SitesBLAST
Comparing WP_013554590.1 NCBI__GCF_000186245.1:WP_013554590.1 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)
52% identity, 95% coverage: 5:497/520 of query aligns to 16:504/505 of P0A8N5
- K114 (= K107) modified: N6-acetyllysine
- K156 (= K149) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1bbuA Lysyl-tRNA synthetase (lyss) complexed with lysine (see paper)
51% identity, 95% coverage: 5:496/520 of query aligns to 5:486/486 of 1bbuA
- active site: R246 (= R256), E248 (= E258), R253 (≠ T263), H254 (= H264), E405 (= E414), N408 (= N417), R464 (= R474)
- binding lysine: G200 (= G210), E224 (= E234), E262 (= E272), Y264 (= Y274), F410 (= F419), E412 (= E421), G457 (= G467), G459 (= G469)
1e24A Lysyl-tRNA synthetase (lysu) hexagonal form complexed with lysine and atp and mn2+ (see paper)
51% identity, 95% coverage: 5:496/520 of query aligns to 5:485/485 of 1e24A
- active site: R245 (= R256), E247 (= E258), R252 (≠ T263), H253 (= H264), E404 (= E414), N407 (= N417), R463 (= R474)
- binding adenosine-5'-triphosphate: R245 (= R256), R252 (≠ T263), H253 (= H264), N254 (= N265), F257 (= F268), M259 (= M270), E404 (= E414), I405 (= I415), G460 (= G471), R463 (= R474)
- binding lysine: G199 (= G210), E223 (= E234), E261 (= E272), Y263 (= Y274), N407 (= N417), F409 (= F419), E411 (= E421), G456 (= G467), G458 (= G469)
- binding manganese (ii) ion: E397 (= E407), E404 (= E414)
1e22A Lysyl-tRNA synthetase (lysu) hexagonal form complexed with lysine and the non-hydrolysable atp analogue amp-pcp (see paper)
51% identity, 95% coverage: 5:496/520 of query aligns to 5:485/485 of 1e22A
- active site: R245 (= R256), E247 (= E258), R252 (≠ T263), H253 (= H264), E404 (= E414), N407 (= N417), R463 (= R474)
- binding phosphomethylphosphonic acid adenylate ester: R245 (= R256), R252 (≠ T263), H253 (= H264), N254 (= N265), F257 (= F268), E404 (= E414), I405 (= I415), G460 (= G471), R463 (= R474)
- binding lysine: G199 (= G210), E223 (= E234), M259 (= M270), E261 (= E272), Y263 (= Y274), N407 (= N417), F409 (= F419), E411 (= E421), G456 (= G467), G458 (= G469)
- binding magnesium ion: E397 (= E407), E404 (= E414)
1e1tA Lysyl-tRNA synthetase (lysu) hexagonal form complexed with the lysyl_adenylate intermediate (see paper)
51% identity, 95% coverage: 5:496/520 of query aligns to 5:485/485 of 1e1tA
- active site: R245 (= R256), E247 (= E258), R252 (≠ T263), H253 (= H264), E404 (= E414), N407 (= N417), R463 (= R474)
- binding adenosine-5'-[lysyl-phosphate]: G199 (= G210), E223 (= E234), R245 (= R256), R252 (≠ T263), H253 (= H264), N254 (= N265), F257 (= F268), M259 (= M270), E261 (= E272), Y263 (= Y274), E404 (= E414), I405 (= I415), N407 (= N417), F409 (= F419), E411 (= E421), G456 (= G467), G458 (= G469), G460 (= G471)
- binding magnesium ion: E397 (= E407), E404 (= E414)
- binding pyrophosphate 2-: H253 (= H264), E404 (= E414), R463 (= R474)
5yzxA Crystal structure of e.Coli lysu t146d mutant
51% identity, 95% coverage: 5:496/520 of query aligns to 4:484/484 of 5yzxA
- binding bis(adenosine)-5'-tetraphosphate: R244 (= R256), E246 (= E258), H252 (= H264), N253 (= N265), F256 (= F268), M258 (= M270), D358 (= D369), E403 (= E414), I404 (= I415), G459 (= G471), R462 (= R474)
- binding calcium ion: D358 (= D369), E396 (= E407), E396 (= E407), E403 (= E414), N406 (= N417)
1e1oA Lysyl-tRNA synthetase (lysu) hexagonal form, complexed with lysine (see paper)
51% identity, 95% coverage: 5:496/520 of query aligns to 5:484/484 of 1e1oA
- active site: R245 (= R256), E247 (= E258), H252 (= H264), E403 (= E414), N406 (= N417), R462 (= R474)
- binding lysine: G199 (= G210), E223 (= E234), E260 (= E272), Y262 (= Y274), N406 (= N417), F408 (= F419), E410 (= E421), G455 (= G467), G457 (= G469)
4ex5A Crystal structure of lysyl-tRNA synthetase lysrs from burkholderia thailandensis bound to lysine (see paper)
48% identity, 95% coverage: 4:495/520 of query aligns to 1:485/486 of 4ex5A
- active site: R242 (= R256), E244 (= E258), R249 (≠ T263), H250 (= H264), E405 (= E414), N408 (= N417), R464 (= R474)
- binding lysine: E220 (= E234), E258 (= E272), Y260 (= Y274), F410 (= F419), E412 (= E421), G457 (= G467), G459 (= G469)
3e9iA Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with l-lysine hydroxamate-amp (see paper)
48% identity, 94% coverage: 5:495/520 of query aligns to 3:483/484 of 3e9iA
- active site: R245 (= R256), E247 (= E258), R252 (≠ T263), H253 (= H264), E403 (= E414), N406 (= N417), R462 (= R474)
- binding 5'-O-{(R)-hydroxy[(L-lysylamino)oxy]phosphoryl}adenosine: G199 (= G210), E223 (= E234), R245 (= R256), H253 (= H264), N254 (= N265), F257 (= F268), M259 (= M270), E261 (= E272), Y263 (= Y274), E403 (= E414), H404 (≠ I415), N406 (= N417), F408 (= F419), E410 (= E421), G459 (= G471)
3e9hA Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with l-lysylsulfamoyl adenosine (see paper)
48% identity, 94% coverage: 5:495/520 of query aligns to 3:483/484 of 3e9hA
- active site: R245 (= R256), E247 (= E258), R252 (≠ T263), H253 (= H264), E403 (= E414), N406 (= N417), R462 (= R474)
- binding 5'-o-[(l-lysylamino)sulfonyl]adenosine: E223 (= E234), R245 (= R256), H253 (= H264), N254 (= N265), F257 (= F268), M259 (= M270), E261 (= E272), Y263 (= Y274), E403 (= E414), H404 (≠ I415), N406 (= N417), F408 (= F419), E410 (= E421), G455 (= G467), G459 (= G471), R462 (= R474)
- binding magnesium ion: E396 (= E407), E403 (= E414), N406 (= N417)
3a74A Lysyl-tRNA synthetase from bacillus stearothermophilus complexed with diadenosine tetraphosphate (ap4a)
48% identity, 94% coverage: 5:495/520 of query aligns to 3:483/484 of 3a74A
- active site: R245 (= R256), E247 (= E258), R252 (≠ T263), H253 (= H264), E403 (= E414), N406 (= N417), R462 (= R474)
- binding bis(adenosine)-5'-tetraphosphate: R245 (= R256), E247 (= E258), R252 (≠ T263), H253 (= H264), N254 (= N265), F257 (= F268), M259 (= M270), E358 (≠ D369), E362 (= E373), E403 (= E414), N406 (= N417), G459 (= G471), R462 (= R474)
- binding 2,6-diamino-hexanoic acid amide: G199 (= G210), E223 (= E234), M259 (= M270), E261 (= E272), Y263 (= Y274), N406 (= N417), F408 (= F419), E410 (= E421)
- binding magnesium ion: E396 (= E407), E396 (= E407), E403 (= E414), E403 (= E414)
6wbdB Crystal structure of lysyl-tRNA synthetase from stenotrophomonas maltophilia with bound l-lysine
47% identity, 95% coverage: 4:496/520 of query aligns to 2:485/485 of 6wbdB
Q15046 Lysine--tRNA ligase; Lysyl-tRNA synthetase; LysRS; EC 2.7.7.-; EC 6.1.1.6 from Homo sapiens (Human) (see 16 papers)
41% identity, 98% coverage: 5:512/520 of query aligns to 74:591/597 of Q15046
- R80 (= R11) to H: in DEAPLE; uncertain significance; dbSNP:rs369114426
- V101 (≠ R32) mutation V->D,R,W: Disrupts interaction with AIMP2 and the multisynthase complex.
- L105 (≠ S36) to H: in CMTRIB; severely affects enzyme activity; dbSNP:rs267607194
- G189 (≠ F122) to D: in LEPID; does not rescue the developmental defects caused by KARS1 depletion in xenopus
- P200 (≠ C133) to L: in DEAPLE and LEPID; reduces interaction with AIMP2. Reduces tRNA-lysine aminoacylation
- S207 (= S140) 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 (= F196) to V: in DEAPLE; reduces interaction with AIMP2. Reduces tRNA-lysine aminoacylation; dbSNP:rs772410450
- G277 (= G210) binding
- E301 (= E234) binding
- RNE 323:325 (= RNE 256:258) binding
- HN 331:332 (= HN 264:265) binding
- E339 (= E272) binding
- Y341 (= Y274) binding
- D346 (≠ T279) mutation to R: Induces protein aggregation. Releases from the subunit complex.
- L350 (= L283) to H: found in a patient with hypertrophic cardiomyopathy and mild intellectual disability together with proximal muscle weakness; uncertain significance
- P390 (= P316) to R: found in a patient with hypertrophic cardiomyopathy and mild intellectual disability together with proximal muscle weakness; uncertain significance
- R438 (≠ L358) to W: in LEPID; uncertain significance; dbSNP:rs761527468
- V448 (≠ F368) to F: in DEAPLE; uncertain significance
- R477 (≠ D397) 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 414:415) binding
- N497 (= N417) binding
- E501 (= E421) binding
- P505 (= P425) to S: in DEAPLE; decreases tRNA-lysine aminoacylation; slightly induces protein aggregation; no effect on cytoplasmic location; no effect on oligomerization; dbSNP:rs1555512658
- E525 (= E446) to K: in LEPID; uncertain significance; dbSNP:rs770522582
- G540 (= G461) 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 471:474) binding
- L568 (= L489) 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
6kctA Crystal structure of plasmodium lysyl-tRNA synthetase in complex with a cladosporin derivative 5 (see paper)
42% identity, 94% coverage: 7:496/520 of query aligns to 6:504/506 of 6kctA
- active site: R253 (= R256), E255 (= E258), T260 (= T263), H261 (= H264), E423 (= E414), N426 (= N417), R482 (= R474)
- binding 3-(cyclohexylmethyl)-6,8-bis(oxidanyl)isochromen-1-one: E255 (= E258), H261 (= H264), N262 (= N265), F265 (= F268), E423 (= E414), V424 (≠ I415), L425 (≠ A416), G477 (= G469), R482 (= R474)
- binding lysine: E231 (= E234), E269 (= E272), Y271 (= Y274), N426 (= N417), Y428 (≠ F419), E430 (= E421), G475 (= G467), L476 (≠ E468), G477 (= G469)
6kabA Crystal structure of plasmodium lysyl-tRNA synthetase in complex with a cladosporin derivative 2 (see paper)
42% identity, 94% coverage: 7:496/520 of query aligns to 6:504/506 of 6kabA
- active site: R253 (= R256), E255 (= E258), T260 (= T263), H261 (= H264), E423 (= E414), N426 (= N417), R482 (= R474)
- binding (3~{S})-3-(cyclohexylmethyl)-6,8-bis(oxidanyl)-3,4-dihydroisochromen-1-one: E255 (= E258), H261 (= H264), N262 (= N265), F265 (= F268), E423 (= E414), V424 (≠ I415), L425 (≠ A416), N426 (= N417), G477 (= G469), R482 (= R474)
- binding lysine: E231 (= E234), E269 (= E272), Y271 (= Y274), N426 (= N417), Y428 (≠ F419), E430 (= E421), G475 (= G467), G477 (= G469)
6agtB Crystal structure of pfkrs complexed with chromone inhibitor (see paper)
42% identity, 94% coverage: 7:496/520 of query aligns to 6:504/506 of 6agtB
- active site: R253 (= R256), E255 (= E258), T260 (= T263), H261 (= H264), E423 (= E414), N426 (= N417), R482 (= R474)
- binding N-(cyclohexylmethyl)-4-oxo-4H-1-benzopyran-2-carboxamide: R253 (= R256), E255 (= E258), T260 (= T263), H261 (= H264), N262 (= N265), F265 (= F268), G477 (= G469), R482 (= R474)
- binding lysine: E231 (= E234), E269 (= E272), Y271 (= Y274), N426 (= N417), Y428 (≠ F419), E430 (= E421), G475 (= G467), G477 (= G469)
6kbfA Crystal structure of plasmodium lysyl-tRNA synthetase in complex with a cladosporin derivative 3 (see paper)
42% identity, 94% coverage: 7:496/520 of query aligns to 5:503/504 of 6kbfA
- active site: R252 (= R256), E254 (= E258), T259 (= T263), H260 (= H264), E422 (= E414), N425 (= N417), R481 (= R474)
- binding (3~{S})-3-[[(1~{S},3~{S})-3-methylcyclohexyl]methyl]-6,8-bis(oxidanyl)-3,4-dihydro-2~{H}-isoquinolin-1-one: R252 (= R256), E254 (= E258), H260 (= H264), N261 (= N265), F264 (= F268), E422 (= E414), L424 (≠ A416), G476 (= G469), R481 (= R474)
- binding lysine: G206 (= G210), E230 (= E234), E268 (= E272), Y270 (= Y274), N425 (= N417), Y427 (≠ F419), E429 (= E421), G474 (= G467)
6bniA Crystal structure of lysyl-tRNA synthetase from cryptosporidium parvum complexed with l-lysine and adenosine
44% identity, 86% coverage: 51:495/520 of query aligns to 44:501/502 of 6bniA
- active site: R252 (= R256), E254 (= E258), T259 (= T263), H260 (= H264), E421 (= E414), N424 (= N417), R480 (= R474)
- binding adenosine: H260 (= H264), N261 (= N265), F264 (= F268), E421 (= E414), L422 (≠ I415), G477 (= G471), R480 (= R474)
- binding lysine: G206 (= G210), E230 (= E234), E268 (= E272), Y270 (= Y274), N424 (= N417), Y426 (≠ F419), E428 (= E421), G473 (= G467), W474 (≠ E468)
5eloA Crystal structure of lysyl-tRNA synthetase from cryptosporidium parvum complexed with l-lysine and cladosporin (see paper)
44% identity, 86% coverage: 51:495/520 of query aligns to 44:501/502 of 5eloA
- active site: R252 (= R256), E254 (= E258), T259 (= T263), H260 (= H264), E421 (= E414), N424 (= N417), R480 (= R474)
- binding cladosporin: R252 (= R256), E254 (= E258), H260 (= H264), N261 (= N265), F264 (= F268), E421 (= E414), L422 (≠ I415), G475 (= G469), G477 (= G471), R480 (= R474)
- binding lysine: G206 (= G210), E230 (= E234), E268 (= E272), Y270 (= Y274), N424 (= N417), Y426 (≠ F419), E428 (= E421), G473 (= G467), W474 (≠ E468), G475 (= G469)
6hcwA Crystal structure of lysyl-tRNA synthetase from cryptosporidium parvum complexed with l-lysine and a difluoro cyclohexyl chromone ligand (see paper)
44% identity, 86% coverage: 51:495/520 of query aligns to 43:500/501 of 6hcwA
- active site: R251 (= R256), E253 (= E258), T258 (= T263), H259 (= H264), E420 (= E414), N423 (= N417), R479 (= R474)
- binding ~{N}-[[4,4-bis(fluoranyl)-1-oxidanyl-cyclohexyl]methyl]-6-fluoranyl-4-oxidanylidene-chromene-2-carboxamide: R251 (= R256), E253 (= E258), H259 (= H264), N260 (= N265), F263 (= F268), E420 (= E414), L421 (≠ I415), G474 (= G469), L475 (≠ I470), G476 (= G471), R479 (= R474)
- binding lysine: G205 (= G210), E229 (= E234), E267 (= E272), Y269 (= Y274), N423 (= N417), Y425 (≠ F419), E427 (= E421), G472 (= G467)
Query Sequence
>WP_013554590.1 NCBI__GCF_000186245.1:WP_013554590.1
MIFENPYVQERIKKAQTLREEGINPYPAGRTRGTPSAEFLAENRDLLERPEGERIAQDRH
YRLTGRIKFIRIMGKAAFAKLEDSEGLVQIYYNRDDLPEGYYNKIKKLIEVGDIVEAEGF
PFVTRTGEITLHCTDLRIVSKAVHPLPEKFHGLTDQEIRYRQRYLDMIMNPEVKKTFKLR
SRIVSLVRRFFEEKGFLEVETPMMHPIPGGANARPFVTRHNALGVDRYLRIAPELYLKRL
IVGGMEAVFEINRNFRNEGMDHTHNPEFTMIEYYWAWHTYEDLMRLTEELFDYLFENLGL
PRKLPYGDQEVDFTTPFRKVGYLESLHTIGGVPEAVITDREKARAYLKEHGVETDPNLSL
GYLQAELFDAFVEEKLINPTFVVDFPVEISPLARRSDENPEIAERFELFIAGKEIANGFN
ELNDPLDQYERFKMQVEAKEVTGDDEAMHMDLDYVRALSYGMAPTAGEGIGIDRLVMLLT
NQHSIRDVLLFPAMRPEAKLESAESNESNESNENEPQTKE
Or try a new SitesBLAST search
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