SitesBLAST
Comparing WP_005351729.1 NCBI__GCF_000173975.1:WP_005351729.1 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)
57% identity, 97% coverage: 14:458/460 of query aligns to 16:464/466 of P0A8M0
- Y426 (= Y420) 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: 15:454/460 of query aligns to 16:428/434 of 1x55A
- active site: R211 (= R228), E213 (= E230), R219 (= R236), H220 (= H237), E357 (= E383), G360 (= G386), R408 (= R434)
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E168 (= E165), S188 (= S205), Q190 (= Q207), R211 (= R228), H220 (= H237), L221 (≠ A238), F224 (= F241), H226 (≠ M243), E228 (= E245), E357 (= E383), I358 (= I384), I359 (= I385), R364 (= R390), F402 (= F428), G403 (= G429), G405 (= G431), R408 (= R434)
1x54A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate (see paper)
35% identity, 96% coverage: 15:454/460 of query aligns to 16:428/434 of 1x54A
- active site: R211 (= R228), E213 (= E230), R219 (= R236), H220 (= H237), E357 (= E383), G360 (= G386), R408 (= R434)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E168 (= E165), S188 (= S205), Q190 (= Q207), R211 (= R228), H220 (= H237), L221 (≠ A238), F224 (= F241), H226 (≠ M243), E228 (= E245), E357 (= E383), I358 (= I384), I359 (= I385), R364 (= R390), F402 (= F428), G403 (= G429), G405 (= G431), R408 (= R434)
1b8aA Aspartyl-tRNA synthetase (see paper)
32% identity, 97% coverage: 10:453/460 of query aligns to 11:431/438 of 1b8aA
- binding adenosine-5'-triphosphate: R214 (= R228), E216 (= E230), H223 (= H237), L224 (≠ A238), E361 (= E383), I362 (= I384), S363 (≠ I385), S364 (≠ G386), G409 (= G431), R412 (= R434)
- binding manganese (ii) ion: E361 (= E383), S364 (≠ G386)
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
32% identity, 97% coverage: 10:453/460 of query aligns to 11:431/438 of 3nemB
- active site: R214 (= R228), E216 (= E230), R222 (= R236), H223 (= H237), E361 (= E383), S364 (≠ G386), R412 (= R434)
- binding adenosine-5'-triphosphate: R214 (= R228), E216 (= E230), H223 (= H237), L224 (≠ A238), E361 (= E383), I362 (= I384), S363 (≠ I385), S364 (≠ G386), G407 (= G429), G409 (= G431), R412 (= R434)
- binding magnesium ion: E361 (= E383), S364 (≠ G386)
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
32% identity, 97% coverage: 10:453/460 of query aligns to 11:431/438 of 3nemA
- active site: R214 (= R228), E216 (= E230), R222 (= R236), H223 (= H237), E361 (= E383), S364 (≠ G386), R412 (= R434)
- binding aspartyl-adenosine-5'-monophosphate: E170 (= E165), Q192 (= Q207), K195 (≠ A210), R214 (= R228), E216 (= E230), H223 (= H237), L224 (≠ A238), Y339 (= Y361), E361 (= E383), I362 (= I384), S363 (≠ I385), S364 (≠ G386), G365 (= G387), R368 (= R390), F406 (= F428), G407 (= G429), G409 (= G431), R412 (= R434)
3nelA Aspartyl-tRNA synthetase complexed with aspartic acid (see paper)
32% identity, 97% coverage: 10:453/460 of query aligns to 11:431/438 of 3nelA
- active site: R214 (= R228), E216 (= E230), R222 (= R236), H223 (= H237), E361 (= E383), S364 (≠ G386), R412 (= R434)
- binding aspartic acid: E170 (= E165), Q192 (= Q207), K195 (≠ A210), Y339 (= Y361), S364 (≠ G386), R368 (= R390), F406 (= F428), G407 (= G429)
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)
32% identity, 97% coverage: 10:453/460 of query aligns to 11:431/438 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 (= K83) 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, 100% coverage: 1:458/460 of query aligns to 1:431/433 of 2xgtB
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E163 (= E165), S183 (= S205), Q185 (= Q207), R206 (= R228), E208 (= E230), H215 (= H237), L216 (≠ A238), Y219 (≠ F241), H221 (≠ M243), E223 (= E245), E356 (= E383), I357 (= I384), V358 (≠ I385), G359 (= G386), R363 (= R390), Y401 (≠ F428), G402 (= G429), G404 (= G431)
2xtiA Asparaginyl-tRNA synthetase from brugia malayi complexed with atp:mg and l-asp-beta-noh adenylate:ppi:mg (see paper)
30% identity, 100% coverage: 1:458/460 of query aligns to 3:431/433 of 2xtiA
- binding 5'-O-[(R)-{[(2S)-2-amino-4-(hydroxyamino)-4-oxobutanoyl]oxy}(hydroxy)phosphoryl]adenosine: E163 (= E165), S183 (= S205), Q185 (= Q207), R206 (= R228), E208 (= E230), H215 (= H237), L216 (≠ A238), Y219 (≠ F241), H221 (≠ M243), E223 (= E245), Y333 (= Y361), E356 (= E383), I357 (= I384), V358 (≠ I385), G359 (= G386), R363 (= R390), Y401 (≠ F428), G402 (= G429), G404 (= G431), R407 (= R434)
- binding pyrophosphate 2-: R214 (= R236), H215 (= H237), E356 (= E383), R407 (= R434)
2xtiB Asparaginyl-tRNA synthetase from brugia malayi complexed with atp:mg and l-asp-beta-noh adenylate:ppi:mg (see paper)
31% identity, 100% coverage: 1:458/460 of query aligns to 2:427/429 of 2xtiB
- binding adenosine-5'-triphosphate: R202 (= R228), E204 (= E230), R210 (= R236), H211 (= H237), L212 (≠ A238), Y215 (≠ F241), E352 (= E383), I353 (= I384), V354 (≠ I385), G400 (= G431), R403 (= R434)
8h53A Human asparaginyl-tRNA synthetase in complex with asparagine-amp (see paper)
28% identity, 97% coverage: 11:458/460 of query aligns to 10:425/427 of 8h53A
- binding imidodiphosphoric acid: R209 (= R236), H210 (= H237), E350 (= E383), R401 (= R434)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E158 (= E165), S178 (= S205), Q180 (= Q207), R201 (= R228), L211 (≠ A238), Y214 (≠ F241), H216 (≠ M243), E218 (= E245), E350 (= E383), I351 (= I384), V352 (≠ I385), R357 (= R390), Y395 (≠ F428), G396 (= G429), G398 (= G431), R401 (= R434)
8tc8A Human asparaginyl-tRNA synthetase bound to adenosine 5'-sulfamate (see paper)
28% identity, 97% coverage: 11:458/460 of query aligns to 12:433/435 of 8tc8A
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E166 (= E165), S186 (= S205), Q188 (= Q207), R209 (= R228), E211 (= E230), H218 (= H237), L219 (≠ A238), Y222 (≠ F241), H224 (≠ M243), E226 (= E245), E358 (= E383), I359 (= I384), V360 (≠ I385), R365 (= R390), Y403 (≠ F428), G404 (= G429), G406 (= G431)
8tc9A Human asparaginyl-tRNA synthetase bound to osm-s-106 (see paper)
27% identity, 97% coverage: 11:458/460 of query aligns to 12:432/434 of 8tc9A
- binding N~1~-[(3M)-3-(4-aminothieno[3,2-d]pyrimidin-6-yl)benzene-1-sulfonyl]-L-aspartamide: E165 (= E165), S185 (= S205), Q187 (= Q207), R208 (= R228), H217 (= H237), L218 (≠ A238), Y221 (≠ F241), H223 (≠ M243), E225 (= E245), R364 (= R390), Y402 (≠ F428), G403 (= G429), R408 (= R434)
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, 97% coverage: 15:459/460 of query aligns to 16:435/436 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 (≠ K83) 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
27% identity, 97% coverage: 16:459/460 of query aligns to 16:434/435 of 3m4pA
- active site: R211 (= R228), E213 (= E230), R219 (= R236), H220 (= H237), E358 (= E383), G361 (= G386), R409 (= R434)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: S188 (= S205), Q190 (= Q207), R211 (= R228), H220 (= H237), L221 (≠ A238), Y224 (≠ F241), H226 (≠ M243), E358 (= E383), I359 (= I384), V360 (≠ I385), R365 (= R390), Y403 (≠ F428), G404 (= G429), G406 (= G431), R409 (= R434)
1aszA The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction (see paper)
29% identity, 82% coverage: 75:453/460 of query aligns to 129:483/490 of 1aszA
- active site: R258 (= R228), E260 (= E230), R266 (= R236), H267 (= H237), E411 (= E383), S414 (≠ G386), R464 (= R434)
- binding adenosine-5'-triphosphate: R258 (= R228), M268 (≠ A238), F271 (= F241), E411 (= E383), I412 (= I384), L413 (≠ I385), G459 (= G429), R464 (= R434)
- binding : E135 (≠ Q81), P138 (= P85), L140 (≠ E87), A154 (≠ P101), L156 (≠ Y103), P157 (= P104), V158 (≠ L105), N160 (≠ K107), T163 (≠ H110), S213 (≠ C164), E214 (= E165), G215 (= G166), G216 (≠ A167), S217 (≠ G168), Q233 (≠ V204), F237 (≠ L208), E260 (= E230), N261 (= N231), S262 (= S232), N263 (= N233), H267 (= H237), S356 (≠ Q332), T357 (= T333), F388 (= F360)
Sites not aligning to the query:
- binding : 52, 53, 54, 57, 58, 60, 71, 73, 110, 112, 113, 486
1asyA Class ii aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA asp (see paper)
29% identity, 82% coverage: 75:453/460 of query aligns to 129:483/490 of 1asyA
- active site: R258 (= R228), E260 (= E230), R266 (= R236), H267 (= H237), E411 (= E383), S414 (≠ G386), R464 (= R434)
- binding : E135 (≠ Q81), P138 (= P85), A154 (≠ P101), L156 (≠ Y103), P157 (= P104), V158 (≠ L105), V159 (≠ Q106), D162 (≠ R109), T163 (≠ H110), R258 (= R228), E260 (= E230), N261 (= N231), S262 (= S232), N263 (= N233), T264 (= T234), H267 (= H237), M268 (≠ A238), F271 (= F241), T357 (= T333), E411 (= E383), I412 (= I384), L413 (≠ I385), S414 (≠ G386), G459 (= G429), R464 (= R434)
Sites not aligning to the query:
- binding : 52, 53, 54, 58, 60, 71, 73, 88, 111, 112, 113, 114, 486
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)
30% identity, 82% coverage: 75:453/460 of query aligns to 196:550/557 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
Q9RVH4 Aspartate--tRNA(Asp/Asn) ligase; Aspartyl-tRNA synthetase 2; AspRS2; Non-discriminating aspartyl-tRNA synthetase; ND-AspRS; EC 6.1.1.23 from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) (see paper)
26% identity, 98% coverage: 4:453/460 of query aligns to 7:428/435 of Q9RVH4
- H28 (≠ R25) mutation to Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn).
- P77 (≠ K83) mutation P->C,I,L,F,S,V: Seems not to be able to charge tRNA(Asn) in vivo, but Asp-tRNA(Asp) formation is not affected.; mutation to K: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn) and increasing the efficiency of Asp-tRNA(Asp) synthesis in vitro. Seems not to be able to charge tRNA(Asn) in vivo.
Query Sequence
>WP_005351729.1 NCBI__GCF_000173975.1:WP_005351729.1
MTIREIYKNSEQFLNKEVKLGGWIRSIRGSKHFGFLVLHDGTFFKPIQVVYEEKLENFQE
ISKMNVGAAVIVEGTLVPTPQAKQPFEIQAATVTLEGASAPDYPLQKKRHSLEYLRTISH
LRPRTNTFQAVFRIRSMAAYAIHQFFQERGFVYVHTPLITASDCEGAGEMFQVTTLDLNN
IPKDKEGNVDFAQDFFNKPTNLTVSGQLNAETFAQAFRNTYTFGPTFRAENSNTARHAAE
FWMIEPEMAFADLKDDMEVAEAMLKYVISYVMENAPEEMDFLNQFVDKGLKDRLNHVLNS
EFGHVTYTEAVEILEKHNDKFEYKVSWGTDLQTEHERYLTEEVFKRPVFVTDYPKEIKAF
YMKLNPDGKTVAAMDCLVPGIGEIIGGSQREDDYEMLKKRMEEVGLDEEKYQFYLDLRKY
GSTHHSGFGLGFERCVMYLTGISNIRDAIPFPRTVNNCEL
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