SitesBLAST
Comparing Synpcc7942_0830 FitnessBrowser__SynE:Synpcc7942_0830 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)
58% identity, 100% coverage: 1:462/462 of query aligns to 1:466/466 of P0A8M0
- M1 (= M1) modified: Initiator methionine, Removed
- Y426 (= Y422) mutation to F: No effect.; mutation to S: 15-fold increase in Km for ATP.
1x55A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate analogue (see paper)
36% identity, 96% coverage: 16:457/462 of query aligns to 16:429/434 of 1x55A
- active site: R211 (= R230), E213 (= E232), R219 (= R238), H220 (= H239), E357 (= E385), G360 (= G388), R408 (= R436)
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E168 (= E168), S188 (= S207), Q190 (= Q209), R211 (= R230), H220 (= H239), L221 (= L240), F224 (= F243), H226 (≠ M245), E228 (= E247), E357 (= E385), I358 (= I386), I359 (= I387), R364 (= R392), F402 (= F430), G403 (= G431), G405 (= G433), R408 (= R436)
1x54A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate (see paper)
36% identity, 96% coverage: 16:457/462 of query aligns to 16:429/434 of 1x54A
- active site: R211 (= R230), E213 (= E232), R219 (= R238), H220 (= H239), E357 (= E385), G360 (= G388), R408 (= R436)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E168 (= E168), S188 (= S207), Q190 (= Q209), R211 (= R230), H220 (= H239), L221 (= L240), F224 (= F243), H226 (≠ M245), E228 (= E247), E357 (= E385), I358 (= I386), I359 (= I387), R364 (= R392), F402 (= F430), G403 (= G431), G405 (= G433), R408 (= R436)
1b8aA Aspartyl-tRNA synthetase (see paper)
31% identity, 95% coverage: 16:455/462 of query aligns to 16:431/438 of 1b8aA
- binding adenosine-5'-triphosphate: R214 (= R230), E216 (= E232), H223 (= H239), L224 (= L240), E361 (= E385), I362 (= I386), S363 (≠ I387), S364 (≠ G388), G409 (= G433), R412 (= R436)
- binding manganese (ii) ion: E361 (= E385), S364 (≠ G388)
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
31% identity, 95% coverage: 16:455/462 of query aligns to 16:431/438 of 3nemB
- active site: R214 (= R230), E216 (= E232), R222 (= R238), H223 (= H239), E361 (= E385), S364 (≠ G388), R412 (= R436)
- binding adenosine-5'-triphosphate: R214 (= R230), E216 (= E232), H223 (= H239), L224 (= L240), E361 (= E385), I362 (= I386), S363 (≠ I387), S364 (≠ G388), G407 (= G431), G409 (= G433), R412 (= R436)
- binding magnesium ion: E361 (= E385), S364 (≠ G388)
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
31% identity, 95% coverage: 16:455/462 of query aligns to 16:431/438 of 3nemA
- active site: R214 (= R230), E216 (= E232), R222 (= R238), H223 (= H239), E361 (= E385), S364 (≠ G388), R412 (= R436)
- binding aspartyl-adenosine-5'-monophosphate: E170 (= E168), Q192 (= Q209), K195 (≠ A212), R214 (= R230), E216 (= E232), H223 (= H239), L224 (= L240), Y339 (= Y363), E361 (= E385), I362 (= I386), S363 (≠ I387), S364 (≠ G388), G365 (= G389), R368 (= R392), F406 (= F430), G407 (= G431), G409 (= G433), R412 (= R436)
3nelA Aspartyl-tRNA synthetase complexed with aspartic acid (see paper)
31% identity, 95% coverage: 16:455/462 of query aligns to 16:431/438 of 3nelA
- active site: R214 (= R230), E216 (= E232), R222 (= R238), H223 (= H239), E361 (= E385), S364 (≠ G388), R412 (= R436)
- binding aspartic acid: E170 (= E168), Q192 (= Q209), K195 (≠ A212), Y339 (= Y363), S364 (≠ G388), R368 (= R392), F406 (= F430), G407 (= G431)
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, 95% coverage: 16:455/462 of query aligns to 16:431/438 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 (≠ G85) 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).
8h53A Human asparaginyl-tRNA synthetase in complex with asparagine-amp
30% identity, 97% coverage: 12:460/462 of query aligns to 10:425/427 of 8h53A
- binding imidodiphosphoric acid: R209 (= R238), H210 (= H239), E350 (= E385), R401 (= R436)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E158 (= E168), S178 (= S207), Q180 (= Q209), R201 (= R230), L211 (= L240), Y214 (≠ F243), H216 (≠ M245), E218 (= E247), E350 (= E385), I351 (= I386), V352 (≠ I387), R357 (= R392), Y395 (≠ F430), G396 (= G431), G398 (= G433), R401 (= R436)
2xgtB Asparaginyl-tRNA synthetase from brugia malayi complexed with the sulphamoyl analogue of asparaginyl-adenylate (see paper)
31% identity, 98% coverage: 4:455/462 of query aligns to 1:426/433 of 2xgtB
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E163 (= E168), S183 (= S207), Q185 (= Q209), R206 (= R230), E208 (= E232), H215 (= H239), L216 (= L240), Y219 (≠ F243), H221 (≠ M245), E223 (= E247), E356 (= E385), I357 (= I386), V358 (≠ I387), G359 (= G388), R363 (= R392), Y401 (≠ F430), G402 (= G431), G404 (= G433)
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: 2:455/462 of query aligns to 1:426/433 of 2xtiA
- binding 5'-O-[(R)-{[(2S)-2-amino-4-(hydroxyamino)-4-oxobutanoyl]oxy}(hydroxy)phosphoryl]adenosine: E163 (= E168), S183 (= S207), Q185 (= Q209), R206 (= R230), E208 (= E232), H215 (= H239), L216 (= L240), Y219 (≠ F243), H221 (≠ M245), E223 (= E247), Y333 (= Y363), E356 (= E385), I357 (= I386), V358 (≠ I387), G359 (= G388), R363 (= R392), Y401 (≠ F430), G402 (= G431), G404 (= G433), R407 (= R436)
- binding pyrophosphate 2-: R214 (= R238), H215 (= H239), E356 (= E385), R407 (= R436)
8tc9A Human asparaginyl-tRNA synthetase bound to osm-s-106 (see paper)
31% identity, 97% coverage: 12:460/462 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 (= E168), S185 (= S207), Q187 (= Q209), R208 (= R230), H217 (= H239), L218 (= L240), Y221 (≠ F243), H223 (≠ M245), E225 (= E247), R364 (= R392), Y402 (≠ F430), G403 (= G431), R408 (= R436)
8tc8A Human asparaginyl-tRNA synthetase bound to adenosine 5'-sulfamate (see paper)
30% identity, 97% coverage: 12:460/462 of query aligns to 12:433/435 of 8tc8A
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E166 (= E168), S186 (= S207), Q188 (= Q209), R209 (= R230), E211 (= E232), H218 (= H239), L219 (= L240), Y222 (≠ F243), H224 (≠ M245), E226 (= E247), E358 (= E385), I359 (= I386), V360 (≠ I387), R365 (= R392), Y403 (≠ F430), G404 (= G431), G406 (= G433)
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: 4:455/462 of query aligns to 2:422/429 of 2xtiB
- binding adenosine-5'-triphosphate: R202 (= R230), E204 (= E232), R210 (= R238), H211 (= H239), L212 (= L240), Y215 (≠ F243), E352 (= E385), I353 (= I386), V354 (≠ I387), G400 (= G433), R403 (= R436)
3m4pA Entamoeba histolytica asparaginyl-tRNA synthetase (asnrs) in complex with asparaginyl-adenylate
27% identity, 97% coverage: 13:461/462 of query aligns to 12:434/435 of 3m4pA
- active site: R211 (= R230), E213 (= E232), R219 (= R238), H220 (= H239), E358 (= E385), G361 (= G388), R409 (= R436)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: S188 (= S207), Q190 (= Q209), R211 (= R230), H220 (= H239), L221 (= L240), Y224 (≠ F243), H226 (≠ M245), E358 (= E385), I359 (= I386), V360 (≠ I387), R365 (= R392), Y403 (≠ F430), G404 (= G431), G406 (= G433), R409 (= R436)
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: 16:461/462 of query aligns to 16:435/436 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 (≠ G85) mutation P->A,K: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn).
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, 72% coverage: 127:458/462 of query aligns to 240:553/557 of P04802
- P273 (= P160) 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)
30% identity, 72% coverage: 127:458/462 of query aligns to 173:486/490 of 1aszA
- active site: R258 (= R230), E260 (= E232), R266 (= R238), H267 (= H239), E411 (= E385), S414 (≠ G388), R464 (= R436)
- binding adenosine-5'-triphosphate: R258 (= R230), M268 (≠ L240), F271 (= F243), E411 (= E385), I412 (= I386), L413 (≠ I387), G459 (= G431), R464 (= R436)
- binding : S213 (≠ C167), E214 (= E168), G215 (= G169), G216 (≠ A170), S217 (≠ G171), Q233 (≠ V206), F237 (≠ L210), E260 (= E232), N261 (= N233), S262 (= S234), N263 (= N235), H267 (= H239), S356 (≠ Q334), T357 (≠ S335), F388 (= F362), K486 (≠ Q458)
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)
30% identity, 72% coverage: 127:458/462 of query aligns to 173:486/490 of 1asyA
- active site: R258 (= R230), E260 (= E232), R266 (= R238), H267 (= H239), E411 (= E385), S414 (≠ G388), R464 (= R436)
- binding : R258 (= R230), E260 (= E232), N261 (= N233), S262 (= S234), N263 (= N235), T264 (= T236), H267 (= H239), M268 (≠ L240), F271 (= F243), T357 (≠ S335), E411 (= E385), I412 (= I386), L413 (≠ I387), S414 (≠ G388), G459 (= G431), R464 (= R436), K486 (≠ Q458)
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
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)
27% identity, 95% coverage: 16:455/462 of query aligns to 18:428/435 of Q9RVH4
- H28 (≠ R26) mutation to Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn).
- P77 (≠ G85) 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
>Synpcc7942_0830 FitnessBrowser__SynE:Synpcc7942_0830
MASARIVDLLSQGQPGQTVVVRGWIRTARQLKEFTFVEVNDGSCLKGIQVVLGQELADYE
MLAKQLDTGAAIAVEGQLVASPAKGQRVELQAASVEIVGGADPEQYPLQKKRHSFEFLRT
IAHLRPRTNSLGAVMRVRNAAATAIHDFFQERGFLWVHTPIITASDCEGAGELFTVTNLD
LDKLGQSQQAPDFEQDFFGKRAYLTVSGQLEAEIMALAFSNVYTFGPTFRAENSNTSRHL
AEFWMVEPEMAFCDLGGDMDLAEAFLKFVFQRVSDRCSEDLEFFNQRIDSEVLNRAETIL
NNDFERVSYTDAIALLEKADRSFDYPVAWGIDLQSEHERYLAEEYFRKPLIVYDYPREIK
AFYMRLNDDQKTVAAMDVLAPGIGEIIGGSQREERLDVLKQRLAEANLPEENYWWYLDLR
RYGSVPHAGFGLGFERLVQFITGMGNIRDVIPFPRTPQNAEF
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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