SitesBLAST
Comparing WP_013010070.1 NCBI__GCF_000025725.1:WP_013010070.1 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)
56% identity, 97% coverage: 15:453/453 of query aligns to 17:466/466 of P0A8M0
- Y426 (= Y413) 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, 97% coverage: 14:451/453 of query aligns to 12:432/434 of 1x55A
- active site: R211 (= R221), E213 (= E223), R219 (= R229), H220 (= H230), E357 (= E376), G360 (= G379), R408 (= R427)
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E168 (= E166), S188 (= S198), Q190 (= Q200), R211 (= R221), H220 (= H230), L221 (≠ A231), F224 (= F234), H226 (≠ M236), E228 (= E238), E357 (= E376), I358 (≠ L377), I359 (= I378), R364 (= R383), F402 (= F421), G403 (= G422), G405 (= G424), R408 (= R427)
1x54A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate (see paper)
34% identity, 97% coverage: 14:451/453 of query aligns to 12:432/434 of 1x54A
- active site: R211 (= R221), E213 (= E223), R219 (= R229), H220 (= H230), E357 (= E376), G360 (= G379), R408 (= R427)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E168 (= E166), S188 (= S198), Q190 (= Q200), R211 (= R221), H220 (= H230), L221 (≠ A231), F224 (= F234), H226 (≠ M236), E228 (= E238), E357 (= E376), I358 (≠ L377), I359 (= I378), R364 (= R383), F402 (= F421), G403 (= G422), G405 (= G424), R408 (= R427)
2xgtB Asparaginyl-tRNA synthetase from brugia malayi complexed with the sulphamoyl analogue of asparaginyl-adenylate (see paper)
31% identity, 98% coverage: 4:446/453 of query aligns to 2:426/433 of 2xgtB
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E163 (= E166), S183 (= S198), Q185 (= Q200), R206 (= R221), E208 (= E223), H215 (= H230), L216 (≠ A231), Y219 (≠ F234), H221 (≠ M236), E223 (= E238), E356 (= E376), I357 (≠ L377), V358 (≠ I378), G359 (= G379), R363 (= R383), Y401 (≠ F421), G402 (= G422), G404 (= G424)
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: 4:446/453 of query aligns to 4:426/433 of 2xtiA
- binding 5'-O-[(R)-{[(2S)-2-amino-4-(hydroxyamino)-4-oxobutanoyl]oxy}(hydroxy)phosphoryl]adenosine: E163 (= E166), S183 (= S198), Q185 (= Q200), R206 (= R221), E208 (= E223), H215 (= H230), L216 (≠ A231), Y219 (≠ F234), H221 (≠ M236), E223 (= E238), Y333 (= Y354), E356 (= E376), I357 (≠ L377), V358 (≠ I378), G359 (= G379), R363 (= R383), Y401 (≠ F421), G402 (= G422), G404 (= G424), R407 (= R427)
- binding pyrophosphate 2-: R214 (= R229), H215 (= H230), E356 (= E376), R407 (= R427)
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: 4:446/453 of query aligns to 3:422/429 of 2xtiB
- binding adenosine-5'-triphosphate: R202 (= R221), E204 (= E223), R210 (= R229), H211 (= H230), L212 (≠ A231), Y215 (≠ F234), E352 (= E376), I353 (≠ L377), V354 (≠ I378), G400 (= G424), R403 (= R427)
1b8aA Aspartyl-tRNA synthetase (see paper)
32% identity, 96% coverage: 18:451/453 of query aligns to 19:436/438 of 1b8aA
- binding adenosine-5'-triphosphate: R214 (= R221), E216 (= E223), H223 (= H230), L224 (≠ A231), E361 (= E376), I362 (≠ L377), S363 (≠ I378), S364 (≠ G379), G409 (= G424), R412 (= R427)
- binding manganese (ii) ion: E361 (= E376), S364 (≠ G379)
8tc8A Human asparaginyl-tRNA synthetase bound to adenosine 5'-sulfamate (see paper)
31% identity, 95% coverage: 18:446/453 of query aligns to 19:428/435 of 8tc8A
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E166 (= E166), S186 (= S198), Q188 (= Q200), R209 (= R221), E211 (= E223), H218 (= H230), L219 (≠ A231), Y222 (≠ F234), H224 (≠ M236), E226 (= E238), E358 (= E376), I359 (≠ L377), V360 (≠ I378), R365 (= R383), Y403 (≠ F421), G404 (= G422), G406 (= G424)
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
32% identity, 96% coverage: 18:451/453 of query aligns to 19:436/438 of 3nemB
- active site: R214 (= R221), E216 (= E223), R222 (= R229), H223 (= H230), E361 (= E376), S364 (≠ G379), R412 (= R427)
- binding adenosine-5'-triphosphate: R214 (= R221), E216 (= E223), H223 (= H230), L224 (≠ A231), E361 (= E376), I362 (≠ L377), S363 (≠ I378), S364 (≠ G379), G407 (= G422), G409 (= G424), R412 (= R427)
- binding magnesium ion: E361 (= E376), S364 (≠ G379)
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
32% identity, 96% coverage: 18:451/453 of query aligns to 19:436/438 of 3nemA
- active site: R214 (= R221), E216 (= E223), R222 (= R229), H223 (= H230), E361 (= E376), S364 (≠ G379), R412 (= R427)
- binding aspartyl-adenosine-5'-monophosphate: E170 (= E166), Q192 (= Q200), K195 (≠ A203), R214 (= R221), E216 (= E223), H223 (= H230), L224 (≠ A231), Y339 (= Y354), E361 (= E376), I362 (≠ L377), S363 (≠ I378), S364 (≠ G379), G365 (= G380), R368 (= R383), F406 (= F421), G407 (= G422), G409 (= G424), R412 (= R427)
3nelA Aspartyl-tRNA synthetase complexed with aspartic acid (see paper)
32% identity, 96% coverage: 18:451/453 of query aligns to 19:436/438 of 3nelA
- active site: R214 (= R221), E216 (= E223), R222 (= R229), H223 (= H230), E361 (= E376), S364 (≠ G379), R412 (= R427)
- binding aspartic acid: E170 (= E166), Q192 (= Q200), K195 (≠ A203), Y339 (= Y354), S364 (≠ G379), R368 (= R383), F406 (= F421), G407 (= G422)
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, 96% coverage: 18:451/453 of query aligns to 19:436/438 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 (≠ G83) 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 (see paper)
30% identity, 95% coverage: 18:446/453 of query aligns to 17:420/427 of 8h53A
- binding imidodiphosphoric acid: R209 (= R229), H210 (= H230), E350 (= E376), R401 (= R427)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E158 (= E166), S178 (= S198), Q180 (= Q200), R201 (= R221), L211 (≠ A231), Y214 (≠ F234), H216 (≠ M236), E218 (= E238), E350 (= E376), I351 (≠ L377), V352 (≠ I378), R357 (= R383), Y395 (≠ F421), G396 (= G422), G398 (= G424), R401 (= R427)
8tc9A Human asparaginyl-tRNA synthetase bound to osm-s-106 (see paper)
31% identity, 95% coverage: 18:446/453 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 (= E166), S185 (= S198), Q187 (= Q200), R208 (= R221), H217 (= H230), L218 (≠ A231), Y221 (≠ F234), H223 (≠ M236), E225 (= E238), R364 (= R383), Y402 (≠ F421), G403 (= G422), R408 (= R427)
3m4pA Entamoeba histolytica asparaginyl-tRNA synthetase (asnrs) in complex with asparaginyl-adenylate
28% identity, 95% coverage: 18:446/453 of query aligns to 18:428/435 of 3m4pA
- active site: R211 (= R221), E213 (= E223), R219 (= R229), H220 (= H230), E358 (= E376), G361 (= G379), R409 (= R427)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: S188 (= S198), Q190 (= Q200), R211 (= R221), H220 (= H230), L221 (≠ A231), Y224 (≠ F234), H226 (≠ M236), E358 (= E376), I359 (≠ L377), V360 (≠ I378), R365 (= R383), Y403 (≠ F421), G404 (= G422), G406 (= G424), R409 (= R427)
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: 2:452/453 of query aligns to 4:435/436 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 (≠ G83) 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)
32% identity, 74% coverage: 118:451/453 of query aligns to 235:555/557 of P04802
- P273 (= P158) 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)
27% identity, 98% coverage: 1:446/453 of query aligns to 1:428/435 of Q9RVH4
- H28 (≠ R25) mutation to Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn).
- P77 (≠ G83) 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.
1aszA The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction (see paper)
32% identity, 74% coverage: 118:451/453 of query aligns to 168:488/490 of 1aszA
- active site: R258 (= R221), E260 (= E223), R266 (= R229), H267 (= H230), E411 (= E376), S414 (≠ G379), R464 (= R427)
- binding adenosine-5'-triphosphate: R258 (= R221), M268 (≠ A231), F271 (= F234), E411 (= E376), I412 (≠ L377), L413 (≠ I378), G459 (= G422), R464 (= R427)
- binding : S213 (≠ C165), E214 (= E166), G215 (= G167), G216 (≠ A168), S217 (≠ G169), Q233 (≠ V197), F237 (≠ L201), E260 (= E223), N261 (= N224), S262 (= S225), N263 (= N226), H267 (= H230), S356 (≠ Q325), T357 (= T326), F388 (= F353), K486 (= K449)
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)
32% identity, 74% coverage: 118:451/453 of query aligns to 168:488/490 of 1asyA
- active site: R258 (= R221), E260 (= E223), R266 (= R229), H267 (= H230), E411 (= E376), S414 (≠ G379), R464 (= R427)
- binding : R258 (= R221), E260 (= E223), N261 (= N224), S262 (= S225), N263 (= N226), T264 (= T227), H267 (= H230), M268 (≠ A231), F271 (= F234), T357 (= T326), E411 (= E376), I412 (≠ L377), L413 (≠ I378), S414 (≠ G379), G459 (= G422), R464 (= R427), K486 (= K449)
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
>WP_013010070.1 NCBI__GCF_000025725.1:WP_013010070.1
MRNKIKDLLNAEHPESDITVHGWVRSKRDSKNFTFLELNDGSCLKNLQAIADEDIGTYDV
LKDINTGASVEIKGDLIESPGKGQKWELKAKAVALVGGADQETYPLQKKRHSDEFLRQIA
HLRPRTNKYGAIFRIRSEASFAVHQFFRERGFHYVHTPIITGSDCEGAGQMFRVTTLEDT
KKPVAEDFFGKAAYLTVSGQLDAESYACALGSVYTFGPTFRAENSNTPRHAAEFWMIEPE
MAFADIHDNMTLAEEFVKYLIWFLMENCKEDLELFFNFVDKELEAKLTNMLTNDFERVEY
REAVKILENSGEKFEYPVGFGVDLQTEHERYLTEKHFKKPVFVYNYPKSIKPFYMRQNDD
GETVAAMDLLVPSVGELIGGSQREERLDVLDSAIEKMGLSMEEYGWYAELRKYGTVPHAG
FGLGFERLLMFVTGVTNIRDVIPFARTPKNLEF
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