SitesBLAST
Comparing WP_017751456.1 NCBI__GCF_000816635.1:WP_017751456.1 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, 96% coverage: 18:463/463 of query aligns to 17:466/466 of P0A8M0
- Y426 (= Y423) 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)
35% identity, 95% coverage: 19:459/463 of query aligns to 17:430/434 of 1x55A
- active site: R211 (= R231), E213 (= E233), R219 (= R239), H220 (= H240), E357 (= E386), G360 (= G389), R408 (= R437)
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E168 (= E168), S188 (= S208), Q190 (= Q210), R211 (= R231), H220 (= H240), L221 (≠ A241), F224 (= F244), H226 (≠ M246), E228 (= E248), E357 (= E386), I358 (= I387), I359 (≠ V388), R364 (= R393), F402 (= F431), G403 (= G432), G405 (= G434), R408 (= R437)
1x54A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate (see paper)
35% identity, 95% coverage: 19:459/463 of query aligns to 17:430/434 of 1x54A
- active site: R211 (= R231), E213 (= E233), R219 (= R239), H220 (= H240), E357 (= E386), G360 (= G389), R408 (= R437)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E168 (= E168), S188 (= S208), Q190 (= Q210), R211 (= R231), H220 (= H240), L221 (≠ A241), F224 (= F244), H226 (≠ M246), E228 (= E248), E357 (= E386), I358 (= I387), I359 (≠ V388), R364 (= R393), F402 (= F431), G403 (= G432), G405 (= G434), R408 (= R437)
1b8aA Aspartyl-tRNA synthetase (see paper)
33% identity, 96% coverage: 13:456/463 of query aligns to 11:431/438 of 1b8aA
- binding adenosine-5'-triphosphate: R214 (= R231), E216 (= E233), H223 (= H240), L224 (≠ A241), E361 (= E386), I362 (= I387), S363 (≠ V388), S364 (≠ G389), G409 (= G434), R412 (= R437)
- binding manganese (ii) ion: E361 (= E386), S364 (≠ G389)
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
33% identity, 96% coverage: 13:456/463 of query aligns to 11:431/438 of 3nemB
- active site: R214 (= R231), E216 (= E233), R222 (= R239), H223 (= H240), E361 (= E386), S364 (≠ G389), R412 (= R437)
- binding adenosine-5'-triphosphate: R214 (= R231), E216 (= E233), H223 (= H240), L224 (≠ A241), E361 (= E386), I362 (= I387), S363 (≠ V388), S364 (≠ G389), G407 (= G432), G409 (= G434), R412 (= R437)
- binding magnesium ion: E361 (= E386), S364 (≠ G389)
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
33% identity, 96% coverage: 13:456/463 of query aligns to 11:431/438 of 3nemA
- active site: R214 (= R231), E216 (= E233), R222 (= R239), H223 (= H240), E361 (= E386), S364 (≠ G389), R412 (= R437)
- binding aspartyl-adenosine-5'-monophosphate: E170 (= E168), Q192 (= Q210), K195 (≠ A213), R214 (= R231), E216 (= E233), H223 (= H240), L224 (≠ A241), Y339 (= Y364), E361 (= E386), I362 (= I387), S363 (≠ V388), S364 (≠ G389), G365 (= G390), R368 (= R393), F406 (= F431), G407 (= G432), G409 (= G434), R412 (= R437)
3nelA Aspartyl-tRNA synthetase complexed with aspartic acid (see paper)
33% identity, 96% coverage: 13:456/463 of query aligns to 11:431/438 of 3nelA
- active site: R214 (= R231), E216 (= E233), R222 (= R239), H223 (= H240), E361 (= E386), S364 (≠ G389), R412 (= R437)
- binding aspartic acid: E170 (= E168), Q192 (= Q210), K195 (≠ A213), Y339 (= Y364), S364 (≠ G389), R368 (= R393), F406 (= F431), G407 (= G432)
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)
33% identity, 96% coverage: 13:456/463 of query aligns to 11:431/438 of Q52428
- W26 (≠ R28) 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 (= K86) 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, 96% coverage: 14:456/463 of query aligns to 10:420/427 of 8h53A
- binding imidodiphosphoric acid: R209 (= R239), H210 (= H240), E350 (= E386), R401 (= R437)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E158 (= E168), S178 (= S208), Q180 (= Q210), R201 (= R231), L211 (≠ A241), Y214 (≠ F244), H216 (≠ M246), E218 (= E248), E350 (= E386), I351 (= I387), V352 (= V388), R357 (= R393), Y395 (≠ F431), G396 (= G432), G398 (= G434), R401 (= R437)
8tc9A Human asparaginyl-tRNA synthetase bound to osm-s-106 (see paper)
30% identity, 96% coverage: 14:456/463 of query aligns to 12:427/434 of 8tc9A
- binding N~1~-[(3M)-3-(4-aminothieno[3,2-d]pyrimidin-6-yl)benzene-1-sulfonyl]-L-aspartamide: E165 (= E168), S185 (= S208), Q187 (= Q210), R208 (= R231), H217 (= H240), L218 (≠ A241), Y221 (≠ F244), H223 (≠ M246), E225 (= E248), R364 (= R393), Y402 (≠ F431), G403 (= G432), R408 (= R437)
8tc8A Human asparaginyl-tRNA synthetase bound to adenosine 5'-sulfamate (see paper)
30% identity, 96% coverage: 14:456/463 of query aligns to 12:428/435 of 8tc8A
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E166 (= E168), S186 (= S208), Q188 (= Q210), R209 (= R231), E211 (= E233), H218 (= H240), L219 (≠ A241), Y222 (≠ F244), H224 (≠ M246), E226 (= E248), E358 (= E386), I359 (= I387), V360 (= V388), R365 (= R393), Y403 (≠ F431), G404 (= G432), G406 (= G434)
3m4pA Entamoeba histolytica asparaginyl-tRNA synthetase (asnrs) in complex with asparaginyl-adenylate
28% identity, 99% coverage: 3:462/463 of query aligns to 1:434/435 of 3m4pA
- active site: R211 (= R231), E213 (= E233), R219 (= R239), H220 (= H240), E358 (= E386), G361 (= G389), R409 (= R437)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: S188 (= S208), Q190 (= Q210), R211 (= R231), H220 (= H240), L221 (≠ A241), Y224 (≠ F244), H226 (≠ M246), E358 (= E386), I359 (= I387), V360 (= V388), R365 (= R393), Y403 (≠ F431), G404 (= G432), G406 (= G434), R409 (= R437)
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: 11:461/463 of query aligns to 6:431/433 of 2xtiA
- binding 5'-O-[(R)-{[(2S)-2-amino-4-(hydroxyamino)-4-oxobutanoyl]oxy}(hydroxy)phosphoryl]adenosine: E163 (= E168), S183 (= S208), Q185 (= Q210), R206 (= R231), E208 (= E233), H215 (= H240), L216 (≠ A241), Y219 (≠ F244), H221 (≠ M246), E223 (= E248), Y333 (= Y364), E356 (= E386), I357 (= I387), V358 (= V388), G359 (= G389), R363 (= R393), Y401 (≠ F431), G402 (= G432), G404 (= G434), R407 (= R437)
- binding pyrophosphate 2-: R214 (= R239), H215 (= H240), E356 (= E386), R407 (= R437)
2xgtB Asparaginyl-tRNA synthetase from brugia malayi complexed with the sulphamoyl analogue of asparaginyl-adenylate (see paper)
30% identity, 97% coverage: 11:461/463 of query aligns to 4:431/433 of 2xgtB
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E163 (= E168), S183 (= S208), Q185 (= Q210), R206 (= R231), E208 (= E233), H215 (= H240), L216 (≠ A241), Y219 (≠ F244), H221 (≠ M246), E223 (= E248), E356 (= E386), I357 (= I387), V358 (= V388), G359 (= G389), R363 (= R393), Y401 (≠ F431), G402 (= G432), G404 (= G434)
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: 11:461/463 of query aligns to 5:427/429 of 2xtiB
- binding adenosine-5'-triphosphate: R202 (= R231), E204 (= E233), R210 (= R239), H211 (= H240), L212 (≠ A241), Y215 (≠ F244), E352 (= E386), I353 (= I387), V354 (= V388), G400 (= G434), R403 (= R437)
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)
28% identity, 95% coverage: 19:456/463 of query aligns to 17:429/436 of O07683
- H26 (≠ R28) mutation H->A,Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn).
- P84 (≠ K86) 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, 71% coverage: 127:456/463 of query aligns to 173:483/490 of 1aszA
- active site: R258 (= R231), E260 (= E233), R266 (= R239), H267 (= H240), E411 (= E386), S414 (≠ G389), R464 (= R437)
- binding adenosine-5'-triphosphate: R258 (= R231), M268 (≠ A241), F271 (= F244), E411 (= E386), I412 (= I387), L413 (≠ V388), G459 (= G432), R464 (= R437)
- binding : S213 (≠ C167), E214 (= E168), G215 (= G169), G216 (≠ A170), S217 (≠ G171), Q233 (≠ V207), F237 (≠ L211), E260 (= E233), N261 (≠ D234), S262 (= S235), N263 (= N236), H267 (= H240), S356 (≠ Q335), T357 (= T336), F388 (= F363)
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, 486
1asyA Class ii aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA asp (see paper)
30% identity, 71% coverage: 127:456/463 of query aligns to 173:483/490 of 1asyA
- active site: R258 (= R231), E260 (= E233), R266 (= R239), H267 (= H240), E411 (= E386), S414 (≠ G389), R464 (= R437)
- binding : R258 (= R231), E260 (= E233), N261 (≠ D234), S262 (= S235), N263 (= N236), T264 (= T237), H267 (= H240), M268 (≠ A241), F271 (= F244), T357 (= T336), E411 (= E386), I412 (= I387), L413 (≠ V388), S414 (≠ G389), G459 (= G432), R464 (= R437)
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, 486
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, 71% coverage: 127:456/463 of query aligns to 240:550/557 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
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, 98% coverage: 1:456/463 of query aligns to 1:428/435 of Q9RVH4
- H28 (≠ R28) mutation to Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn).
- P77 (≠ K86) 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_017751456.1 NCBI__GCF_000816635.1:WP_017751456.1
METTLVKTIYRNTEKFSDKEVKVLGWIRTIRDSKNFGFIELNDGTFFKNIQIVFDNTIDN
FKEVAKLPISSSLAIEGKVVITPNAKQPFEIHAKNIFIEGMSSSDYPLQKKRHTLEYLRT
IAHLRGRSNTFSAVFRVRSVAAYAVHRFFQERGFVYAQTPLITGSDCEGAGEMFKVTTLD
LNNVPKTEDGKVDYSKDFFGKETNLTVSGQLSAETMALAFRNVYTFGPTFRAEDSNTARH
AAEFWMIEPEMAFADLNDYMDTAEELVKYIIKYVLENIPEEMQFFNSFIDKGLFDRLDNV
VNSKFGRITYTEAVDVLRKSGQKFEYPVEWGIDLQTEHERFLTEKVYGKPIFVTDYPKDI
KAFYMRANGDGKTVAAADLLVPGVGEIVGGSQREERYEVLENRIKELGLNKEDYWWYLEL
RKYGETKHSGFGLGFERILMYITGMSNIRDVIPFPRTTGSAEF
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