SitesBLAST
Comparing WP_084058810.1 NCBI__GCF_900176285.1:WP_084058810.1 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)
57% identity, 96% coverage: 18:468/468 of query aligns to 16:466/466 of P0A8M0
- Y426 (≠ F428) 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, 95% coverage: 20:464/468 of query aligns to 17:430/434 of 1x55A
- active site: R211 (= R236), E213 (= E238), R219 (= R244), H220 (= H245), E357 (= E391), G360 (= G394), R408 (= R442)
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E168 (= E172), S188 (= S213), Q190 (= Q215), R211 (= R236), H220 (= H245), L221 (= L246), F224 (= F249), H226 (≠ M251), E228 (= E253), E357 (= E391), I358 (= I392), I359 (= I393), R364 (= R398), F402 (= F436), G403 (= G437), G405 (= G439), R408 (= R442)
1x54A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate (see paper)
34% identity, 95% coverage: 20:464/468 of query aligns to 17:430/434 of 1x54A
- active site: R211 (= R236), E213 (= E238), R219 (= R244), H220 (= H245), E357 (= E391), G360 (= G394), R408 (= R442)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E168 (= E172), S188 (= S213), Q190 (= Q215), R211 (= R236), H220 (= H245), L221 (= L246), F224 (= F249), H226 (≠ M251), E228 (= E253), E357 (= E391), I358 (= I392), I359 (= I393), R364 (= R398), F402 (= F436), G403 (= G437), G405 (= G439), R408 (= R442)
1b8aA Aspartyl-tRNA synthetase (see paper)
31% identity, 94% coverage: 20:461/468 of query aligns to 17:431/438 of 1b8aA
- binding adenosine-5'-triphosphate: R214 (= R236), E216 (= E238), H223 (= H245), L224 (= L246), E361 (= E391), I362 (= I392), S363 (≠ I393), S364 (≠ G394), G409 (= G439), R412 (= R442)
- binding manganese (ii) ion: E361 (= E391), S364 (≠ G394)
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
30% identity, 94% coverage: 20:461/468 of query aligns to 17:431/438 of 3nemB
- active site: R214 (= R236), E216 (= E238), R222 (= R244), H223 (= H245), E361 (= E391), S364 (≠ G394), R412 (= R442)
- binding adenosine-5'-triphosphate: R214 (= R236), E216 (= E238), H223 (= H245), L224 (= L246), E361 (= E391), I362 (= I392), S363 (≠ I393), S364 (≠ G394), G407 (= G437), G409 (= G439), R412 (= R442)
- binding magnesium ion: E361 (= E391), S364 (≠ G394)
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
30% identity, 94% coverage: 20:461/468 of query aligns to 17:431/438 of 3nemA
- active site: R214 (= R236), E216 (= E238), R222 (= R244), H223 (= H245), E361 (= E391), S364 (≠ G394), R412 (= R442)
- binding aspartyl-adenosine-5'-monophosphate: E170 (= E172), Q192 (= Q215), K195 (≠ A218), R214 (= R236), E216 (= E238), H223 (= H245), L224 (= L246), Y339 (= Y369), E361 (= E391), I362 (= I392), S363 (≠ I393), S364 (≠ G394), G365 (= G395), R368 (= R398), F406 (= F436), G407 (= G437), G409 (= G439), R412 (= R442)
3nelA Aspartyl-tRNA synthetase complexed with aspartic acid (see paper)
30% identity, 94% coverage: 20:461/468 of query aligns to 17:431/438 of 3nelA
- active site: R214 (= R236), E216 (= E238), R222 (= R244), H223 (= H245), E361 (= E391), S364 (≠ G394), R412 (= R442)
- binding aspartic acid: E170 (= E172), Q192 (= Q215), K195 (≠ A218), Y339 (= Y369), S364 (≠ G394), R368 (= R398), F406 (= F436), G407 (= G437)
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, 94% coverage: 20:461/468 of query aligns to 17:431/438 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 (≠ G89) 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
28% identity, 96% coverage: 14:461/468 of query aligns to 9:428/435 of 3m4pA
- active site: R211 (= R236), E213 (= E238), R219 (= R244), H220 (= H245), E358 (= E391), G361 (= G394), R409 (= R442)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: S188 (= S213), Q190 (= Q215), R211 (= R236), H220 (= H245), L221 (= L246), Y224 (≠ F249), H226 (≠ M251), E358 (= E391), I359 (= I392), V360 (≠ I393), R365 (= R398), Y403 (≠ F436), G404 (= G437), G406 (= G439), R409 (= R442)
2xgtB Asparaginyl-tRNA synthetase from brugia malayi complexed with the sulphamoyl analogue of asparaginyl-adenylate (see paper)
29% identity, 96% coverage: 17:466/468 of query aligns to 9:431/433 of 2xgtB
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E163 (= E172), S183 (= S213), Q185 (= Q215), R206 (= R236), E208 (= E238), H215 (= H245), L216 (= L246), Y219 (≠ F249), H221 (≠ M251), E223 (= E253), E356 (= E391), I357 (= I392), V358 (≠ I393), G359 (= G394), R363 (= R398), Y401 (≠ F436), G402 (= G437), G404 (= G439)
2xtiA Asparaginyl-tRNA synthetase from brugia malayi complexed with atp:mg and l-asp-beta-noh adenylate:ppi:mg (see paper)
28% identity, 96% coverage: 17:466/468 of query aligns to 11:431/433 of 2xtiA
- binding 5'-O-[(R)-{[(2S)-2-amino-4-(hydroxyamino)-4-oxobutanoyl]oxy}(hydroxy)phosphoryl]adenosine: E163 (= E172), S183 (= S213), Q185 (= Q215), R206 (= R236), E208 (= E238), H215 (= H245), L216 (= L246), Y219 (≠ F249), H221 (≠ M251), E223 (= E253), Y333 (= Y369), E356 (= E391), I357 (= I392), V358 (≠ I393), G359 (= G394), R363 (= R398), Y401 (≠ F436), G402 (= G437), G404 (= G439), R407 (= R442)
- binding pyrophosphate 2-: R214 (= R244), H215 (= H245), E356 (= E391), R407 (= R442)
2xtiB Asparaginyl-tRNA synthetase from brugia malayi complexed with atp:mg and l-asp-beta-noh adenylate:ppi:mg (see paper)
29% identity, 96% coverage: 17:466/468 of query aligns to 10:427/429 of 2xtiB
- binding adenosine-5'-triphosphate: R202 (= R236), E204 (= E238), R210 (= R244), H211 (= H245), L212 (= L246), Y215 (≠ F249), E352 (= E391), I353 (= I392), V354 (≠ I393), G400 (= G439), R403 (= R442)
8h53A Human asparaginyl-tRNA synthetase in complex with asparagine-amp
28% identity, 94% coverage: 20:461/468 of query aligns to 15:420/427 of 8h53A
- binding imidodiphosphoric acid: R209 (= R244), H210 (= H245), E350 (= E391), R401 (= R442)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E158 (= E172), S178 (= S213), Q180 (= Q215), R201 (= R236), L211 (= L246), Y214 (≠ F249), H216 (≠ M251), E218 (= E253), E350 (= E391), I351 (= I392), V352 (≠ I393), R357 (= R398), Y395 (≠ F436), G396 (= G437), G398 (= G439), R401 (= R442)
8tc9A Human asparaginyl-tRNA synthetase bound to osm-s-106 (see paper)
27% identity, 94% coverage: 20:461/468 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 (= E172), S185 (= S213), Q187 (= Q215), R208 (= R236), H217 (= H245), L218 (= L246), Y221 (≠ F249), H223 (≠ M251), E225 (= E253), R364 (= R398), Y402 (≠ F436), G403 (= G437), R408 (= R442)
8tc8A Human asparaginyl-tRNA synthetase bound to adenosine 5'-sulfamate (see paper)
27% identity, 94% coverage: 20:461/468 of query aligns to 17:428/435 of 8tc8A
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E166 (= E172), S186 (= S213), Q188 (= Q215), R209 (= R236), E211 (= E238), H218 (= H245), L219 (= L246), Y222 (≠ F249), H224 (≠ M251), E226 (= E253), E358 (= E391), I359 (= I392), V360 (≠ I393), R365 (= R398), Y403 (≠ F436), G404 (= G437), G406 (= G439)
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: 20:463/468 of query aligns to 17:431/436 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 (≠ G89) 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)
27% identity, 98% coverage: 6:463/468 of query aligns to 26:485/490 of 1aszA
- active site: R258 (= R236), E260 (= E238), R266 (= R244), H267 (= H245), E411 (= E391), S414 (≠ G394), R464 (= R442)
- binding adenosine-5'-triphosphate: R258 (= R236), M268 (≠ L246), F271 (= F249), E411 (= E391), I412 (= I392), L413 (≠ I393), G459 (= G437), R464 (= R442)
- binding : R52 (= R32), Q53 (≠ D33), Q54 (≠ S34), T57 (≠ G37), L58 (≠ I38), F60 (= F40), Q71 (≠ N51), L73 (≠ Q53), E110 (≠ S85), I112 (≠ G87), K113 (= K88), E135 (vs. gap), P138 (vs. gap), L140 (vs. gap), A154 (= A108), L156 (≠ Y110), P157 (= P111), V158 (≠ L112), N160 (≠ K114), T163 (≠ H117), S213 (≠ C171), E214 (= E172), G215 (= G173), G216 (≠ A174), S217 (≠ G175), Q233 (≠ V212), F237 (≠ L216), E260 (= E238), N261 (= N239), S262 (= S240), N263 (= N241), H267 (= H245), S356 (≠ Q340), T357 (≠ S341), F388 (= F368)
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)
27% identity, 98% coverage: 6:463/468 of query aligns to 26:485/490 of 1asyA
- active site: R258 (= R236), E260 (= E238), R266 (= R244), H267 (= H245), E411 (= E391), S414 (≠ G394), R464 (= R442)
- binding : R52 (= R32), Q53 (≠ D33), Q54 (≠ S34), L58 (≠ I38), F60 (= F40), Q71 (≠ N51), L73 (≠ Q53), K88 (≠ E68), P111 (= P86), I112 (≠ G87), K113 (= K88), S114 (≠ G89), E135 (vs. gap), P138 (vs. gap), A154 (= A108), L156 (≠ Y110), P157 (= P111), V158 (≠ L112), V159 (≠ Q113), D162 (≠ R116), T163 (≠ H117), R258 (= R236), E260 (= E238), N261 (= N239), S262 (= S240), N263 (= N241), T264 (= T242), H267 (= H245), M268 (≠ L246), F271 (= F249), T357 (≠ S341), E411 (= E391), I412 (= I392), L413 (≠ I393), S414 (≠ G394), G459 (= G437), R464 (= R442)
Sites not aligning to the query:
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: 17:461/468 of query aligns to 16:428/435 of Q9RVH4
- H28 (≠ R29) mutation to Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn).
- P77 (≠ G89) 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.
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: 131:463/468 of query aligns to 240:552/557 of P04802
- P273 (= P164) mutation to G: Loss of activity; important for dimerization.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
Query Sequence
>WP_084058810.1 NCBI__GCF_900176285.1:WP_084058810.1
MEKAIRIDQIFKNETAHLEKEVTIQGWVRTRRDSKAGISFIEVNDGSCLRNLQVIADRSR
PELESVVERLATGCAVQVQGVVQASPGKGQSIEVHAERIDLFGWADPAVYPLQKKRHSFE
FLRTIGHLRPRTNTLGAVARIRNRLSFAVHQFFQKEGFFYVHTPIITSSDCEGAGEVFRV
TTLDPAAPPAPGNPDGNVYSQDFFEKPAYLTVSGQLQAEIYALALGKVYTFGPTFRAENS
NTSRHLAEFWMIEPEMAFYDLQDNLELAQSFIKYVISAVLDDCQEDLNLFARFVEPTLME
TLETLVRETFQVITYTEAVEILKKSGESFDYPVEWGTDLQSEHERYLTEKKFRKPVAIID
FPRAIKPFYMRVNDDEKTVAAVDVLVPRVGEIIGGSQREERLDVLLKQMEIKAVPAEEYQ
WYVDLRRFGSAPHSGFGLGLERLVQFTTGLGNIREVIPFPRTPGHADF
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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