SitesBLAST
Comparing WP_084276583.1 NCBI__GCF_900176045.1:WP_084276583.1 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)
53% identity, 97% coverage: 8:493/503 of query aligns to 20:503/505 of P0A8N5
- K114 (= K104) modified: N6-acetyllysine
- K156 (= K146) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1e24A Lysyl-tRNA synthetase (lysu) hexagonal form complexed with lysine and atp and mn2+ (see paper)
52% identity, 97% coverage: 8:493/503 of query aligns to 9:485/485 of 1e24A
- active site: R245 (= R253), E247 (= E255), R252 (≠ T260), H253 (= H261), E404 (= E413), N407 (= N416), R463 (= R471)
- binding adenosine-5'-triphosphate: R245 (= R253), R252 (≠ T260), H253 (= H261), N254 (= N262), F257 (= F265), M259 (= M267), E404 (= E413), I405 (= I414), G460 (= G468), R463 (= R471)
- binding lysine: G199 (= G207), E223 (= E231), E261 (= E269), Y263 (= Y271), N407 (= N416), F409 (= F418), E411 (= E420), G456 (= G464), G458 (= G466)
- 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)
52% identity, 97% coverage: 8:493/503 of query aligns to 9:485/485 of 1e22A
- active site: R245 (= R253), E247 (= E255), R252 (≠ T260), H253 (= H261), E404 (= E413), N407 (= N416), R463 (= R471)
- binding phosphomethylphosphonic acid adenylate ester: R245 (= R253), R252 (≠ T260), H253 (= H261), N254 (= N262), F257 (= F265), E404 (= E413), I405 (= I414), G460 (= G468), R463 (= R471)
- binding lysine: G199 (= G207), E223 (= E231), M259 (= M267), E261 (= E269), Y263 (= Y271), N407 (= N416), F409 (= F418), E411 (= E420), G456 (= G464), G458 (= G466)
- binding magnesium ion: E397 (= E406), E404 (= E413)
1e1tA Lysyl-tRNA synthetase (lysu) hexagonal form complexed with the lysyl_adenylate intermediate (see paper)
52% identity, 97% coverage: 8:493/503 of query aligns to 9:485/485 of 1e1tA
- active site: R245 (= R253), E247 (= E255), R252 (≠ T260), H253 (= H261), E404 (= E413), N407 (= N416), R463 (= R471)
- binding adenosine-5'-[lysyl-phosphate]: G199 (= G207), E223 (= E231), R245 (= R253), R252 (≠ T260), H253 (= H261), N254 (= N262), F257 (= F265), M259 (= M267), E261 (= E269), Y263 (= Y271), E404 (= E413), I405 (= I414), N407 (= N416), F409 (= F418), E411 (= E420), G456 (= G464), G458 (= G466), G460 (= G468)
- binding magnesium ion: E397 (= E406), E404 (= E413)
- binding pyrophosphate 2-: H253 (= H261), E404 (= E413), R463 (= R471)
5yzxA Crystal structure of e.Coli lysu t146d mutant
52% identity, 97% coverage: 8:493/503 of query aligns to 8:484/484 of 5yzxA
- binding bis(adenosine)-5'-tetraphosphate: R244 (= R253), E246 (= E255), H252 (= H261), N253 (= N262), F256 (= F265), M258 (= M267), D358 (= D368), E403 (= E413), I404 (= I414), G459 (= G468), R462 (= R471)
- binding calcium ion: D358 (= D368), E396 (= E406), E396 (= E406), E403 (= E413), N406 (= N416)
1e1oA Lysyl-tRNA synthetase (lysu) hexagonal form, complexed with lysine (see paper)
52% identity, 97% coverage: 8:493/503 of query aligns to 9:484/484 of 1e1oA
- active site: R245 (= R253), E247 (= E255), H252 (= H261), E403 (= E413), N406 (= N416), R462 (= R471)
- binding lysine: G199 (= G207), E223 (= E231), E260 (= E269), Y262 (= Y271), N406 (= N416), F408 (= F418), E410 (= E420), G455 (= G464), G457 (= G466)
1bbuA Lysyl-tRNA synthetase (lyss) complexed with lysine (see paper)
52% identity, 97% coverage: 4:493/503 of query aligns to 5:486/486 of 1bbuA
- active site: R246 (= R253), E248 (= E255), R253 (≠ T260), H254 (= H261), E405 (= E413), N408 (= N416), R464 (= R471)
- binding lysine: G200 (= G207), E224 (= E231), E262 (= E269), Y264 (= Y271), F410 (= F418), E412 (= E420), G457 (= G464), G459 (= G466)
3e9iA Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with l-lysine hydroxamate-amp (see paper)
49% identity, 96% coverage: 8:492/503 of query aligns to 10:483/484 of 3e9iA
- active site: R245 (= R253), E247 (= E255), R252 (≠ T260), H253 (= H261), E403 (= E413), N406 (= N416), R462 (= R471)
- binding 5'-O-{(R)-hydroxy[(L-lysylamino)oxy]phosphoryl}adenosine: G199 (= G207), E223 (= E231), R245 (= R253), H253 (= H261), N254 (= N262), F257 (= F265), M259 (= M267), E261 (= E269), Y263 (= Y271), E403 (= E413), H404 (≠ I414), N406 (= N416), F408 (= F418), E410 (= E420), G459 (= G468)
3e9hA Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with l-lysylsulfamoyl adenosine (see paper)
49% identity, 96% coverage: 8:492/503 of query aligns to 10:483/484 of 3e9hA
- active site: R245 (= R253), E247 (= E255), R252 (≠ T260), H253 (= H261), E403 (= E413), N406 (= N416), R462 (= R471)
- binding 5'-o-[(l-lysylamino)sulfonyl]adenosine: E223 (= E231), R245 (= R253), H253 (= H261), N254 (= N262), F257 (= F265), M259 (= M267), E261 (= E269), Y263 (= Y271), E403 (= E413), H404 (≠ I414), N406 (= N416), F408 (= F418), E410 (= E420), G455 (= G464), G459 (= G468), R462 (= R471)
- binding magnesium ion: E396 (= E406), E403 (= E413), N406 (= N416)
3a74A Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with diadenosine tetraphosphate (ap4a)
49% identity, 96% coverage: 8:492/503 of query aligns to 10:483/484 of 3a74A
- active site: R245 (= R253), E247 (= E255), R252 (≠ T260), H253 (= H261), E403 (= E413), N406 (= N416), R462 (= R471)
- binding bis(adenosine)-5'-tetraphosphate: R245 (= R253), E247 (= E255), R252 (≠ T260), H253 (= H261), N254 (= N262), F257 (= F265), M259 (= M267), E358 (≠ D368), E362 (= E372), E403 (= E413), N406 (= N416), G459 (= G468), R462 (= R471)
- binding 2,6-diamino-hexanoic acid amide: G199 (= G207), E223 (= E231), M259 (= M267), E261 (= E269), Y263 (= Y271), N406 (= N416), F408 (= F418), E410 (= E420)
- binding magnesium ion: E396 (= E406), E396 (= E406), E403 (= E413), E403 (= E413)
4ex5A Crystal structure of lysyl-tRNA synthetase lysrs from burkholderia thailandensis bound to lysine (see paper)
48% identity, 97% coverage: 3:492/503 of query aligns to 1:485/486 of 4ex5A
- active site: R242 (= R253), E244 (= E255), R249 (≠ T260), H250 (= H261), E405 (= E413), N408 (= N416), R464 (= R471)
- binding lysine: E220 (= E231), E258 (= E269), Y260 (= Y271), F410 (= F418), E412 (= E420), G457 (= G464), G459 (= G466)
6wbdB Crystal structure of lysyl-tRNA synthetase from stenotrophomonas maltophilia with bound l-lysine
46% identity, 98% coverage: 3:493/503 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)
42% identity, 100% coverage: 1:503/503 of query aligns to 7:517/529 of 4up7A
- active site: R258 (= R253), E260 (= E255), T265 (= T260), H266 (= H261), E426 (= E413), N429 (= N416), R485 (= R471)
- binding adenosine-5'-[lysyl-phosphate]: E236 (= E231), R258 (= R253), H266 (= H261), F270 (= F265), E274 (= E269), Y276 (= Y271), E426 (= E413), I427 (= I414), Y431 (≠ F418), E433 (= E420), G478 (= G464), R485 (= R471)
4up9A Crystal structure of entamoeba histolytica lysyl-tRNA synthetase in complex with atp (see paper)
42% identity, 100% coverage: 1:503/503 of query aligns to 4:502/514 of 4up9A
- active site: R255 (= R253), E257 (= E255), T262 (= T260), H263 (= H261), E418 (= E413), N421 (= N416), R470 (= R471)
- binding adenosine-5'-triphosphate: R255 (= R253), T262 (= T260), H263 (= H261), N264 (= N262), F267 (= F265), R470 (= R471)
4upaA Crystal structure of entamoeba histolytica lysyl-tRNA synthetase in complex with amppnp (see paper)
42% identity, 100% coverage: 1:503/503 of query aligns to 4:503/515 of 4upaA
- active site: R255 (= R253), E257 (= E255), T262 (= T260), H263 (= H261), E419 (= E413), N422 (= N416), R471 (= R471)
- binding phosphoaminophosphonic acid-adenylate ester: R255 (= R253), H263 (= H261), N264 (= N262), F267 (= F265), R471 (= R471)
Q15046 Lysine--tRNA ligase; Lysyl-tRNA synthetase; LysRS; EC 2.7.7.-; EC 6.1.1.6 from Homo sapiens (Human) (see 16 papers)
42% identity, 98% coverage: 4:498/503 of query aligns to 74:580/597 of Q15046
- R80 (= R10) to H: in DEAPLE; uncertain significance; dbSNP:rs369114426
- V101 (≠ K31) mutation V->D,R,W: Disrupts interaction with AIMP2 and the multisynthase complex.
- L105 (≠ N35) to H: in CMTRIB; severely affects enzyme activity; dbSNP:rs267607194
- G189 (≠ F119) to D: in LEPID; does not rescue the developmental defects caused by KARS1 depletion in xenopus
- P200 (≠ A130) to L: in DEAPLE and LEPID; reduces interaction with AIMP2. Reduces tRNA-lysine aminoacylation
- S207 (≠ T137) 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 (= F193) to V: in DEAPLE; reduces interaction with AIMP2. Reduces tRNA-lysine aminoacylation; dbSNP:rs772410450
- G277 (= G207) binding
- E301 (= E231) binding
- RNE 323:325 (= RNE 253:255) binding
- HN 331:332 (= HN 261:262) binding
- E339 (= E269) binding
- Y341 (= Y271) binding
- D346 (≠ T276) mutation to R: Induces protein aggregation. Releases from the subunit complex.
- L350 (= L280) to H: found in a patient with hypertrophic cardiomyopathy and mild intellectual disability together with proximal muscle weakness; uncertain significance
- P390 (= P313) to R: found in a patient with hypertrophic cardiomyopathy and mild intellectual disability together with proximal muscle weakness; uncertain significance
- R438 (≠ M357) to W: in LEPID; uncertain significance; dbSNP:rs761527468
- V448 (≠ F367) 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 (= EI 413:414) binding
- N497 (= N416) binding
- E501 (= E420) binding
- 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 (= E443) to K: in LEPID; uncertain significance; dbSNP:rs770522582
- G540 (= G458) 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 468:471) binding
- L568 (≠ I486) 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
42% identity, 97% coverage: 4:493/503 of query aligns to 4:505/506 of 6chdA
- binding 5'-o-[(l-lysylamino)sulfonyl]adenosine: G207 (= G207), A229 (= A229), E231 (= E231), R253 (= R253), H261 (= H261), N262 (= N262), F265 (= F265), E269 (= E269), Y271 (= Y271), E424 (= E413), I425 (= I414), N427 (= N416), Y429 (≠ F418), E431 (= E420), G476 (= G464), G478 (= G466), G480 (= G468), R483 (= R471)
4ycuA Crystal structure of cladosporin in complex with human lysyl-tRNA synthetase (see paper)
42% identity, 97% coverage: 4:493/503 of query aligns to 3:504/505 of 4ycuA
- active site: R252 (= R253), E254 (= E255), T259 (= T260), H260 (= H261), E423 (= E413), N426 (= N416), R482 (= R471)
- binding cladosporin: E254 (= E255), H260 (= H261), N261 (= N262), F264 (= F265), N426 (= N416), G479 (= G468), R482 (= R471)
- binding lysine: G206 (= G207), E230 (= E231), E268 (= E269), Y270 (= Y271), N426 (= N416), Y428 (≠ F418), E430 (= E420), G475 (= G464)
6hcwA Crystal structure of lysyl-tRNA synthetase from cryptosporidium parvum complexed with l-lysine and a difluoro cyclohexyl chromone ligand (see paper)
43% identity, 97% coverage: 4:492/503 of query aligns to 1:500/501 of 6hcwA
- active site: R251 (= R253), E253 (= E255), T258 (= T260), H259 (= H261), E420 (= E413), N423 (= N416), R479 (= R471)
- binding ~{N}-[[4,4-bis(fluoranyl)-1-oxidanyl-cyclohexyl]methyl]-6-fluoranyl-4-oxidanylidene-chromene-2-carboxamide: R251 (= R253), E253 (= E255), H259 (= H261), N260 (= N262), F263 (= F265), E420 (= E413), L421 (≠ I414), G474 (= G466), L475 (≠ I467), G476 (= G468), R479 (= R471)
- binding lysine: G205 (= G207), E229 (= E231), E267 (= E269), Y269 (= Y271), N423 (= N416), Y425 (≠ F418), E427 (= E420), G472 (= G464)
6c86A Crystal structure of lysyl-tRNA synthetase from cryptosporidium parvum complexed with l-lysylsulfamoyl adenosine
43% identity, 97% coverage: 4:492/503 of query aligns to 1:500/501 of 6c86A
- active site: R251 (= R253), E253 (= E255), T258 (= T260), H259 (= H261), E420 (= E413), N423 (= N416), R479 (= R471)
- binding 5'-o-[(l-lysylamino)sulfonyl]adenosine: G205 (= G207), A227 (= A229), E229 (= E231), R251 (= R253), T258 (= T260), H259 (= H261), N260 (= N262), F263 (= F265), E267 (= E269), Y269 (= Y271), E420 (= E413), L421 (≠ I414), N423 (= N416), Y425 (≠ F418), E427 (= E420), G472 (= G464), W473 (≠ E465), G474 (= G466), G476 (= G468), R479 (= R471)
Query Sequence
>WP_084276583.1 NCBI__GCF_900176045.1:WP_084276583.1
MFDNQYEQQRIQKAEELRKEGINPYGHGFCKEITNKQFLEKYAYVKEREEKKDESVCVKL
NGRIKFLRHMGKAVFAKIEDESGIVQIYFNQDSLGKEWFKKVKKLIEVGDIIEAIGYPFV
TKTGELTLHANELNLVTKAIVPLPEKYHGLQDKELRYRQRYLDLIMNPDVKKVFVLRSRI
VSLIRDFFENHGFLEVETPMMHPIPGGANARPFITHHNALGVDRYLRIAPELYLKRLIVG
GFEAVFEINRNFRNEGMDATHNPEFTMIEFYWAYHTYEDLMKLTEDLFDYLFEKLGLPKK
LPYGEHTIDFSTPFDKIKYKDAIVEIGDVPQEVVEDKEKIISYLKERGIELEFPHKMSLG
ALQAELFDNFVEEKLINPTFITHFPIDISPLARRSDDNPEIAERFELFIAGKEIANGFNE
LNDPLDQYERFKAQVASKDVDDEAMHMDEDFVRALGHGMPPTAGEGIGIDRLVMLLTNQH
SIRDVILFPAMRPLPKEEKGEKE
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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