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
- W26 (≠ R25) 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 (≠ G83) 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).
2xtiB 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 4:422/429 of 2xtiB
- binding adenosine-5'-triphosphate: R202 (= R227), E204 (= E229), R210 (= R235), H211 (= H236), L212 (≠ A237), Y215 (≠ F240), E352 (= E382), I353 (= I383), V354 (≠ I384), G400 (= G430), R403 (= R433)
3m4pA Entamoeba histolytica asparaginyl-tRNA synthetase (asnrs) in complex with asparaginyl-adenylate
29% identity, 96% coverage: 12:452/459 of query aligns to 12:428/435 of 3m4pA
- active site: R211 (= R227), E213 (= E229), R219 (= R235), H220 (= H236), E358 (= E382), G361 (= G385), R409 (= R433)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: S188 (= S204), Q190 (= Q206), R211 (= R227), H220 (= H236), L221 (≠ A237), Y224 (≠ F240), H226 (≠ M242), E358 (= E382), I359 (= I383), V360 (≠ I384), R365 (= R389), Y403 (≠ F427), G404 (= G428), G406 (= G430), R409 (= R433)
8h53A Human asparaginyl-tRNA synthetase in complex with asparagine-amp (see paper)
29% identity, 96% coverage: 11:452/459 of query aligns to 10:420/427 of 8h53A
- binding imidodiphosphoric acid: R209 (= R235), H210 (= H236), E350 (= E382), R401 (= R433)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E158 (= E165), S178 (= S204), Q180 (= Q206), R201 (= R227), L211 (≠ A237), Y214 (≠ F240), H216 (≠ M242), E218 (= E244), E350 (= E382), I351 (= I383), V352 (≠ I384), R357 (= R389), Y395 (≠ F427), G396 (= G428), G398 (= G430), R401 (= R433)
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)
30% identity, 100% coverage: 2:458/459 of query aligns to 4:435/436 of O07683
- H26 (≠ R25) mutation H->A,Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn).
- P84 (≠ G83) mutation P->A,K: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn).
8tc9A Human asparaginyl-tRNA synthetase bound to osm-s-106 (see paper)
28% identity, 96% coverage: 11:452/459 of query aligns to 12:427/434 of 8tc9A
- binding N~1~-[(3M)-3-(4-aminothieno[3,2-d]pyrimidin-6-yl)benzene-1-sulfonyl]-L-aspartamide: E165 (= E165), S185 (= S204), Q187 (= Q206), R208 (= R227), H217 (= H236), L218 (≠ A237), Y221 (≠ F240), H223 (≠ M242), E225 (= E244), R364 (= R389), Y402 (≠ F427), G403 (= G428), R408 (= R433)
8tc8A Human asparaginyl-tRNA synthetase bound to adenosine 5'-sulfamate (see paper)
28% identity, 96% coverage: 11:452/459 of query aligns to 12:428/435 of 8tc8A
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E166 (= E165), S186 (= S204), Q188 (= Q206), R209 (= R227), E211 (= E229), H218 (= H236), L219 (≠ A237), Y222 (≠ F240), H224 (≠ M242), E226 (= E244), E358 (= E382), I359 (= I383), V360 (≠ I384), R365 (= R389), Y403 (≠ F427), G404 (= G428), G406 (= G430)
1aszA The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction (see paper)
29% identity, 72% coverage: 124:455/459 of query aligns to 173:486/490 of 1aszA
- active site: R258 (= R227), E260 (= E229), R266 (= R235), H267 (= H236), E411 (= E382), S414 (≠ G385), R464 (= R433)
- binding adenosine-5'-triphosphate: R258 (= R227), M268 (≠ A237), F271 (= F240), E411 (= E382), I412 (= I383), L413 (≠ I384), G459 (= G428), R464 (= R433)
- binding : S213 (≠ C164), E214 (= E165), G215 (= G166), G216 (≠ A167), S217 (≠ G168), Q233 (≠ V203), F237 (≠ L207), E260 (= E229), N261 (= N230), S262 (= S231), N263 (= N232), H267 (= H236), S356 (≠ Q331), T357 (= T332), F388 (= F359), K486 (≠ R455)
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)
29% identity, 72% coverage: 124:455/459 of query aligns to 173:486/490 of 1asyA
- active site: R258 (= R227), E260 (= E229), R266 (= R235), H267 (= H236), E411 (= E382), S414 (≠ G385), R464 (= R433)
- binding : R258 (= R227), E260 (= E229), N261 (= N230), S262 (= S231), N263 (= N232), T264 (= T233), H267 (= H236), M268 (≠ A237), F271 (= F240), T357 (= T332), E411 (= E382), I412 (= I383), L413 (≠ I384), S414 (≠ G385), G459 (= G428), R464 (= R433), K486 (≠ R455)
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
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)
29% identity, 72% coverage: 124:455/459 of query aligns to 240:553/557 of P04802
- P273 (= P157) mutation to G: Loss of activity; important for dimerization.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
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)
25% identity, 97% coverage: 9:455/459 of query aligns to 98:576/580 of O74407
- S282 (≠ T160) modified: Phosphoserine
- S307 (= S204) modified: Phosphoserine
Query Sequence
>WP_011735595.1 NCBI__GCF_000015045.1:WP_011735595.1
MRTIIRQLLSQGVSGQTYAIAGWVRSLRISKGIAFIALNDGSNLAGIQVVVEEQSPAFSE
IDAIATGCSLRVTGTLVASPAAGQERELRAESIAIVGTSDENYPLQKKRHSFEYLREIAH
LRPRSNTFGAVFRLRSRLAQAIHRFFGDNNFLYVHTPIITASDCEGAGELFRVTTLDAAS
PPLLEGRPDFGQDFFGQKTGLTVSGQLEGELFALAFSDIYTFGPTFRAENSNTPRHAAEF
WMIEPEMAFADLADDAALAEKFVRYLCRFALEECAEEMAFFDRQIEKGLLERVRRVAEAD
FVRMEYDEAIQRLQRSGVTFSYPVEWGLDLQTEHERYITEKIVGGPAFILNYPRDIKAFY
MRSNPDNRTVAAMDLLVPKVGEIIGGSQREERLDVLEARMAELGIAREPLWWYLESRRWG
SCPHAGFGLGFERLVMYLSGMENIRDVIPFPRTPRHAEF
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