SitesBLAST
Comparing WP_011735595.1 NCBI__GCF_000015045.1:WP_011735595.1 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: 20:459/459 of query aligns to 22:466/466 of P0A8M0
- Y426 (≠ W419) 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)
33% identity, 98% coverage: 7:454/459 of query aligns to 8:429/434 of 1x55A
- active site: R211 (= R227), E213 (= E229), R219 (= R235), H220 (= H236), E357 (= E382), G360 (= G385), R408 (= R433)
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E168 (= E165), S188 (= S204), Q190 (= Q206), R211 (= R227), H220 (= H236), L221 (≠ A237), F224 (= F240), H226 (≠ M242), E228 (= E244), E357 (= E382), I358 (= I383), I359 (= I384), R364 (= R389), F402 (= F427), G403 (= G428), G405 (= G430), R408 (= R433)
1x54A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate (see paper)
33% identity, 98% coverage: 7:454/459 of query aligns to 8:429/434 of 1x54A
- active site: R211 (= R227), E213 (= E229), R219 (= R235), H220 (= H236), E357 (= E382), G360 (= G385), R408 (= R433)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E168 (= E165), S188 (= S204), Q190 (= Q206), R211 (= R227), H220 (= H236), L221 (≠ A237), F224 (= F240), H226 (≠ M242), E228 (= E244), E357 (= E382), I358 (= I383), I359 (= I384), R364 (= R389), F402 (= F427), G403 (= G428), G405 (= G430), R408 (= R433)
2xgtB Asparaginyl-tRNA synthetase from brugia malayi complexed with the sulphamoyl analogue of asparaginyl-adenylate (see paper)
31% identity, 98% coverage: 5:452/459 of query aligns to 3:426/433 of 2xgtB
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E163 (= E165), S183 (= S204), Q185 (= Q206), R206 (= R227), E208 (= E229), H215 (= H236), L216 (≠ A237), Y219 (≠ F240), H221 (≠ M242), E223 (= E244), E356 (= E382), I357 (= I383), V358 (≠ I384), G359 (= G385), R363 (= R389), Y401 (≠ F427), G402 (= G428), G404 (= G430)
2xtiA Asparaginyl-tRNA synthetase from brugia malayi complexed with atp:mg and l-asp-beta-noh adenylate:ppi:mg (see paper)
31% identity, 98% coverage: 5:452/459 of query aligns to 5:426/433 of 2xtiA
- binding 5'-O-[(R)-{[(2S)-2-amino-4-(hydroxyamino)-4-oxobutanoyl]oxy}(hydroxy)phosphoryl]adenosine: E163 (= E165), S183 (= S204), Q185 (= Q206), R206 (= R227), E208 (= E229), H215 (= H236), L216 (≠ A237), Y219 (≠ F240), H221 (≠ M242), E223 (= E244), Y333 (= Y360), E356 (= E382), I357 (= I383), V358 (≠ I384), G359 (= G385), R363 (= R389), Y401 (≠ F427), G402 (= G428), G404 (= G430), R407 (= R433)
- binding pyrophosphate 2-: R214 (= R235), H215 (= H236), E356 (= E382), R407 (= R433)
1b8aA Aspartyl-tRNA synthetase (see paper)
30% identity, 99% coverage: 2:455/459 of query aligns to 3:434/438 of 1b8aA
- binding adenosine-5'-triphosphate: R214 (= R227), E216 (= E229), H223 (= H236), L224 (≠ A237), E361 (= E382), I362 (= I383), S363 (≠ I384), S364 (≠ G385), G409 (= G430), R412 (= R433)
- binding manganese (ii) ion: E361 (= E382), S364 (≠ G385)
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
30% identity, 99% coverage: 2:455/459 of query aligns to 3:434/438 of 3nemB
- active site: R214 (= R227), E216 (= E229), R222 (= R235), H223 (= H236), E361 (= E382), S364 (≠ G385), R412 (= R433)
- binding adenosine-5'-triphosphate: R214 (= R227), E216 (= E229), H223 (= H236), L224 (≠ A237), E361 (= E382), I362 (= I383), S363 (≠ I384), S364 (≠ G385), G407 (= G428), G409 (= G430), R412 (= R433)
- binding magnesium ion: E361 (= E382), S364 (≠ G385)
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
30% identity, 99% coverage: 2:455/459 of query aligns to 3:434/438 of 3nemA
- active site: R214 (= R227), E216 (= E229), R222 (= R235), H223 (= H236), E361 (= E382), S364 (≠ G385), R412 (= R433)
- binding aspartyl-adenosine-5'-monophosphate: E170 (= E165), Q192 (= Q206), K195 (≠ G209), R214 (= R227), E216 (= E229), H223 (= H236), L224 (≠ A237), Y339 (= Y360), E361 (= E382), I362 (= I383), S363 (≠ I384), S364 (≠ G385), G365 (= G386), R368 (= R389), F406 (= F427), G407 (= G428), G409 (= G430), R412 (= R433)
3nelA Aspartyl-tRNA synthetase complexed with aspartic acid (see paper)
30% identity, 99% coverage: 2:455/459 of query aligns to 3:434/438 of 3nelA
- active site: R214 (= R227), E216 (= E229), R222 (= R235), H223 (= H236), E361 (= E382), S364 (≠ G385), R412 (= R433)
- binding aspartic acid: E170 (= E165), Q192 (= Q206), K195 (≠ G209), Y339 (= Y360), S364 (≠ G385), R368 (= R389), F406 (= F427), G407 (= G428)
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)
30% identity, 99% coverage: 2:455/459 of query aligns to 3:434/438 of Q52428