SitesBLAST
Comparing 353399 FitnessBrowser__Btheta:353399 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)
57% identity, 98% coverage: 9:467/467 of query aligns to 6:466/466 of P0A8M0
- Y426 (≠ F427) 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)
34% identity, 96% coverage: 13:462/467 of query aligns to 10:429/434 of 1x55A
- active site: R211 (= R232), E213 (= E234), R219 (= R240), H220 (= H241), E357 (= E390), G360 (= G393), R408 (= R441)
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E168 (= E169), S188 (= S209), Q190 (= Q211), R211 (= R232), H220 (= H241), L221 (= L242), F224 (= F245), H226 (≠ M247), E228 (= E249), E357 (= E390), I358 (= I391), I359 (= I392), R364 (= R397), F402 (= F435), G403 (= G436), G405 (= G438), R408 (= R441)
1x54A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate (see paper)
34% identity, 96% coverage: 13:462/467 of query aligns to 10:429/434 of 1x54A
- active site: R211 (= R232), E213 (= E234), R219 (= R240), H220 (= H241), E357 (= E390), G360 (= G393), R408 (= R441)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E168 (= E169), S188 (= S209), Q190 (= Q211), R211 (= R232), H220 (= H241), L221 (= L242), F224 (= F245), H226 (≠ M247), E228 (= E249), E357 (= E390), I358 (= I391), I359 (= I392), R364 (= R397), F402 (= F435), G403 (= G436), G405 (= G438), R408 (= R441)
2xgtB Asparaginyl-tRNA synthetase from brugia malayi complexed with the sulphamoyl analogue of asparaginyl-adenylate (see paper)
30% identity, 97% coverage: 7:460/467 of query aligns to 1:426/433 of 2xgtB
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E163 (= E169), S183 (= S209), Q185 (= Q211), R206 (= R232), E208 (= E234), H215 (= H241), L216 (= L242), Y219 (≠ F245), H221 (≠ M247), E223 (= E249), E356 (= E390), I357 (= I391), V358 (≠ I392), G359 (= G393), R363 (= R397), Y401 (≠ F435), G402 (= G436), G404 (= G438)
2xtiA Asparaginyl-tRNA synthetase from brugia malayi complexed with atp:mg and l-asp-beta-noh adenylate:ppi:mg (see paper)
30% identity, 97% coverage: 7:460/467 of query aligns to 3:426/433 of 2xtiA
- binding 5'-O-[(R)-{[(2S)-2-amino-4-(hydroxyamino)-4-oxobutanoyl]oxy}(hydroxy)phosphoryl]adenosine: E163 (= E169), S183 (= S209), Q185 (= Q211), R206 (= R232), E208 (= E234), H215 (= H241), L216 (= L242), Y219 (≠ F245), H221 (≠ M247), E223 (= E249), Y333 (= Y368), E356 (= E390), I357 (= I391), V358 (≠ I392), G359 (= G393), R363 (= R397), Y401 (≠ F435), G402 (= G436), G404 (= G438), R407 (= R441)
- binding pyrophosphate 2-: R214 (= R240), H215 (= H241), E356 (= E390), R407 (= R441)
2xtiB Asparaginyl-tRNA synthetase from brugia malayi complexed with atp:mg and l-asp-beta-noh adenylate:ppi:mg (see paper)
30% identity, 97% coverage: 7:460/467 of query aligns to 2:422/429 of 2xtiB
- binding adenosine-5'-triphosphate: R202 (= R232), E204 (= E234), R210 (= R240), H211 (= H241), L212 (= L242), Y215 (≠ F245), E352 (= E390), I353 (= I391), V354 (≠ I392), G400 (= G438), R403 (= R441)
8tc9A Human asparaginyl-tRNA synthetase bound to osm-s-106 (see paper)
29% identity, 95% coverage: 19:460/467 of query aligns to 16:427/434 of 8tc9A
- binding N~1~-[(3M)-3-(4-aminothieno[3,2-d]pyrimidin-6-yl)benzene-1-sulfonyl]-L-aspartamide: E165 (= E169), S185 (= S209), Q187 (= Q211), R208 (= R232), H217 (= H241), L218 (= L242), Y221 (≠ F245), H223 (≠ M247), E225 (= E249), R364 (= R397), Y402 (≠ F435), G403 (= G436), R408 (= R441)
8h53A Human asparaginyl-tRNA synthetase in complex with asparagine-amp
29% identity, 95% coverage: 19:460/467 of query aligns to 14:420/427 of 8h53A
- binding imidodiphosphoric acid: R209 (= R240), H210 (= H241), E350 (= E390), R401 (= R441)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E158 (= E169), S178 (= S209), Q180 (= Q211), R201 (= R232), L211 (= L242), Y214 (≠ F245), H216 (≠ M247), E218 (= E249), E350 (= E390), I351 (= I391), V352 (≠ I392), R357 (= R397), Y395 (≠ F435), G396 (= G436), G398 (= G438), R401 (= R441)
8tc8A Human asparaginyl-tRNA synthetase bound to adenosine 5'-sulfamate (see paper)
29% identity, 95% coverage: 19:460/467 of query aligns to 16:428/435 of 8tc8A
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E166 (= E169), S186 (= S209), Q188 (= Q211), R209 (= R232), E211 (= E234), H218 (= H241), L219 (= L242), Y222 (≠ F245), H224 (≠ M247), E226 (= E249), E358 (= E390), I359 (= I391), V360 (≠ I392), R365 (= R397), Y403 (≠ F435), G404 (= G436), G406 (= G438)
1b8aA Aspartyl-tRNA synthetase (see paper)
30% identity, 98% coverage: 6:463/467 of query aligns to 3:434/438 of 1b8aA
- binding adenosine-5'-triphosphate: R214 (= R232), E216 (= E234), H223 (= H241), L224 (= L242), E361 (= E390), I362 (= I391), S363 (≠ I392), S364 (≠ G393), G409 (= G438), R412 (= R441)
- binding manganese (ii) ion: E361 (= E390), S364 (≠ G393)
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
29% identity, 98% coverage: 6:463/467 of query aligns to 3:434/438 of 3nemB
- active site: R214 (= R232), E216 (= E234), R222 (= R240), H223 (= H241), E361 (= E390), S364 (≠ G393), R412 (= R441)
- binding adenosine-5'-triphosphate: R214 (= R232), E216 (= E234), H223 (= H241), L224 (= L242), E361 (= E390), I362 (= I391), S363 (≠ I392), S364 (≠ G393), G407 (= G436), G409 (= G438), R412 (= R441)
- binding magnesium ion: E361 (= E390), S364 (≠ G393)
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
29% identity, 98% coverage: 6:463/467 of query aligns to 3:434/438 of 3nemA
- active site: R214 (= R232), E216 (= E234), R222 (= R240), H223 (= H241), E361 (= E390), S364 (≠ G393), R412 (= R441)
- binding aspartyl-adenosine-5'-monophosphate: E170 (= E169), Q192 (= Q211), K195 (≠ G214), R214 (= R232), E216 (= E234), H223 (= H241), L224 (= L242), Y339 (= Y368), E361 (= E390), I362 (= I391), S363 (≠ I392), S364 (≠ G393), G365 (= G394), R368 (= R397), F406 (= F435), G407 (= G436), G409 (= G438), R412 (= R441)
3nelA Aspartyl-tRNA synthetase complexed with aspartic acid (see paper)
29% identity, 98% coverage: 6:463/467 of query aligns to 3:434/438 of 3nelA
- active site: R214 (= R232), E216 (= E234), R222 (= R240), H223 (= H241), E361 (= E390), S364 (≠ G393), R412 (= R441)
- binding aspartic acid: E170 (= E169), Q192 (= Q211), K195 (≠ G214), Y339 (= Y368), S364 (≠ G393), R368 (= R397), F406 (= F435), G407 (= G436)
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)
29% identity, 98% coverage: 6:463/467 of query aligns to 3:434/438 of Q52428
- W26 (≠ R29) 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 (≠ G87) 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).
3m4pA Entamoeba histolytica asparaginyl-tRNA synthetase (asnrs) in complex with asparaginyl-adenylate
27% identity, 95% coverage: 19:460/467 of query aligns to 15:428/435 of 3m4pA
- active site: R211 (= R232), E213 (= E234), R219 (= R240), H220 (= H241), E358 (= E390), G361 (= G393), R409 (= R441)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: S188 (= S209), Q190 (= Q211), R211 (= R232), H220 (= H241), L221 (= L242), Y224 (≠ F245), H226 (≠ M247), E358 (= E390), I359 (= I391), V360 (≠ I392), R365 (= R397), Y403 (≠ F435), G404 (= G436), G406 (= G438), R409 (= R441)
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)
25% identity, 98% coverage: 6:462/467 of query aligns to 4:431/436 of O07683
- H26 (≠ R29) mutation H->A,Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn).
- P84 (≠ G87) mutation P->A,K: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn).
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)
26% identity, 98% coverage: 7:463/467 of query aligns to 93:576/580 of O74407
- S282 (≠ T164) modified: Phosphoserine
- S307 (= S209) modified: Phosphoserine
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: 128:463/467 of query aligns to 240:553/557 of P04802
- P273 (= P161) 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)
29% identity, 72% coverage: 128:463/467 of query aligns to 173:486/490 of 1aszA
- active site: R258 (= R232), E260 (= E234), R266 (= R240), H267 (= H241), E411 (= E390), S414 (≠ G393), R464 (= R441)
- binding adenosine-5'-triphosphate: R258 (= R232), M268 (≠ L242), F271 (= F245), E411 (= E390), I412 (= I391), L413 (≠ I392), G459 (= G436), R464 (= R441)
- binding : S213 (≠ C168), E214 (= E169), G215 (= G170), G216 (≠ A171), S217 (≠ G172), Q233 (≠ V208), F237 (≠ L212), E260 (= E234), N261 (= N235), S262 (= S236), N263 (= N237), H267 (= H241), S356 (≠ A339), T357 (≠ S340), F388 (= F367), K486 (≠ R463)
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: 128:463/467 of query aligns to 173:486/490 of 1asyA
- active site: R258 (= R232), E260 (= E234), R266 (= R240), H267 (= H241), E411 (= E390), S414 (≠ G393), R464 (= R441)
- binding : R258 (= R232), E260 (= E234), N261 (= N235), S262 (= S236), N263 (= N237), T264 (= T238), H267 (= H241), M268 (≠ L242), F271 (= F245), T357 (≠ S340), E411 (= E390), I412 (= I391), L413 (≠ I392), S414 (≠ G393), G459 (= G436), R464 (= R441), K486 (≠ R463)
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
Query Sequence
>353399 FitnessBrowser__Btheta:353399
MEKIGRTKIVDLLKREDIGAMVNVKGWVRTRRGSKQVNFIALNDGSTINNVQIVVDLANF
DEEMLKLITTGACISVNGVMVESVGSGQKVEVQAKEIEVLGTCDNTYPLQKKGHSMEFLR
EIAHLRPRTNTFGAVFRIRHNMAIAIHKFFHEKGFFYFHTPIITGSDCEGAGQMFQVTTM
NLYDLKKDERGSISYDDDFFGKQASLTVSGQLEGELAATALGAIYTFGPTFRAENSNTPR
HLAEFWMIEPEVAFNDIADNMDLAEEFIKYCVKWALDNCADDVKFLNDMFDKGLIERLQG
VLKDDFVRLPYTDGIKILEDAVAKGHKFEFPVYWGVDLASEHERYLVEEHFKRPVILTDY
PKEIKAFYMKQNEDGKTVRAMDVLFPKIGEIIGGSEREADYNKLMTRIEEMHIPMKDMWW
YLDTRKFGTCPHSGFGLGFERLLLFVTGMSNIRDVIPFPRTPRNADF
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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