SitesBLAST
Comparing WP_012673914.1 NCBI__GCF_000021545.1:WP_012673914.1 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, 76% coverage: 139:575/577 of query aligns to 67:504/505 of P0A8N5
- K114 (≠ D186) modified: N6-acetyllysine
- K156 (= K228) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3e9iA Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with l-lysine hydroxamate-amp (see paper)
52% identity, 75% coverage: 139:573/577 of query aligns to 55:483/484 of 3e9iA
- active site: R245 (= R335), E247 (= E337), R252 (≠ T342), H253 (= H343), E403 (= E493), N406 (= N496), R462 (= R552)
- binding 5'-O-{(R)-hydroxy[(L-lysylamino)oxy]phosphoryl}adenosine: G199 (= G289), E223 (= E313), R245 (= R335), H253 (= H343), N254 (= N344), F257 (= F347), M259 (= M349), E261 (= E351), Y263 (= Y353), E403 (= E493), H404 (≠ L494), N406 (= N496), F408 (≠ Y498), E410 (= E500), G459 (= G549)
3e9hA Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with l-lysylsulfamoyl adenosine (see paper)
52% identity, 75% coverage: 139:573/577 of query aligns to 55:483/484 of 3e9hA
- active site: R245 (= R335), E247 (= E337), R252 (≠ T342), H253 (= H343), E403 (= E493), N406 (= N496), R462 (= R552)
- binding 5'-o-[(l-lysylamino)sulfonyl]adenosine: E223 (= E313), R245 (= R335), H253 (= H343), N254 (= N344), F257 (= F347), M259 (= M349), E261 (= E351), Y263 (= Y353), E403 (= E493), H404 (≠ L494), N406 (= N496), F408 (≠ Y498), E410 (= E500), G455 (= G545), G459 (= G549), R462 (= R552)
- binding magnesium ion: E396 (= E486), E403 (= E493), N406 (= N496)
3a74A Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with diadenosine tetraphosphate (ap4a)
52% identity, 75% coverage: 139:573/577 of query aligns to 55:483/484 of 3a74A
- active site: R245 (= R335), E247 (= E337), R252 (≠ T342), H253 (= H343), E403 (= E493), N406 (= N496), R462 (= R552)
- binding bis(adenosine)-5'-tetraphosphate: R245 (= R335), E247 (= E337), R252 (≠ T342), H253 (= H343), N254 (= N344), F257 (= F347), M259 (= M349), E358 (= E448), E362 (= E452), E403 (= E493), N406 (= N496), G459 (= G549), R462 (= R552)
- binding 2,6-diamino-hexanoic acid amide: G199 (= G289), E223 (= E313), M259 (= M349), E261 (= E351), Y263 (= Y353), N406 (= N496), F408 (≠ Y498), E410 (= E500)
- binding magnesium ion: E396 (= E486), E396 (= E486), E403 (= E493), E403 (= E493)
1bbuA Lysyl-tRNA synthetase (lyss) complexed with lysine (see paper)
50% identity, 76% coverage: 139:574/577 of query aligns to 56:486/486 of 1bbuA
- active site: R246 (= R335), E248 (= E337), R253 (≠ T342), H254 (= H343), E405 (= E493), N408 (= N496), R464 (= R552)
- binding lysine: G200 (= G289), E224 (= E313), E262 (= E351), Y264 (= Y353), F410 (≠ Y498), E412 (= E500), G457 (= G545), G459 (= G547)
1e24A Lysyl-tRNA synthetase (lysu) hexagonal form complexed with lysine and atp and mn2+ (see paper)
50% identity, 76% coverage: 139:574/577 of query aligns to 56:485/485 of 1e24A
- active site: R245 (= R335), E247 (= E337), R252 (≠ T342), H253 (= H343), E404 (= E493), N407 (= N496), R463 (= R552)
- binding adenosine-5'-triphosphate: R245 (= R335), R252 (≠ T342), H253 (= H343), N254 (= N344), F257 (= F347), M259 (= M349), E404 (= E493), I405 (≠ L494), G460 (= G549), R463 (= R552)
- binding lysine: G199 (= G289), E223 (= E313), E261 (= E351), Y263 (= Y353), N407 (= N496), F409 (≠ Y498), E411 (= E500), G456 (= G545), G458 (= G547)
- binding manganese (ii) ion: E397 (= E486), E404 (= E493)
1e22A Lysyl-tRNA synthetase (lysu) hexagonal form complexed with lysine and the non-hydrolysable atp analogue amp-pcp (see paper)
50% identity, 76% coverage: 139:574/577 of query aligns to 56:485/485 of 1e22A
- active site: R245 (= R335), E247 (= E337), R252 (≠ T342), H253 (= H343), E404 (= E493), N407 (= N496), R463 (= R552)
- binding phosphomethylphosphonic acid adenylate ester: R245 (= R335), R252 (≠ T342), H253 (= H343), N254 (= N344), F257 (= F347), E404 (= E493), I405 (≠ L494), G460 (= G549), R463 (= R552)
- binding lysine: G199 (= G289), E223 (= E313), M259 (= M349), E261 (= E351), Y263 (= Y353), N407 (= N496), F409 (≠ Y498), E411 (= E500), G456 (= G545), G458 (= G547)
- binding magnesium ion: E397 (= E486), E404 (= E493)
1e1tA Lysyl-tRNA synthetase (lysu) hexagonal form complexed with the lysyl_adenylate intermediate (see paper)
50% identity, 76% coverage: 139:574/577 of query aligns to 56:485/485 of 1e1tA
- active site: R245 (= R335), E247 (= E337), R252 (≠ T342), H253 (= H343), E404 (= E493), N407 (= N496), R463 (= R552)
- binding adenosine-5'-[lysyl-phosphate]: G199 (= G289), E223 (= E313), R245 (= R335), R252 (≠ T342), H253 (= H343), N254 (= N344), F257 (= F347), M259 (= M349), E261 (= E351), Y263 (= Y353), E404 (= E493), I405 (≠ L494), N407 (= N496), F409 (≠ Y498), E411 (= E500), G456 (= G545), G458 (= G547), G460 (= G549)
- binding magnesium ion: E397 (= E486), E404 (= E493)
- binding pyrophosphate 2-: H253 (= H343), E404 (= E493), R463 (= R552)
5yzxA Crystal structure of e.Coli lysu t146d mutant
50% identity, 76% coverage: 139:574/577 of query aligns to 55:484/484 of 5yzxA
- binding bis(adenosine)-5'-tetraphosphate: R244 (= R335), E246 (= E337), H252 (= H343), N253 (= N344), F256 (= F347), M258 (= M349), D358 (≠ E448), E403 (= E493), I404 (≠ L494), G459 (= G549), R462 (= R552)
- binding calcium ion: D358 (≠ E448), E396 (= E486), E396 (= E486), E403 (= E493), N406 (= N496)
1e1oA Lysyl-tRNA synthetase (lysu) hexagonal form, complexed with lysine (see paper)
50% identity, 76% coverage: 139:574/577 of query aligns to 56:484/484 of 1e1oA
- active site: R245 (= R335), E247 (= E337), H252 (= H343), E403 (= E493), N406 (= N496), R462 (= R552)
- binding lysine: G199 (= G289), E223 (= E313), E260 (= E351), Y262 (= Y353), N406 (= N496), F408 (≠ Y498), E410 (= E500), G455 (= G545), G457 (= G547)
4up7A Crystal structure of entamoeba histolytica lysyl-tRNA synthetase in complex with lysyl-adenylate (see paper)
51% identity, 76% coverage: 140:575/577 of query aligns to 61:508/529 of 4up7A
- active site: R258 (= R335), E260 (= E337), T265 (= T342), H266 (= H343), E426 (= E493), N429 (= N496), R485 (= R552)
- binding adenosine-5'-[lysyl-phosphate]: E236 (= E313), R258 (= R335), H266 (= H343), F270 (= F347), E274 (= E351), Y276 (= Y353), E426 (= E493), I427 (≠ L494), Y431 (= Y498), E433 (= E500), G478 (= G545), R485 (= R552)
6wbdB Crystal structure of lysyl-tRNA synthetase from stenotrophomonas maltophilia with bound l-lysine
48% identity, 76% coverage: 137:574/577 of query aligns to 55:485/485 of 6wbdB
4up9A Crystal structure of entamoeba histolytica lysyl-tRNA synthetase in complex with atp (see paper)
51% identity, 76% coverage: 140:575/577 of query aligns to 58:493/514 of 4up9A
- active site: R255 (= R335), E257 (= E337), T262 (= T342), H263 (= H343), E418 (= E493), N421 (= N496), R470 (= R552)
- binding adenosine-5'-triphosphate: R255 (= R335), T262 (= T342), H263 (= H343), N264 (= N344), F267 (= F347), R470 (= R552)
4ex5A Crystal structure of lysyl-tRNA synthetase lysrs from burkholderia thailandensis bound to lysine (see paper)
49% identity, 75% coverage: 139:573/577 of query aligns to 53:485/486 of 4ex5A
- active site: R242 (= R335), E244 (= E337), R249 (≠ T342), H250 (= H343), E405 (= E493), N408 (= N496), R464 (= R552)
- binding lysine: E220 (= E313), E258 (= E351), Y260 (= Y353), F410 (≠ Y498), E412 (= E500), G457 (= G545), G459 (= G547)
4upaA Crystal structure of entamoeba histolytica lysyl-tRNA synthetase in complex with amppnp (see paper)
51% identity, 76% coverage: 140:575/577 of query aligns to 58:494/515 of 4upaA
- active site: R255 (= R335), E257 (= E337), T262 (= T342), H263 (= H343), E419 (= E493), N422 (= N496), R471 (= R552)
- binding phosphoaminophosphonic acid-adenylate ester: R255 (= R335), H263 (= H343), N264 (= N344), F267 (= F347), R471 (= R552)
Q15046 Lysine--tRNA ligase; Lysyl-tRNA synthetase; LysRS; EC 2.7.7.-; EC 6.1.1.6 from Homo sapiens (Human) (see 16 papers)
48% identity, 75% coverage: 142:575/577 of query aligns to 128:576/597 of Q15046
- G189 (≠ F201) to D: in LEPID; does not rescue the developmental defects caused by KARS1 depletion in xenopus
- P200 (≠ V212) to L: in DEAPLE and LEPID; reduces interaction with AIMP2. Reduces tRNA-lysine aminoacylation
- S207 (= S219) 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 (= F275) to V: in DEAPLE; reduces interaction with AIMP2. Reduces tRNA-lysine aminoacylation; dbSNP:rs772410450
- G277 (= G289) binding substrate
- E301 (= E313) binding substrate
- RNE 323:325 (= RNE 335:337) binding ATP
- HN 331:332 (= HN 343:344) binding ATP
- E339 (= E351) binding substrate
- Y341 (= Y353) binding substrate
- D346 (= D358) mutation to R: Induces protein aggregation. Releases from the subunit complex.
- L350 (= L362) to H: found in a patient with hypertrophic cardiomyopathy and mild intellectual disability together with proximal muscle weakness; uncertain significance
- P390 (= P395) to R: found in a patient with hypertrophic cardiomyopathy and mild intellectual disability together with proximal muscle weakness; uncertain significance
- R438 (vs. gap) to W: in LEPID; uncertain significance; dbSNP:rs761527468
- V448 (≠ F447) to F: in DEAPLE; uncertain significance
- R477 (= R476) 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 493:494) binding ATP
- N497 (= N496) binding substrate
- E501 (= E500) binding substrate
- P505 (= P504) to S: in DEAPLE; decreases tRNA-lysine aminoacylation; slightly induces protein aggregation; no effect on cytoplasmic location; no effect on oligomerization; dbSNP:rs1555512658
- E525 (= E524) to K: in LEPID; uncertain significance; dbSNP:rs770522582
- G540 (= G539) 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 549:552) binding ATP
- L568 (≠ I567) 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
- 80 R → H: in DEAPLE; uncertain significance; dbSNP:rs369114426
- 101 mutation V->D,R,W: Disrupts interaction with AIMP2 and the multisynthase complex.
- 105 L → H: in CMTRIB; severely affects enzyme activity; dbSNP:rs267607194
- 595 T → S: in dbSNP:rs6834
4ycuA Crystal structure of cladosporin in complex with human lysyl-tRNA synthetase (see paper)
48% identity, 75% coverage: 142:575/577 of query aligns to 57:505/505 of 4ycuA
- active site: R252 (= R335), E254 (= E337), T259 (= T342), H260 (= H343), E423 (= E493), N426 (= N496), R482 (= R552)
- binding cladosporin: E254 (= E337), H260 (= H343), N261 (= N344), F264 (= F347), N426 (= N496), G479 (= G549), R482 (= R552)
- binding lysine: G206 (= G289), E230 (= E313), E268 (= E351), Y270 (= Y353), N426 (= N496), Y428 (= Y498), E430 (= E500), G475 (= G545)
6chdA Crystal structure of human lysyl-tRNA synthetase complexed with l- lysylsulfamoyl adenosine
48% identity, 75% coverage: 142:575/577 of query aligns to 58:506/506 of 6chdA
- binding 5'-o-[(l-lysylamino)sulfonyl]adenosine: G207 (= G289), A229 (= A311), E231 (= E313), R253 (= R335), H261 (= H343), N262 (= N344), F265 (= F347), E269 (= E351), Y271 (= Y353), E424 (= E493), I425 (≠ L494), N427 (= N496), Y429 (= Y498), E431 (= E500), G476 (= G545), G478 (= G547), G480 (= G549), R483 (= R552)
3bjuA Crystal structure of tetrameric form of human lysyl-tRNA synthetase (see paper)
48% identity, 75% coverage: 142:575/577 of query aligns to 59:503/503 of 3bjuA
- active site: R250 (= R335), E252 (= E337), T257 (= T342), H258 (= H343), E421 (= E493), N424 (= N496), R480 (= R552)
- binding adenosine-5'-triphosphate: R250 (= R335), H258 (= H343), N259 (= N344), F262 (= F347), E421 (= E493), G477 (= G549), R480 (= R552)
- binding calcium ion: E414 (= E486), E421 (= E493)
- binding lysine: G204 (= G289), E228 (= E313), E266 (= E351), Y268 (= Y353), N424 (= N496), Y426 (= Y498), E428 (= E500), G473 (= G545)
4dpgA Crystal structure of human lysrs: p38/aimp2 complex i (see paper)
48% identity, 75% coverage: 142:574/577 of query aligns to 58:501/501 of 4dpgA
- active site: R249 (= R335), E251 (= E337), T256 (= T342), H257 (= H343), E420 (= E493), N423 (= N496), R479 (= R552)
- binding diphosphomethylphosphonic acid adenosyl ester: R249 (= R335), T256 (= T342), H257 (= H343), N258 (= N344), F261 (= F347), R479 (= R552)
- binding lysine: E227 (= E313), E265 (= E351), Y267 (= Y353), N423 (= N496), Y425 (= Y498), E427 (= E500), G472 (= G545)
- binding magnesium ion: E413 (= E486), E420 (= E493)
Query Sequence
>WP_012673914.1 NCBI__GCF_000021545.1:WP_012673914.1
MSEEILESRLERLKKMEKEGINPYPHKFETTHTLKSVREGLEFEPEDKEVILKGKIKRVS
KKDNDYVIRFEDLNGHSEILVIFPQKEKLSPNTVASFKGKLKRVDGKLTLIADEVYFEEK
GEDVSKVKQLYDKDPEGKEVAVAGRLVALRDQGKAAFGHLQDADGKLQIYFNADILGQEN
YQKAMDLIDIGDIVGVKGKLFRTMTGELTVEVHSYQILSKSLRPLPEKWHGLRDVEERYR
YRFLDLIANQRSREIFKLRSKAIKSLREFLESKGFIEVETPILQPVASGALAKPFITYHN
ALDMNLYLRIAPELYLKMLVVGGFNRVFEIGRNFRNEGIDTTHNPEFTMVEFYAAYLDYN
DLMALTEELFRKILLDTVGTLKIKWEDQEIDFEKPFRRLPFFEALKQKTGKDKEFFLDYE
KAKNFAKEVGIPKADTLTHMKILDKLFEHFVEEDLVQPTFVIDFPKILSPLAKTHRNDPD
LVERFELIINKQELANAYTELNDPFDQRERFIQQIREKEMGDEEAMDVDETFLTALEYGL
PPTAGEGIGIDRLVMMLTDSVSIREVILFPTLRPEGS
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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