SitesBLAST
Comparing 208934 MicrobesOnline__882:208934 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)
56% identity, 100% coverage: 1:461/461 of query aligns to 1:466/466 of P0A8M0
- M1 (= M1) modified: Initiator methionine, Removed
- Y426 (≠ F421) 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)
37% identity, 96% coverage: 19:459/461 of query aligns to 19:432/434 of 1x55A
- active site: R211 (= R229), E213 (= E231), R219 (= R237), H220 (= H238), E357 (= E384), G360 (= G387), R408 (= R435)
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E168 (= E167), S188 (= S206), Q190 (= Q208), R211 (= R229), H220 (= H238), L221 (≠ A239), F224 (= F242), H226 (≠ M244), E228 (= E246), E357 (= E384), I358 (≠ L385), I359 (= I386), R364 (= R391), F402 (= F429), G403 (= G430), G405 (= G432), R408 (= R435)
1x54A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate (see paper)
37% identity, 96% coverage: 19:459/461 of query aligns to 19:432/434 of 1x54A
- active site: R211 (= R229), E213 (= E231), R219 (= R237), H220 (= H238), E357 (= E384), G360 (= G387), R408 (= R435)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E168 (= E167), S188 (= S206), Q190 (= Q208), R211 (= R229), H220 (= H238), L221 (≠ A239), F224 (= F242), H226 (≠ M244), E228 (= E246), E357 (= E384), I358 (≠ L385), I359 (= I386), R364 (= R391), F402 (= F429), G403 (= G430), G405 (= G432), R408 (= R435)
8h53A Human asparaginyl-tRNA synthetase in complex with asparagine-amp
30% identity, 95% coverage: 19:454/461 of query aligns to 17:420/427 of 8h53A
- binding imidodiphosphoric acid: R209 (= R237), H210 (= H238), E350 (= E384), R401 (= R435)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E158 (= E167), S178 (= S206), Q180 (= Q208), R201 (= R229), L211 (≠ A239), Y214 (≠ F242), H216 (≠ M244), E218 (= E246), E350 (= E384), I351 (≠ L385), V352 (≠ I386), R357 (= R391), Y395 (≠ F429), G396 (= G430), G398 (= G432), R401 (= R435)
1b8aA Aspartyl-tRNA synthetase (see paper)
31% identity, 98% coverage: 1:454/461 of query aligns to 1:431/438 of 1b8aA
- binding adenosine-5'-triphosphate: R214 (= R229), E216 (= E231), H223 (= H238), L224 (≠ A239), E361 (= E384), I362 (≠ L385), S363 (≠ I386), S364 (≠ G387), G409 (= G432), R412 (= R435)
- binding manganese (ii) ion: E361 (= E384), S364 (≠ G387)
8tc9A Human asparaginyl-tRNA synthetase bound to osm-s-106 (see paper)
30% identity, 95% coverage: 19:454/461 of query aligns to 19:427/434 of 8tc9A
- binding N~1~-[(3M)-3-(4-aminothieno[3,2-d]pyrimidin-6-yl)benzene-1-sulfonyl]-L-aspartamide: E165 (= E167), S185 (= S206), Q187 (= Q208), R208 (= R229), H217 (= H238), L218 (≠ A239), Y221 (≠ F242), H223 (≠ M244), E225 (= E246), R364 (= R391), Y402 (≠ F429), G403 (= G430), R408 (= R435)
8tc8A Human asparaginyl-tRNA synthetase bound to adenosine 5'-sulfamate (see paper)
30% identity, 95% coverage: 19:454/461 of query aligns to 19:428/435 of 8tc8A
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E166 (= E167), S186 (= S206), Q188 (= Q208), R209 (= R229), E211 (= E231), H218 (= H238), L219 (≠ A239), Y222 (≠ F242), H224 (≠ M244), E226 (= E246), E358 (= E384), I359 (≠ L385), V360 (≠ I386), R365 (= R391), Y403 (≠ F429), G404 (= G430), G406 (= G432)
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
30% identity, 98% coverage: 1:454/461 of query aligns to 1:431/438 of 3nemB
- active site: R214 (= R229), E216 (= E231), R222 (= R237), H223 (= H238), E361 (= E384), S364 (≠ G387), R412 (= R435)
- binding adenosine-5'-triphosphate: R214 (= R229), E216 (= E231), H223 (= H238), L224 (≠ A239), E361 (= E384), I362 (≠ L385), S363 (≠ I386), S364 (≠ G387), G407 (= G430), G409 (= G432), R412 (= R435)
- binding magnesium ion: E361 (= E384), S364 (≠ G387)
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
30% identity, 98% coverage: 1:454/461 of query aligns to 1:431/438 of 3nemA
- active site: R214 (= R229), E216 (= E231), R222 (= R237), H223 (= H238), E361 (= E384), S364 (≠ G387), R412 (= R435)
- binding aspartyl-adenosine-5'-monophosphate: E170 (= E167), Q192 (= Q208), K195 (≠ A211), R214 (= R229), E216 (= E231), H223 (= H238), L224 (≠ A239), Y339 (= Y362), E361 (= E384), I362 (≠ L385), S363 (≠ I386), S364 (≠ G387), G365 (= G388), R368 (= R391), F406 (= F429), G407 (= G430), G409 (= G432), R412 (= R435)
3nelA Aspartyl-tRNA synthetase complexed with aspartic acid (see paper)
30% identity, 98% coverage: 1:454/461 of query aligns to 1:431/438 of 3nelA
- active site: R214 (= R229), E216 (= E231), R222 (= R237), H223 (= H238), E361 (= E384), S364 (≠ G387), R412 (= R435)
- binding aspartic acid: E170 (= E167), Q192 (= Q208), K195 (≠ A211), Y339 (= Y362), S364 (≠ G387), R368 (= R391), F406 (= F429), G407 (= G430)
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, 98% coverage: 1:454/461 of query aligns to 1:431/438 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 (≠ G84) 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, 95% coverage: 20:457/461 of query aligns to 13:429/433 of 2xgtB
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E163 (= E167), S183 (= S206), Q185 (= Q208), R206 (= R229), E208 (= E231), H215 (= H238), L216 (≠ A239), Y219 (≠ F242), H221 (≠ M244), E223 (= E246), E356 (= E384), I357 (≠ L385), V358 (≠ I386), G359 (= G387), R363 (= R391), Y401 (≠ F429), G402 (= G430), G404 (= G432)
2xtiA Asparaginyl-tRNA synthetase from brugia malayi complexed with atp:mg and l-asp-beta-noh adenylate:ppi:mg (see paper)
30% identity, 95% coverage: 20:457/461 of query aligns to 15:429/433 of 2xtiA
- binding 5'-O-[(R)-{[(2S)-2-amino-4-(hydroxyamino)-4-oxobutanoyl]oxy}(hydroxy)phosphoryl]adenosine: E163 (= E167), S183 (= S206), Q185 (= Q208), R206 (= R229), E208 (= E231), H215 (= H238), L216 (≠ A239), Y219 (≠ F242), H221 (≠ M244), E223 (= E246), Y333 (= Y362), E356 (= E384), I357 (≠ L385), V358 (≠ I386), G359 (= G387), R363 (= R391), Y401 (≠ F429), G402 (= G430), G404 (= G432), R407 (= R435)
- binding pyrophosphate 2-: R214 (= R237), H215 (= H238), E356 (= E384), R407 (= R435)
2xtiB Asparaginyl-tRNA synthetase from brugia malayi complexed with atp:mg and l-asp-beta-noh adenylate:ppi:mg (see paper)
30% identity, 95% coverage: 20:457/461 of query aligns to 14:425/429 of 2xtiB
- binding adenosine-5'-triphosphate: R202 (= R229), E204 (= E231), R210 (= R237), H211 (= H238), L212 (≠ A239), Y215 (≠ F242), E352 (= E384), I353 (≠ L385), V354 (≠ I386), G400 (= G432), R403 (= R435)
3m4pA Entamoeba histolytica asparaginyl-tRNA synthetase (asnrs) in complex with asparaginyl-adenylate
27% identity, 94% coverage: 23:454/461 of query aligns to 22:428/435 of 3m4pA
- active site: R211 (= R229), E213 (= E231), R219 (= R237), H220 (= H238), E358 (= E384), G361 (= G387), R409 (= R435)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: S188 (= S206), Q190 (= Q208), R211 (= R229), H220 (= H238), L221 (≠ A239), Y224 (≠ F242), H226 (≠ M244), E358 (= E384), I359 (≠ L385), V360 (≠ I386), R365 (= R391), Y403 (≠ F429), G404 (= G430), G406 (= G432), R409 (= R435)
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)
29% identity, 100% coverage: 1:460/461 of query aligns to 2:435/436 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 (≠ G84) mutation P->A,K: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn).
1aszA The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction (see paper)
30% identity, 74% coverage: 120:459/461 of query aligns to 169:488/490 of 1aszA
- active site: R258 (= R229), E260 (= E231), R266 (= R237), H267 (= H238), E411 (= E384), S414 (≠ G387), R464 (= R435)
- binding adenosine-5'-triphosphate: R258 (= R229), M268 (≠ A239), F271 (= F242), E411 (= E384), I412 (≠ L385), L413 (≠ I386), G459 (= G430), R464 (= R435)
- binding : S213 (≠ C166), E214 (= E167), G215 (= G168), G216 (≠ A169), S217 (≠ G170), Q233 (≠ V205), F237 (≠ L209), E260 (= E231), N261 (= N232), S262 (= S233), N263 (= N234), H267 (= H238), S356 (≠ Q333), T357 (= T334), F388 (= F361), K486 (≠ G457)
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, 74% coverage: 120:459/461 of query aligns to 169:488/490 of 1asyA
- active site: R258 (= R229), E260 (= E231), R266 (= R237), H267 (= H238), E411 (= E384), S414 (≠ G387), R464 (= R435)
- binding : R258 (= R229), E260 (= E231), N261 (= N232), S262 (= S233), N263 (= N234), T264 (= T235), H267 (= H238), M268 (≠ A239), F271 (= F242), T357 (= T334), E411 (= E384), I412 (≠ L385), L413 (≠ I386), S414 (≠ G387), G459 (= G430), R464 (= R435), K486 (≠ G457)
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)
30% identity, 74% coverage: 120:459/461 of query aligns to 236:555/557 of P04802
- P273 (= P159) 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, 95% coverage: 19:454/461 of query aligns to 21:428/435 of Q9RVH4
- H28 (≠ R26) mutation to Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn).
- P77 (≠ G84) 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
>208934 MicrobesOnline__882:208934
MQRTQIVDALAATAPQPVIRLCGWVRTRRDAKGFSFLEINDGSCLANIQAIVDEGIPAYA
NIGAVSTGAAVDITGELVESPGKGQKWEVRVQTLTLLGAADAETYPLQKKRHSDEFLRSI
AHLRARTNKYGAAFRIRSEAAFAIHEFYRERGFFYVHTPILTGSDCEGAGEMFRVTTLPV
EGSATPASGNRYENDFFGKECNLTVSGQLEAETLALGLGKVYTFGPTFRAENSNTPRHAA
EFWMIEPEVAFADLEEDMNLAEDMTRTVVRRILDRCAADLDLFNRFVDTTLVERLRQIAD
EPFARCSYTEAIELLLKSGKKFEYPVSFGLDLQTEHERYLAEEHFGKPVIVYNYPKEIKA
FYMRLNDDGRTVAAMDVLVPRIGELIGGSQREERLDVLEARINEMGQNLEDYWWYLDLRR
FGSVPHAGFGMGFERLLMLLTGITNIRDVIPFPRTPGNLEF
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