SitesBLAST
Comparing WP_018125495.1 NCBI__GCF_000375485.1:WP_018125495.1 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)
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),