SitesBLAST
Comparing 16970 FitnessBrowser__Keio:16970 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)
1bbuA Lysyl-tRNA synthetase (lyss) complexed with lysine (see paper)
99% identity, 97% coverage: 12:503/505 of query aligns to 1:486/486 of 1bbuA
- active site: R246 (= R263), E248 (= E265), R253 (= R270), H254 (= H271), E405 (= E422), N408 (= N425), R464 (= R481)
- binding lysine: G200 (= G217), E224 (= E241), E262 (= E279), Y264 (= Y281), F410 (= F427), E412 (= E429), G457 (= G474), G459 (= G476)
P0A8N5 Lysine--tRNA ligase, heat inducible; Lysyl-tRNA synthetase; LysRS; EC 6.1.1.6 from Escherichia coli (strain K12) (see 2 papers)
89% identity, 100% coverage: 1:505/505 of query aligns to 1:505/505 of P0A8N5
- M1 (= M1) modified: Initiator methionine, Removed
- K114 (= K114) modified: N6-acetyllysine
- K156 (= K156) modified: N6-acetyllysine
1e24A Lysyl-tRNA synthetase (lysu) hexagonal form complexed with lysine and atp and mn2+ (see paper)
88% identity, 97% coverage: 13:503/505 of query aligns to 2:485/485 of 1e24A
- active site: R245 (= R263), E247 (= E265), R252 (= R270), H253 (= H271), E404 (= E422), N407 (= N425), R463 (= R481)
- binding adenosine-5'-triphosphate: R245 (= R263), R252 (= R270), H253 (= H271), N254 (= N272), F257 (= F275), M259 (= M277), E404 (= E422), I405 (= I423), G460 (= G478), R463 (= R481)
- binding lysine: G199 (= G217), E223 (= E241), E261 (= E279), Y263 (= Y281), N407 (= N425), F409 (= F427), E411 (= E429), G456 (= G474), G458 (= G476)
- binding manganese (ii) ion: E397 (= E415), E404 (= E422)
1e22A Lysyl-tRNA synthetase (lysu) hexagonal form complexed with lysine and the non-hydrolysable atp analogue amp-pcp (see paper)
88% identity, 97% coverage: 13:503/505 of query aligns to 2:485/485 of 1e22A
- active site: R245 (= R263), E247 (= E265), R252 (= R270), H253 (= H271), E404 (= E422), N407 (= N425), R463 (= R481)
- binding phosphomethylphosphonic acid adenylate ester: R245 (= R263), R252 (= R270), H253 (= H271), N254 (= N272), F257 (= F275), E404 (= E422), I405 (= I423), G460 (= G478), R463 (= R481)
- binding lysine: G199 (= G217), E223 (= E241), M259 (= M277), E261 (= E279), Y263 (= Y281), N407 (= N425), F409 (= F427), E411 (= E429), G456 (= G474), G458 (= G476)
- binding magnesium ion: E397 (= E415), E404 (= E422)
1e1tA Lysyl-tRNA synthetase (lysu) hexagonal form complexed with the lysyl_adenylate intermediate (see paper)
88% identity, 97% coverage: 13:503/505 of query aligns to 2:485/485 of 1e1tA
- active site: R245 (= R263), E247 (= E265), R252 (= R270), H253 (= H271), E404 (= E422), N407 (= N425), R463 (= R481)
- binding adenosine-5'-[lysyl-phosphate]: G199 (= G217), E223 (= E241), R245 (= R263), R252 (= R270), H253 (= H271), N254 (= N272), F257 (= F275), M259 (= M277), E261 (= E279), Y263 (= Y281), E404 (= E422), I405 (= I423), N407 (= N425), F409 (= F427), E411 (= E429), G456 (= G474), G458 (= G476), G460 (= G478)
- binding magnesium ion: E397 (= E415), E404 (= E422)
- binding pyrophosphate 2-: H253 (= H271), E404 (= E422), R463 (= R481)
5yzxA Crystal structure of e.Coli lysu t146d mutant
88% identity, 97% coverage: 13:503/505 of query aligns to 1:484/484 of 5yzxA
- binding bis(adenosine)-5'-tetraphosphate: R244 (= R263), E246 (= E265), H252 (= H271), N253 (= N272), F256 (= F275), M258 (= M277), D358 (≠ E377), E403 (= E422), I404 (= I423), G459 (= G478), R462 (= R481)
- binding calcium ion: D358 (≠ E377), E396 (= E415), E396 (= E415), E403 (= E422), N406 (= N425)
1e1oA Lysyl-tRNA synthetase (lysu) hexagonal form, complexed with lysine (see paper)
88% identity, 97% coverage: 13:503/505 of query aligns to 2:484/484 of 1e1oA
- active site: R245 (= R263), E247 (= E265), H252 (= H271), E403 (= E422), N406 (= N425), R462 (= R481)
- binding lysine: G199 (= G217), E223 (= E241), E260 (= E279), Y262 (= Y281), N406 (= N425), F408 (= F427), E410 (= E429), G455 (= G474), G457 (= G476)
4ex5A Crystal structure of lysyl-tRNA synthetase lysrs from burkholderia thailandensis bound to lysine (see paper)
58% identity, 96% coverage: 16:502/505 of query aligns to 2:485/486 of 4ex5A
- active site: R242 (= R263), E244 (= E265), R249 (= R270), H250 (= H271), E405 (= E422), N408 (= N425), R464 (= R481)
- binding lysine: E220 (= E241), E258 (= E279), Y260 (= Y281), F410 (= F427), E412 (= E429), G457 (= G474), G459 (= G476)
6wbdB Crystal structure of lysyl-tRNA synthetase from stenotrophomonas maltophilia with bound l-lysine
57% identity, 97% coverage: 14:503/505 of query aligns to 1:485/485 of 6wbdB
3e9iA Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with l-lysine hydroxamate-amp (see paper)
54% identity, 97% coverage: 14:502/505 of query aligns to 1:483/484 of 3e9iA
- active site: R245 (= R263), E247 (= E265), R252 (= R270), H253 (= H271), E403 (= E422), N406 (= N425), R462 (= R481)
- binding 5'-O-{(R)-hydroxy[(L-lysylamino)oxy]phosphoryl}adenosine: G199 (= G217), E223 (= E241), R245 (= R263), H253 (= H271), N254 (= N272), F257 (= F275), M259 (= M277), E261 (= E279), Y263 (= Y281), E403 (= E422), H404 (≠ I423), N406 (= N425), F408 (= F427), E410 (= E429), G459 (= G478)
3e9hA Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with l-lysylsulfamoyl adenosine (see paper)
54% identity, 97% coverage: 14:502/505 of query aligns to 1:483/484 of 3e9hA
- active site: R245 (= R263), E247 (= E265), R252 (= R270), H253 (= H271), E403 (= E422), N406 (= N425), R462 (= R481)
- binding 5'-o-[(l-lysylamino)sulfonyl]adenosine: E223 (= E241), R245 (= R263), H253 (= H271), N254 (= N272), F257 (= F275), M259 (= M277), E261 (= E279), Y263 (= Y281), E403 (= E422), H404 (≠ I423), N406 (= N425), F408 (= F427), E410 (= E429), G455 (= G474), G459 (= G478), R462 (= R481)
- binding magnesium ion: E396 (= E415), E403 (= E422), N406 (= N425)
3a74A Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with diadenosine tetraphosphate (ap4a)
54% identity, 97% coverage: 14:502/505 of query aligns to 1:483/484 of 3a74A
- active site: R245 (= R263), E247 (= E265), R252 (= R270), H253 (= H271), E403 (= E422), N406 (= N425), R462 (= R481)
- binding bis(adenosine)-5'-tetraphosphate: R245 (= R263), E247 (= E265), R252 (= R270), H253 (= H271), N254 (= N272), F257 (= F275), M259 (= M277), E358 (= E377), E362 (= E381), E403 (= E422), N406 (= N425), G459 (= G478), R462 (= R481)
- binding 2,6-diamino-hexanoic acid amide: G199 (= G217), E223 (= E241), M259 (= M277), E261 (= E279), Y263 (= Y281), N406 (= N425), F408 (= F427), E410 (= E429)
- binding magnesium ion: E396 (= E415), E396 (= E415), E403 (= E422), E403 (= E422)
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, 97% coverage: 13:503/505 of query aligns to 71:575/597 of Q15046
- R80 (= R22) to H: in DEAPLE; uncertain significance; dbSNP:rs369114426
- V101 (≠ R42) mutation V->D,R,W: Disrupts interaction with AIMP2 and the multisynthase complex.
- L105 (≠ S46) to H: in CMTRIB; severely affects enzyme activity; dbSNP:rs267607194
- G189 (≠ F129) to D: in LEPID; does not rescue the developmental defects caused by KARS1 depletion in xenopus
- P200 (≠ C140) to L: in DEAPLE and LEPID; reduces interaction with AIMP2. Reduces tRNA-lysine aminoacylation
- S207 (≠ T147) 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 (= F203) to V: in DEAPLE; reduces interaction with AIMP2. Reduces tRNA-lysine aminoacylation; dbSNP:rs772410450
- G277 (= G217) binding
- E301 (= E241) binding
- RNE 323:325 (= RNE 263:265) binding
- HN 331:332 (= HN 271:272) binding
- E339 (= E279) binding
- Y341 (= Y281) binding
- D346 (= D286) mutation to R: Induces protein aggregation. Releases from the subunit complex.
- L350 (= L290) to H: found in a patient with hypertrophic cardiomyopathy and mild intellectual disability together with proximal muscle weakness; uncertain significance
- P390 (= P323) to R: found in a patient with hypertrophic cardiomyopathy and mild intellectual disability together with proximal muscle weakness; uncertain significance
- R438 (≠ W366) to W: in LEPID; uncertain significance; dbSNP:rs761527468
- V448 (≠ F376) to F: in DEAPLE; uncertain significance
- R477 (≠ D405) 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 422:423) binding
- N497 (= N425) binding
- E501 (= E429) binding
- P505 (≠ A433) to S: in DEAPLE; decreases tRNA-lysine aminoacylation; slightly induces protein aggregation; no effect on cytoplasmic location; no effect on oligomerization; dbSNP:rs1555512658
- E525 (= E453) to K: in LEPID; uncertain significance; dbSNP:rs770522582
- G540 (= G468) 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 478:481) binding
- L568 (≠ I496) 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, 97% coverage: 13:503/505 of query aligns to 1:505/506 of 6chdA
- binding 5'-o-[(l-lysylamino)sulfonyl]adenosine: G207 (= G217), A229 (= A239), E231 (= E241), R253 (= R263), H261 (= H271), N262 (= N272), F265 (= F275), E269 (= E279), Y271 (= Y281), E424 (= E422), I425 (= I423), N427 (= N425), Y429 (≠ F427), E431 (= E429), G476 (= G474), G478 (= G476), G480 (= G478), R483 (= R481)
4ycuA Crystal structure of cladosporin in complex with human lysyl-tRNA synthetase (see paper)
43% identity, 97% coverage: 14:503/505 of query aligns to 1:504/505 of 4ycuA
- active site: R252 (= R263), E254 (= E265), T259 (≠ R270), H260 (= H271), E423 (= E422), N426 (= N425), R482 (= R481)
- binding cladosporin: E254 (= E265), H260 (= H271), N261 (= N272), F264 (= F275), N426 (= N425), G479 (= G478), R482 (= R481)
- binding lysine: G206 (= G217), E230 (= E241), E268 (= E279), Y270 (= Y281), N426 (= N425), Y428 (≠ F427), E430 (= E429), G475 (= G474)
4dpgA Crystal structure of human lysrs: p38/aimp2 complex i (see paper)
43% identity, 97% coverage: 13:503/505 of query aligns to 1:501/501 of 4dpgA
- active site: R249 (= R263), E251 (= E265), T256 (≠ R270), H257 (= H271), E420 (= E422), N423 (= N425), R479 (= R481)
- binding diphosphomethylphosphonic acid adenosyl ester: R249 (= R263), T256 (≠ R270), H257 (= H271), N258 (= N272), F261 (= F275), R479 (= R481)
- binding lysine: E227 (= E241), E265 (= E279), Y267 (= Y281), N423 (= N425), Y425 (≠ F427), E427 (= E429), G472 (= G474)
- binding magnesium ion: E413 (= E415), E420 (= E422)
3bjuA Crystal structure of tetrameric form of human lysyl-tRNA synthetase (see paper)
43% identity, 97% coverage: 13:503/505 of query aligns to 2:502/503 of 3bjuA
- active site: R250 (= R263), E252 (= E265), T257 (≠ R270), H258 (= H271), E421 (= E422), N424 (= N425), R480 (= R481)
- binding adenosine-5'-triphosphate: R250 (= R263), H258 (= H271), N259 (= N272), F262 (= F275), E421 (= E422), G477 (= G478), R480 (= R481)
- binding calcium ion: E414 (= E415), E421 (= E422)
- binding lysine: G204 (= G217), E228 (= E241), E266 (= E279), Y268 (= Y281), N424 (= N425), Y426 (≠ F427), E428 (= E429), G473 (= G474)
4ycwA Crystal structure of cladosporin in complex with plasmodium like human lysyl-tRNA synthetase mutant
43% identity, 97% coverage: 14:503/505 of query aligns to 1:501/501 of 4ycwA
- active site: R249 (= R263), E251 (= E265), T256 (≠ R270), H257 (= H271), E420 (= E422), N423 (= N425), R479 (= R481)
- binding cladosporin: R249 (= R263), E251 (= E265), H257 (= H271), N258 (= N272), F261 (= F275), E420 (= E422), I421 (= I423), C422 (≠ G424), N423 (= N425), G476 (= G478), R479 (= R481)
- binding lysine: E227 (= E241), E265 (= E279), Y267 (= Y281), N423 (= N425), Y425 (≠ F427), E427 (= E429), G472 (= G474), W473 (≠ L475)
- binding : V30 (≠ R42), S33 (≠ T45), I171 (≠ K185), S174 (= S188), T178 (≠ S192), D185 (≠ V199), E186 (≠ N200), G188 (= G202), F189 (= F203), R240 (= R254), M268 (= M282), Y270 (= Y284), A271 (= A285), D275 (= D289)
6ildB Crystal structure of human lysrs: p38/aimp2 complex ii (see paper)
43% identity, 97% coverage: 14:503/505 of query aligns to 1:499/499 of 6ildB
- active site: R247 (= R263), E249 (= E265), T254 (≠ R270), H255 (= H271), E418 (= E422), N421 (= N425), R477 (= R481)
- binding 5'-O-[(S)-hydroxy(methyl)phosphoryl]adenosine: T254 (≠ R270), H255 (= H271), F259 (= F275), E418 (= E422), R477 (= R481)
- binding lysine: G201 (= G217), E225 (= E241), E263 (= E279), Y265 (= Y281), Y423 (≠ F427), E425 (= E429), G470 (= G474), W471 (≠ L475)
- binding magnesium ion: E411 (= E415), E418 (= E422)
4up7A Crystal structure of entamoeba histolytica lysyl-tRNA synthetase in complex with lysyl-adenylate (see paper)
42% identity, 93% coverage: 36:503/505 of query aligns to 31:507/529 of 4up7A
- active site: R258 (= R263), E260 (= E265), T265 (≠ R270), H266 (= H271), E426 (= E422), N429 (= N425), R485 (= R481)
- binding adenosine-5'-[lysyl-phosphate]: E236 (= E241), R258 (= R263), H266 (= H271), F270 (= F275), E274 (= E279), Y276 (= Y281), E426 (= E422), I427 (= I423), Y431 (≠ F427), E433 (= E429), G478 (= G474), R485 (= R481)
Query Sequence
>16970 FitnessBrowser__Keio:16970
MSEQHAQGADAVVDLNNELKTRREKLANLREQGIAFPNDFRRDHTSDQLHAEFDGKENEE
LEALNIEVAVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDDLPEGVYNEQFKKWDLGD
ILGAKGKLFKTKTGELSIHCTELRLLTKALRPLPDKFHGLQDQEARYRQRYLDLISNDES
RNTFKVRSQILSGIRQFMVNRGFMEVETPMMQVIPGGAAARPFITHHNALDLDMYLRIAP
ELYLKRLVVGGFERVFEINRNFRNEGISVRHNPEFTMMELYMAYADYKDLIELTESLFRT
LAQDILGKTEVTYGDVTLDFGKPFEKLTMREAIKKYRPETDMADLDNFDSAKAIAESIGI
HVEKSWGLGRIVTEIFEEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFIGG
REIGNGFSELNDAEDQAQRFLDQVAAKDAGDDEAMFYDEDYVTALEHGLPPTAGLGIGID
RMVMLFTNSHTIRDVILFPAMRPVK
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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