= E256), R252 (= R261), H253 (= H262), E403 (= E413), N406 (= N416), R462 (= R472)
- binding 5'-O-{(R)-hydroxy[(L-lysylamino)oxy]phosphoryl}adenosine: G199 (= G208), E223 (= E232), R245 (= R254), H253 (= H262), N254 (= N263), F257 (= F266), M259 (= M268), E261 (= E270), Y263 (= Y272), E403 (= E413), H404 (≠ L414), N406 (= N416), F408 (= F418), E410 (= E420), G459 (= G469)
3e9hA Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with l-lysylsulfamoyl adenosine (see paper)
53% identity, 98% coverage: 8:493/496 of query aligns to 3:483/484 of 3e9hA
- active site: R245 (= R254), E247 (= E256), R252 (= R261), H253 (= H262), E403 (= E413), N406 (= N416), R462 (= R472)
- binding 5'-o-[(l-lysylamino)sulfonyl]adenosine: E223 (= E232), R245 (= R254), H253 (= H262), N254 (= N263), F257 (= F266), M259 (= M268), E261 (= E270), Y263 (= Y272), E403 (= E413), H404 (≠ L414), N406 (= N416), F408 (= F418), E410 (= E420), G455 (= G465), G459 (= G469), R462 (= R472)
- binding magnesium ion: E396 (= E406), E403 (= E413), N406 (= N416)
3a74A Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with diadenosine tetraphosphate (ap4a)
53% identity, 98% coverage: 8:493/496 of query aligns to 3:483/484 of 3a74A
- active site: R245 (= R254), E247 (= E256), R252 (= R261), H253 (= H262), E403 (= E413), N406 (= N416), R462 (= R472)
- binding bis(adenosine)-5'-tetraphosphate: R245 (= R254), E247 (= E256), R252 (= R261), H253 (= H262), N254 (= N263), F257 (= F266), M259 (= M268), E358 (= E368), E362 (= E372), E403 (= E413), N406 (= N416), G459 (= G469), R462 (= R472)
- binding 2,6-diamino-hexanoic acid amide: G199 (= G208), E223 (= E232), M259 (= M268), E261 (= E270), Y263 (= Y272), N406 (= N416), F408 (= F418), E410 (= E420)
- binding magnesium ion: E396 (= E406), E396 (= E406), E403 (= E413), E403 (= E413)
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, 99% coverage: 6:495/496 of query aligns to 72:576/597 of Q15046
- R80 (= R14) to H: in DEAPLE; uncertain significance; dbSNP:rs369114426
- V101 (≠ R34) mutation V->D,R,W: Disrupts interaction with AIMP2 and the multisynthase complex.
- L105 (≠ A38) to H: in CMTRIB; severely affects enzyme activity; dbSNP:rs267607194
- G189 (≠ F120) to D: in LEPID; does not rescue the developmental defects caused by KARS1 depletion in xenopus
- P200 (≠ A131) to L: in DEAPLE and LEPID; reduces interaction with AIMP2. Reduces tRNA-lysine aminoacylation
- S207 (≠ T138) 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 (= F194) to V: in DEAPLE; reduces interaction with AIMP2. Reduces tRNA-lysine aminoacylation; dbSNP:rs772410450
- G277 (= G208) binding substrate
- E301 (= E232) binding substrate
- RNE 323:325 (= RNE 254:256) binding ATP
- HN 331:332 (= HN 262:263) binding ATP
- E339 (= E270) binding substrate
- Y341 (= Y272) binding substrate
- D346 (= D277) mutation to R: Induces protein aggregation. Releases from the subunit complex.
- L350 (= L281) to H: found in a patient with hypertrophic cardiomyopathy and mild intellectual disability together with proximal muscle weakness; uncertain significance
- P390 (= P314) to R: found in a patient with hypertrophic cardiomyopathy and mild intellectual disability together with proximal muscle weakness; uncertain significance
- R438 (≠ K361) to W: in LEPID; uncertain significance; dbSNP:rs761527468
- V448 (= V371) to F: in DEAPLE; uncertain significance
- R477 (≠ D396) 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 (≠ EL 413:414) binding ATP
- N497 (= N416) binding substrate
- E501 (= E420) binding substrate
- P505 (= P424) to S: in DEAPLE; decreases tRNA-lysine aminoacylation; slightly induces protein aggregation; no effect on cytoplasmic location; no effect on oligomerization; dbSNP:rs1555512658
- E525 (= E444) to K: in LEPID; uncertain significance; dbSNP:rs770522582
- G540 (= G459) 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 469:472) binding ATP
- L568 (≠ I487) 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)
43% identity, 99% coverage: 6:495/496 of query aligns to 1:505/505 of 4ycuA
- active site: R252 (= R254), E254 (= E256), T259 (≠ R261), H260 (= H262), E423 (= E413), N426 (= N416), R482 (= R472)
- binding cladosporin: E254 (= E256), H260 (= H262), N261 (= N263), F264 (= F266), N426 (= N416), G479 (= G469), R482 (= R472)
- binding lysine: G206 (= G208), E230 (= E232), E268 (= E270), Y270 (= Y272), N426 (= N416), Y428 (≠ F418), E430 (= E420), G475 (= G465)
6chdA Crystal structure of human lysyl-tRNA synthetase complexed with l- lysylsulfamoyl adenosine
43% identity, 99% coverage: 6:495/496 of query aligns to 2:506/506 of 6chdA
- binding 5'-o-[(l-lysylamino)sulfonyl]adenosine: G207 (= G208), A229 (= A230), E231 (= E232), R253 (= R254), H261 (= H262), N262 (= N263), F265 (= F266), E269 (= E270), Y271 (= Y272), E424 (= E413), I425 (≠ L414), N427 (= N416), Y429 (≠ F418), E431 (= E420), G476 (= G465), G478 (= G467), G480 (= G469), R483 (= R472)
3bjuA Crystal structure of tetrameric form of human lysyl-tRNA synthetase (see paper)
42% identity, 99% coverage: 6:495/496 of query aligns to 3:503/503 of 3bjuA
- active site: R250 (= R254), E252 (= E256), T257 (≠ R261), H258 (= H262), E421 (= E413), N424 (= N416), R480 (= R472)
- binding adenosine-5'-triphosphate: R250 (= R254), H258 (= H262), N259 (= N263), F262 (= F266), E421 (= E413), G477 (= G469), R480 (= R472)
- binding calcium ion: E414 (= E406), E421 (= E413)
- binding lysine: G204 (= G208), E228 (= E232), E266 (= E270), Y268 (= Y272), N424 (= N416), Y426 (≠ F418), E428 (= E420), G473 (= G465)
4dpgA Crystal structure of human lysrs: p38/aimp2 complex i (see paper)
42% identity, 99% coverage: 6:494/496 of query aligns to 2:501/501 of 4dpgA
- active site: R249 (= R254), E251 (= E256), T256 (≠ R261), H257 (= H262), E420 (= E413), N423 (= N416), R479 (= R472)
- binding diphosphomethylphosphonic acid adenosyl ester: R249 (= R254), T256 (≠ R261), H257 (= H262), N258 (= N263), F261 (= F266), R479 (= R472)
- binding lysine: E227 (= E232), E265 (= E270), Y267 (= Y272), N423 (= N416), Y425 (≠ F418), E427 (= E420), G472 (= G465)
- binding magnesium ion: E413 (= E406), E420 (= E413)
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, 99% coverage: 6:495/496 of query aligns to 69:579/591 of P15180
- R488 (= R404) 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
4ycwA Crystal structure of cladosporin in complex with plasmodium like human lysyl-tRNA synthetase mutant
42% identity, 99% coverage: 6:494/496 of query aligns to 1:501/501 of 4ycwA
- active site: R249 (= R254), E251 (= E256), T256 (≠ R261), H257 (= H262), E420 (= E413), N423 (= N416), R479 (= R472)
- binding cladosporin: R249 (= R254), E251 (= E256), H257 (= H262), N258 (= N263), F261 (= F266), E420 (= E413), I421 (≠ L414), C422 (≠ A415), N423 (= N416), G476 (= G469), R479 (= R472)
- binding lysine: E227 (= E232), E265 (= E270), Y267 (= Y272), N423 (= N416), Y425 (≠ F418), E427 (= E420), G472 (= G465), W473 (≠ E466)
- binding : V30 (≠ R34), S33 (≠ L37), I171 (≠ Q176), S174 (= S179), T178 (≠ R183), D185 (≠ S190), E186 (= E191), G188 (= G193), F189 (= F194), R240 (≠ K245), M268 (≠ Q273), Y270 (= Y275), A271 (= A276), D275 (= D280)
6ildB Crystal structure of human lysrs: p38/aimp2 complex ii (see paper)
42% identity, 99% coverage: 6:494/496 of query aligns to 1:499/499 of 6ildB
- active site: R247 (= R254), E249 (= E256), T254 (≠ R261), H255 (= H262), E418 (= E413), N421 (= N416), R477 (= R472)
- binding 5'-O-[(S)-hydroxy(methyl)phosphoryl]adenosine: T254 (≠ R261), H255 (= H262), F259 (= F266), E418 (= E413), R477 (= R472)
- binding lysine: G201 (= G208), E225 (= E232), E263 (= E270), Y265 (= Y272), Y423 (≠ F418), E425 (= E420), G470 (= G465), W471 (≠ E466)
- binding magnesium ion: E411 (= E406), E418 (= E413)
Query Sequence
>WP_010959665.1 NCBI__GCF_000008325.1:WP_010959665.1
MSELQDENKLVALRREKLGKLRQTGVAFPNDFRRDALAAELRARYGDETAEALEETAVSV
KLAGRLMGKRIMGKASFAHIQDMSGRIQIFLQRDGLAEGVYEEFKSWDIGDVIGVEGTVF
RTKTGELSVKASNIRLLTKSLRPLPEKFHGLTDAETRYRQRYLDLLMNEESRRVFQLRSA
IVRYIRDFLSERGFIEAETPMMQVIPGGARAKPFVTHHNALGLDLYLRIAPELYLKRLVV
GGFEKVFEINRSFRNEGLSTRHNPEFTMIEFYQAYADYRDLMDLTETLMRGIAQNLLGGT
VVTHQGKDYDLGRPFRRMTVLESIIHYNPDIRAEDLAERESAAAIAAGLGIPVAAGDGLG
KIQTEIFEKTVEDRLDEPTFITAYPAEVSPLARRNDENPFITDRFEFFVGGRELANGFSE
LNDPEDQAERFRKQVEDKAAGDEEAMHYDADYIRALEYGLPPTAGEGIGIDRLVMFFTDS
PSIRDVILFPHMRPES
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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