SitesBLAST
Comparing WP_018125495.1 NCBI__GCF_000375485.1:WP_018125495.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
P0A8M0 Asparagine--tRNA ligase; Asparaginyl-tRNA synthetase; AsnRS; EC 6.1.1.22 from Escherichia coli (strain K12) (see 3 papers)
56% identity, 96% coverage: 18:455/455 of query aligns to 19:466/466 of P0A8M0
- Y426 (≠ F415) mutation to F: No effect.; mutation to S: 15-fold increase in Km for ATP.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1x55A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate analogue (see paper)
35% identity, 96% coverage: 18:453/455 of query aligns to 18:432/434 of 1x55A
- active site: R211 (= R223), E213 (= E225), R219 (= R231), H220 (= H232), E357 (= E378), G360 (= G381), R408 (= R429)
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E168 (= E167), S188 (= S200), Q190 (= Q202), R211 (= R223), H220 (= H232), L221 (≠ V233), F224 (= F236), H226 (≠ M238), E228 (= E240), E357 (= E378), I358 (= I379), I359 (= I380), R364 (= R385), F402 (= F423), G403 (= G424), G405 (= G426), R408 (= R429)
1x54A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate (see paper)
35% identity, 96% coverage: 18:453/455 of query aligns to 18:432/434 of 1x54A
- active site: R211 (= R223), E213 (= E225), R219 (= R231), H220 (= H232), E357 (= E378), G360 (= G381), R408 (= R429)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E168 (= E167), S188 (= S200), Q190 (= Q202), R211 (= R223), H220 (= H232), L221 (≠ V233), F224 (= F236), H226 (≠ M238), E228 (= E240), E357 (= E378), I358 (= I379), I359 (= I380), R364 (= R385), F402 (= F423), G403 (= G424), G405 (= G426), R408 (= R429)
1b8aA Aspartyl-tRNA synthetase (see paper)
31% identity, 100% coverage: 1:453/455 of query aligns to 1:436/438 of 1b8aA
- binding adenosine-5'-triphosphate: R214 (= R223), E216 (= E225), H223 (= H232), L224 (≠ V233), E361 (= E378), I362 (= I379), S363 (≠ I380), S364 (≠ G381), G409 (= G426), R412 (= R429)
- binding manganese (ii) ion: E361 (= E378), S364 (≠ G381)
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
31% identity, 100% coverage: 1:453/455 of query aligns to 1:436/438 of 3nemB
- active site: R214 (= R223), E216 (= E225), R222 (= R231), H223 (= H232), E361 (= E378), S364 (≠ G381), R412 (= R429)
- binding adenosine-5'-triphosphate: R214 (= R223), E216 (= E225), H223 (= H232), L224 (≠ V233), E361 (= E378), I362 (= I379), S363 (≠ I380), S364 (≠ G381), G407 (= G424), G409 (= G426), R412 (= R429)
- binding magnesium ion: E361 (= E378), S364 (≠ G381)
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
31% identity, 100% coverage: 1:453/455 of query aligns to 1:436/438 of 3nemA
- active site: R214 (= R223), E216 (= E225), R222 (= R231), H223 (= H232), E361 (= E378), S364 (≠ G381), R412 (= R429)
- binding aspartyl-adenosine-5'-monophosphate: E170 (= E167), Q192 (= Q202), K195 (≠ A205), R214 (= R223), E216 (= E225), H223 (= H232), L224 (≠ V233), Y339 (= Y356), E361 (= E378), I362 (= I379), S363 (≠ I380), S364 (≠ G381), G365 (= G382), R368 (= R385), F406 (= F423), G407 (= G424), G409 (= G426), R412 (= R429)
3nelA Aspartyl-tRNA synthetase complexed with aspartic acid (see paper)
31% identity, 100% coverage: 1:453/455 of query aligns to 1:436/438 of 3nelA
- active site: R214 (= R223), E216 (= E225), R222 (= R231), H223 (= H232), E361 (= E378), S364 (≠ G381), R412 (= R429)
- binding aspartic acid: E170 (= E167), Q192 (= Q202), K195 (≠ A205), Y339 (= Y356), S364 (≠ G381), R368 (= R385), F406 (= F423), G407 (= G424)
Q52428 Aspartate--tRNA(Asp) ligase; Aspartyl-tRNA synthetase; AspRS; Discriminating aspartyl-tRNA synthetase; D-AspRS; EC 6.1.1.12 from Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) (see paper)
31% identity, 100% coverage: 1:453/455 of query aligns to 1:436/438 of Q52428
- W26 (≠ R26) mutation to H: Gains the ability to form Asp-tRNA(Asn) in vitro. Only 2-fold decrease in catalytic efficiency for Asp-tRNA(Asp) synthesis.
- K85 (≠ G84) mutation to P: Gains the ability to form Asp-tRNA(Asn) in vitro, and is impaired in its ability to synthesize Asp-tRNA(Asp) due to a 8-fold decrease in affinity for tRNA(Asp).
2xgtB Asparaginyl-tRNA synthetase from brugia malayi complexed with the sulphamoyl analogue of asparaginyl-adenylate (see paper)
30% identity, 95% coverage: 19:448/455 of query aligns to 14:426/433 of 2xgtB
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E163 (= E167), S183 (= S200), Q185 (= Q202), R206 (= R223), E208 (= E225), H215 (= H232), L216 (≠ V233), Y219 (≠ F236), H221 (≠ M238), E223 (= E240), E356 (= E378), I357 (= I379), V358 (≠ I380), G359 (= G381), R363 (= R385), Y401 (≠ F423), G402 (= G424), G404 (= G426)
2xtiA Asparaginyl-tRNA synthetase from brugia malayi complexed with atp:mg and l-asp-beta-noh adenylate:ppi:mg (see paper)
31% identity, 95% coverage: 19:448/455 of query aligns to 16:426/433 of 2xtiA
- binding 5'-O-[(R)-{[(2S)-2-amino-4-(hydroxyamino)-4-oxobutanoyl]oxy}(hydroxy)phosphoryl]adenosine: E163 (= E167), S183 (= S200), Q185 (= Q202), R206 (= R223), E208 (= E225), H215 (= H232), L216 (≠ V233), Y219 (≠ F236), H221 (≠ M238), E223 (= E240), Y333 (= Y356), E356 (= E378), I357 (= I379), V358 (≠ I380), G359 (= G381), R363 (= R385), Y401 (≠ F423), G402 (= G424), G404 (= G426), R407 (= R429)
- binding pyrophosphate 2-: R214 (= R231), H215 (= H232), E356 (= E378), R407 (= R429)
8h53A Human asparaginyl-tRNA synthetase in complex with asparagine-amp (see paper)
29% identity, 98% coverage: 2:448/455 of query aligns to 2:420/427 of 8h53A
- binding imidodiphosphoric acid: R209 (= R231), H210 (= H232), E350 (= E378), R401 (= R429)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E158 (= E167), S178 (= S200), Q180 (= Q202), R201 (= R223), L211 (≠ V233), Y214 (≠ F236), H216 (≠ M238), E218 (= E240), E350 (= E378), I351 (= I379), V352 (≠ I380), R357 (= R385), Y395 (≠ F423), G396 (= G424), G398 (= G426), R401 (= R429)
8tc9A Human asparaginyl-tRNA synthetase bound to osm-s-106 (see paper)
29% identity, 95% coverage: 19:448/455 of query aligns to 19:427/434 of 8tc9A
- binding N~1~-[(3M)-3-(4-aminothieno[3,2-d]pyrimidin-6-yl)benzene-1-sulfonyl]-L-aspartamide: E165 (= E167), S185 (= S200), Q187 (= Q202), R208 (= R223), H217 (= H232), L218 (≠ V233), Y221 (≠ F236), H223 (≠ M238), E225 (= E240), R364 (= R385), Y402 (≠ F423), G403 (= G424), R408 (= R429)
2xtiB Asparaginyl-tRNA synthetase from brugia malayi complexed with atp:mg and l-asp-beta-noh adenylate:ppi:mg (see paper)
30% identity, 95% coverage: 19:448/455 of query aligns to 15:422/429 of 2xtiB
- binding adenosine-5'-triphosphate: R202 (= R223), E204 (= E225), R210 (= R231), H211 (= H232), L212 (≠ V233), Y215 (≠ F236), E352 (= E378), I353 (= I379), V354 (≠ I380), G400 (= G426), R403 (= R429)
8tc8A Human asparaginyl-tRNA synthetase bound to adenosine 5'-sulfamate (see paper)
29% identity, 98% coverage: 2:448/455 of query aligns to 4:428/435 of 8tc8A
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E166 (= E167), S186 (= S200), Q188 (= Q202), R209 (= R223), E211 (= E225), H218 (= H232), L219 (≠ V233), Y222 (≠ F236), H224 (≠ M238), E226 (= E240), E358 (= E378), I359 (= I379), V360 (≠ I380), R365 (= R385), Y403 (≠ F423), G404 (= G424), G406 (= G426)
O07683 Aspartate--tRNA(Asp/Asn) ligase; Aspartyl-tRNA synthetase; AspRS; Non-discriminating aspartyl-tRNA synthetase; ND-AspRS; EC 6.1.1.23 from Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium) (see paper)
28% identity, 100% coverage: 1:454/455 of query aligns to 2:435/436 of O07683
- H26 (≠ R26) mutation H->A,Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn).
- P84 (≠ G84) mutation P->A,K: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn).
3m4pA Entamoeba histolytica asparaginyl-tRNA synthetase (asnrs) in complex with asparaginyl-adenylate
28% identity, 95% coverage: 19:448/455 of query aligns to 18:428/435 of 3m4pA
- active site: R211 (= R223), E213 (= E225), R219 (= R231), H220 (= H232), E358 (= E378), G361 (= G381), R409 (= R429)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: S188 (= S200), Q190 (= Q202), R211 (= R223), H220 (= H232), L221 (≠ V233), Y224 (≠ F236), H226 (≠ M238), E358 (= E378), I359 (= I379), V360 (≠ I380), R365 (= R385), Y403 (≠ F423), G404 (= G424), G406 (= G426), R409 (= R429)
P04802 Aspartate--tRNA ligase, cytoplasmic; Aspartyl-tRNA synthetase; AspRS; EC 6.1.1.12 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
33% identity, 73% coverage: 120:453/455 of query aligns to 236:555/557 of P04802
- P273 (= P159) mutation to G: Loss of activity; important for dimerization.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
1aszA The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction (see paper)
33% identity, 73% coverage: 120:453/455 of query aligns to 169:488/490 of 1aszA
- active site: R258 (= R223), E260 (= E225), R266 (= R231), H267 (= H232), E411 (= E378), S414 (≠ G381), R464 (= R429)
- binding adenosine-5'-triphosphate: R258 (= R223), M268 (≠ V233), F271 (= F236), E411 (= E378), I412 (= I379), L413 (≠ I380), G459 (= G424), R464 (= R429)
- binding : S213 (≠ C166), E214 (= E167), G215 (= G168), G216 (≠ A169), S217 (≠ G170), Q233 (≠ V199), F237 (≠ L203), E260 (= E225), N261 (= N226), S262 (= S227), N263 (= N228), H267 (= H232), S356 (≠ Q327), T357 (= T328), F388 (= F355), K486 (≠ N451)
Sites not aligning to the query:
- binding : 52, 53, 54, 57, 58, 60, 71, 73, 110, 112, 113, 135, 138, 140, 154, 156, 157, 158, 160, 163
1asyA Class ii aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA asp (see paper)
33% identity, 73% coverage: 120:453/455 of query aligns to 169:488/490 of 1asyA
- active site: R258 (= R223), E260 (= E225), R266 (= R231), H267 (= H232), E411 (= E378), S414 (≠ G381), R464 (= R429)
- binding : R258 (= R223), E260 (= E225), N261 (= N226), S262 (= S227), N263 (= N228), T264 (= T229), H267 (= H232), M268 (≠ V233), F271 (= F236), T357 (= T328), E411 (= E378), I412 (= I379), L413 (≠ I380), S414 (≠ G381), G459 (= G424), R464 (= R429), K486 (≠ N451)
Sites not aligning to the query:
- binding : 52, 53, 54, 58, 60, 71, 73, 88, 111, 112, 113, 114, 135, 138, 154, 156, 157, 158, 159, 162, 163
O74407 Aspartate--tRNA ligase, cytoplasmic; Aspartyl-tRNA synthetase; AspRS; EC 6.1.1.12 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
30% identity, 73% coverage: 120:453/455 of query aligns to 242:578/580 of O74407
- S282 (≠ T162) modified: Phosphoserine
- S307 (= S200) modified: Phosphoserine
Query Sequence
>WP_018125495.1 NCBI__GCF_000375485.1:WP_018125495.1
MKRTKIKALLNAESAMPEIVVKGWVRTKRDSKGFSFLELNDGSCLKNIQTVIDHTPEIEA
ELAKIGTGASVAIEGELVESPGKGQKWEVRGKSLKLLGEADPETFPLQKKRHSDEFLRGI
AHLRPRTNKFGAMFRIRSELAQAIHKFFAEKDFFYVHTPVLTGSDCEGAGEMFRVTCLEH
GCKSSIEEDFFGKPAHLTVSGQLEAEMFSLALGDVYTFGPTFRAENSNTPRHVAEFWMIE
PEMAFADLADDMDLGEVMIKYLVRHILDNCADDVELFAKWVDKSLMPTLETILENEFIRL
PYTEAINVLKKTKKKFEYPVEWGMDLQTEHERFLCEEKFKQPLYVYDYPKTIKPFYMRMN
DDNETVAAMDCLVPRIGEIIGGSQREERLDVLHARMKEMDLSEEEYWWYLDSRRFGSVPH
AGFGLGFERLLMLVTGVGNIRDAIPFPRTPNHLEF
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