SitesBLAST
Comparing WP_011188572.1 NCBI__GCF_000025945.1:WP_011188572.1 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)
59% identity, 95% coverage: 18:444/449 of query aligns to 20:461/466 of P0A8M0
- Y426 (= Y409) 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)
38% identity, 95% coverage: 18:445/449 of query aligns to 19:430/434 of 1x55A
- active site: R211 (= R217), E213 (= E219), R219 (= R225), H220 (= H226), E357 (= E372), G360 (= G375), R408 (= R423)
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E168 (= E167), S188 (= S194), Q190 (= Q196), R211 (= R217), H220 (= H226), L221 (= L227), F224 (= F230), H226 (≠ M232), E228 (= E234), E357 (= E372), I358 (≠ L373), I359 (≠ V374), R364 (= R379), F402 (= F417), G403 (= G418), G405 (= G420), R408 (= R423)
1x54A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate (see paper)
38% identity, 95% coverage: 18:445/449 of query aligns to 19:430/434 of 1x54A
- active site: R211 (= R217), E213 (= E219), R219 (= R225), H220 (= H226), E357 (= E372), G360 (= G375), R408 (= R423)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E168 (= E167), S188 (= S194), Q190 (= Q196), R211 (= R217), H220 (= H226), L221 (= L227), F224 (= F230), H226 (≠ M232), E228 (= E234), E357 (= E372), I358 (≠ L373), I359 (≠ V374), R364 (= R379), F402 (= F417), G403 (= G418), G405 (= G420), R408 (= R423)
1b8aA Aspartyl-tRNA synthetase (see paper)
33% identity, 95% coverage: 16:442/449 of query aligns to 17:431/438 of 1b8aA
- binding adenosine-5'-triphosphate: R214 (= R217), E216 (= E219), H223 (= H226), L224 (= L227), E361 (= E372), I362 (≠ L373), S363 (≠ V374), S364 (≠ G375), G409 (= G420), R412 (= R423)
- binding manganese (ii) ion: E361 (= E372), S364 (≠ G375)
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
32% identity, 95% coverage: 16:442/449 of query aligns to 17:431/438 of 3nemB
- active site: R214 (= R217), E216 (= E219), R222 (= R225), H223 (= H226), E361 (= E372), S364 (≠ G375), R412 (= R423)
- binding adenosine-5'-triphosphate: R214 (= R217), E216 (= E219), H223 (= H226), L224 (= L227), E361 (= E372), I362 (≠ L373), S363 (≠ V374), S364 (≠ G375), G407 (= G418), G409 (= G420), R412 (= R423)
- binding magnesium ion: E361 (= E372), S364 (≠ G375)
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
32% identity, 95% coverage: 16:442/449 of query aligns to 17:431/438 of 3nemA
- active site: R214 (= R217), E216 (= E219), R222 (= R225), H223 (= H226), E361 (= E372), S364 (≠ G375), R412 (= R423)
- binding aspartyl-adenosine-5'-monophosphate: E170 (= E167), Q192 (= Q196), K195 (≠ A199), R214 (= R217), E216 (= E219), H223 (= H226), L224 (= L227), Y339 (= Y350), E361 (= E372), I362 (≠ L373), S363 (≠ V374), S364 (≠ G375), G365 (= G376), R368 (= R379), F406 (= F417), G407 (= G418), G409 (= G420), R412 (= R423)
3nelA Aspartyl-tRNA synthetase complexed with aspartic acid (see paper)
32% identity, 95% coverage: 16:442/449 of query aligns to 17:431/438 of 3nelA
- active site: R214 (= R217), E216 (= E219), R222 (= R225), H223 (= H226), E361 (= E372), S364 (≠ G375), R412 (= R423)
- binding aspartic acid: E170 (= E167), Q192 (= Q196), K195 (≠ A199), Y339 (= Y350), S364 (≠ G375), R368 (= R379), F406 (= F417), G407 (= G418)
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, 95% coverage: 16:442/449 of query aligns to 17:431/438 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 (≠ 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, 97% coverage: 10:445/449 of query aligns to 6:429/433 of 2xgtB
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E163 (= E167), S183 (= S194), Q185 (= Q196), R206 (= R217), E208 (= E219), H215 (= H226), L216 (= L227), Y219 (≠ F230), H221 (≠ M232), E223 (= E234), E356 (= E372), I357 (≠ L373), V358 (= V374), G359 (= G375), R363 (= R379), Y401 (≠ F417), G402 (= G418), G404 (= G420)
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: 10:445/449 of query aligns to 8:429/433 of 2xtiA
- binding 5'-O-[(R)-{[(2S)-2-amino-4-(hydroxyamino)-4-oxobutanoyl]oxy}(hydroxy)phosphoryl]adenosine: E163 (= E167), S183 (= S194), Q185 (= Q196), R206 (= R217), E208 (= E219), H215 (= H226), L216 (= L227), Y219 (≠ F230), H221 (≠ M232), E223 (= E234), Y333 (= Y350), E356 (= E372), I357 (≠ L373), V358 (= V374), G359 (= G375), R363 (= R379), Y401 (≠ F417), G402 (= G418), G404 (= G420), R407 (= R423)
- binding pyrophosphate 2-: R214 (= R225), H215 (= H226), E356 (= E372), R407 (= R423)
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: 10:445/449 of query aligns to 7:425/429 of 2xtiB
- binding adenosine-5'-triphosphate: R202 (= R217), E204 (= E219), R210 (= R225), H211 (= H226), L212 (= L227), Y215 (≠ F230), E352 (= E372), I353 (≠ L373), V354 (= V374), G400 (= G420), R403 (= R423)
8h53A Human asparaginyl-tRNA synthetase in complex with asparagine-amp (see paper)
30% identity, 95% coverage: 16:442/449 of query aligns to 15:420/427 of 8h53A
- binding imidodiphosphoric acid: R209 (= R225), H210 (= H226), E350 (= E372), R401 (= R423)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E158 (= E167), S178 (= S194), Q180 (= Q196), R201 (= R217), L211 (= L227), Y214 (≠ F230), H216 (≠ M232), E218 (= E234), E350 (= E372), I351 (≠ L373), V352 (= V374), R357 (= R379), Y395 (≠ F417), G396 (= G418), G398 (= G420), R401 (= R423)
8tc9A Human asparaginyl-tRNA synthetase bound to osm-s-106 (see paper)
30% identity, 95% coverage: 16:442/449 of query aligns to 17:427/434 of 8tc9A
- binding N~1~-[(3M)-3-(4-aminothieno[3,2-d]pyrimidin-6-yl)benzene-1-sulfonyl]-L-aspartamide: E165 (= E167), S185 (= S194), Q187 (= Q196), R208 (= R217), H217 (= H226), L218 (= L227), Y221 (≠ F230), H223 (≠ M232), E225 (= E234), R364 (= R379), Y402 (≠ F417), G403 (= G418), R408 (= R423)
8tc8A Human asparaginyl-tRNA synthetase bound to adenosine 5'-sulfamate (see paper)
30% identity, 95% coverage: 16:442/449 of query aligns to 17:428/435 of 8tc8A
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E166 (= E167), S186 (= S194), Q188 (= Q196), R209 (= R217), E211 (= E219), H218 (= H226), L219 (= L227), Y222 (≠ F230), H224 (≠ M232), E226 (= E234), E358 (= E372), I359 (≠ L373), V360 (= V374), R365 (= R379), Y403 (≠ F417), G404 (= G418), G406 (= G420)
3m4pA Entamoeba histolytica asparaginyl-tRNA synthetase (asnrs) in complex with asparaginyl-adenylate
29% identity, 96% coverage: 11:442/449 of query aligns to 11:428/435 of 3m4pA
- active site: R211 (= R217), E213 (= E219), R219 (= R225), H220 (= H226), E358 (= E372), G361 (= G375), R409 (= R423)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: S188 (= S194), Q190 (= Q196), R211 (= R217), H220 (= H226), L221 (= L227), Y224 (≠ F230), H226 (≠ M232), E358 (= E372), I359 (≠ L373), V360 (= V374), R365 (= R379), Y403 (≠ F417), G404 (= G418), G406 (= G420), R409 (= R423)
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)
31% identity, 95% coverage: 18:444/449 of query aligns to 19:431/436 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 (≠ 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)
29% identity, 99% coverage: 2:444/449 of query aligns to 26:485/490 of 1aszA
- active site: R258 (= R217), E260 (= E219), R266 (= R225), H267 (= H226), E411 (= E372), S414 (≠ G375), R464 (= R423)
- binding adenosine-5'-triphosphate: R258 (= R217), M268 (≠ L227), F271 (= F230), E411 (= E372), I412 (≠ L373), L413 (≠ V374), G459 (= G418), R464 (= R423)
- binding : R52 (= R27), Q53 (≠ R28), Q54 (≠ D29), T57 (≠ D32), L58 (≠ F33), F60 (= F35), Q71 (≠ N46), L73 (≠ Q48), E110 (≠ S80), I112 (≠ A82), K113 (= K83), E135 (= E103), P138 (= P106), L140 (≠ Q108), A154 (vs. gap), L156 (vs. gap), P157 (vs. gap), V158 (vs. gap), N160 (vs. gap), T163 (≠ F116), S213 (≠ C166), E214 (= E167), G215 (= G168), G216 (≠ A169), S217 (≠ G170), Q233 (≠ V193), F237 (≠ L197), E260 (= E219), N261 (= N220), S262 (= S221), N263 (= N222), H267 (= H226), S356 (≠ Q321), T357 (≠ S322), F388 (= F349)
Sites not aligning to the query:
1asyA Class ii aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA asp (see paper)
29% identity, 99% coverage: 2:444/449 of query aligns to 26:485/490 of 1asyA
- active site: R258 (= R217), E260 (= E219), R266 (= R225), H267 (= H226), E411 (= E372), S414 (≠ G375), R464 (= R423)
- binding : R52 (= R27), Q53 (≠ R28), Q54 (≠ D29), L58 (≠ F33), F60 (= F35), Q71 (≠ N46), L73 (≠ Q48), K88 (= K63), P111 (= P81), I112 (≠ A82), K113 (= K83), S114 (≠ G84), E135 (= E103), P138 (= P106), A154 (vs. gap), L156 (vs. gap), P157 (vs. gap), V158 (vs. gap), V159 (vs. gap), D162 (≠ E115), T163 (≠ F116), R258 (= R217), E260 (= E219), N261 (= N220), S262 (= S221), N263 (= N222), T264 (= T223), H267 (= H226), M268 (≠ L227), F271 (= F230), T357 (≠ S322), E411 (= E372), I412 (≠ L373), L413 (≠ V374), S414 (≠ G375), G459 (= G418), R464 (= R423)
Sites not aligning to the query:
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, 99% coverage: 2:444/449 of query aligns to 93:552/557 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)
29% identity, 96% coverage: 14:442/449 of query aligns to 17:428/435 of Q9RVH4
- H28 (≠ R25) 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
>WP_011188572.1 NCBI__GCF_000025945.1:WP_011188572.1
MRQRITELLVAKAEEQVVTVAGWIRTRRDTGDFSFLEVNDGSTLINMQVIADKSLGNYEE
EVKKLSTGCSVMVEGVLKESPAKGQSVEVHASSVTVVGWADPETYPLQKKRHSLEFLREI
SHLRPRTNAISAVARVRSRLSYAVHNFFQEKGFTQVHTPIITTSDCEGAGEMFQVAATGK
DGHFFGAPAGLTVSGQLQAEVYATALGDVYTFGPTFRAENSNTSRHLAEFWMIEPEMAFC
DLQGDMEVAEEMLKYVLADVLEHCVTDMNLFDKFISKGIIERLQSVLAHDFARVTYTEAV
DQLLASGQKFDFAVKWGIDLQSEHERYLTEQVYKRPLIVTDYPAAIKPFYMRMNEDGKTV
AAMDILVPGIGELVGGSQREERYDLLAERMEAAGLDLEEYGWYLDLRKYGTVPHAGFGLG
FERLVQFVTGMANIREVIPFPRTPGFAPC
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