SitesBLAST
Comparing WP_004044258.1 NCBI__GCF_000337315.1:WP_004044258.1 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)
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
52% identity, 97% coverage: 13:434/434 of query aligns to 16:438/438 of 3nemB
- active site: R214 (= R211), E216 (= E213), R222 (= R219), H223 (= H220), E361 (= E357), S364 (= S360), R412 (= R408)
- binding adenosine-5'-triphosphate: R214 (= R211), E216 (= E213), H223 (= H220), L224 (= L221), E361 (= E357), I362 (≠ L358), S363 (≠ V359), S364 (= S360), G407 (= G403), G409 (= G405), R412 (= R408)
- binding magnesium ion: E361 (= E357), S364 (= S360)
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
52% identity, 97% coverage: 13:434/434 of query aligns to 16:438/438 of 3nemA
- active site: R214 (= R211), E216 (= E213), R222 (= R219), H223 (= H220), E361 (= E357), S364 (= S360), R412 (= R408)
- binding aspartyl-adenosine-5'-monophosphate: E170 (= E167), Q192 (= Q189), K195 (= K192), R214 (= R211), E216 (= E213), H223 (= H220), L224 (= L221), Y339 (= Y335), E361 (= E357), I362 (≠ L358), S363 (≠ V359), S364 (= S360), G365 (= G361), R368 (= R364), F406 (= F402), G407 (= G403), G409 (= G405), R412 (= R408)
3nelA Aspartyl-tRNA synthetase complexed with aspartic acid (see paper)
52% identity, 97% coverage: 13:434/434 of query aligns to 16:438/438 of 3nelA
- active site: R214 (= R211), E216 (= E213), R222 (= R219), H223 (= H220), E361 (= E357), S364 (= S360), R412 (= R408)
- binding aspartic acid: E170 (= E167), Q192 (= Q189), K195 (= K192), Y339 (= Y335), S364 (= S360), R368 (= R364), F406 (= F402), G407 (= G403)
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)
52% identity, 97% coverage: 13:434/434 of query aligns to 16:438/438 of Q52428
- W26 (≠ H23) 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 (≠ P82) 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).
1b8aA Aspartyl-tRNA synthetase (see paper)
52% identity, 97% coverage: 13:434/434 of query aligns to 16:438/438 of 1b8aA
- binding adenosine-5'-triphosphate: R214 (= R211), E216 (= E213), H223 (= H220), L224 (= L221), E361 (= E357), I362 (≠ L358), S363 (≠ V359), S364 (= S360), G409 (= G405), R412 (= R408)
- binding manganese (ii) ion: E361 (= E357), S364 (= S360)
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)
45% identity, 100% coverage: 1:434/434 of query aligns to 1:436/436 of O07683
- H26 (= H23) mutation H->A,Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn).
- P84 (= P82) mutation P->A,K: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn).
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)
40% identity, 97% coverage: 13:434/434 of query aligns to 18:435/435 of Q9RVH4
- H28 (= H23) mutation to Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn).
- P77 (= P82) 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.
1x55A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate analogue (see paper)
34% identity, 100% coverage: 1:434/434 of query aligns to 1:434/434 of 1x55A
- active site: R211 (= R211), E213 (= E213), R219 (= R219), H220 (= H220), E357 (= E357), G360 (≠ S360), R408 (= R408)
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E168 (= E167), S188 (= S187), Q190 (= Q189), R211 (= R211), H220 (= H220), L221 (= L221), F224 (≠ A224), H226 (≠ S226), E228 (≠ D228), E357 (= E357), I358 (≠ L358), I359 (≠ V359), R364 (= R364), F402 (= F402), G403 (= G403), G405 (= G405), R408 (= R408)
1x54A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate (see paper)
34% identity, 100% coverage: 1:434/434 of query aligns to 1:434/434 of 1x54A
- active site: R211 (= R211), E213 (= E213), R219 (= R219), H220 (= H220), E357 (= E357), G360 (≠ S360), R408 (= R408)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E168 (= E167), S188 (= S187), Q190 (= Q189), R211 (= R211), H220 (= H220), L221 (= L221), F224 (≠ A224), H226 (≠ S226), E228 (≠ D228), E357 (= E357), I358 (≠ L358), I359 (≠ V359), R364 (= R364), F402 (= F402), G403 (= G403), G405 (= G405), R408 (= R408)
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)
36% identity, 97% coverage: 16:434/434 of query aligns to 109:557/557 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
1aszA The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction (see paper)
36% identity, 97% coverage: 16:434/434 of query aligns to 42:490/490 of 1aszA
- active site: R258 (= R211), E260 (= E213), R266 (= R219), H267 (= H220), E411 (= E357), S414 (= S360), R464 (= R408)
- binding adenosine-5'-triphosphate: R258 (= R211), M268 (≠ L221), F271 (≠ A224), E411 (= E357), I412 (≠ L358), L413 (≠ V359), G459 (= G403), R464 (= R408)
- binding : R52 (= R26), Q53 (≠ D27), Q54 (≠ L28), T57 (vs. gap), L58 (≠ I31), F60 (= F33), Q71 (= Q44), L73 (vs. gap), E110 (= E77), I112 (≠ P79), K113 (≠ R80), E135 (= E90), P138 (≠ D93), L140 (≠ I95), A154 (≠ S107), L156 (≠ K109), P157 (≠ V110), V158 (≠ D111), N160 (≠ E113), T163 (= T116), S213 (≠ T166), E214 (= E167), G215 (= G168), G216 (= G169), S217 (≠ T170), Q233 (= Q186), F237 (≠ L190), E260 (= E213), N261 (≠ E214), S262 (≠ H215), N263 (= N216), H267 (= H220), S356 (≠ P307), T357 (= T308), F388 (= F334), K486 (≠ Q430)
1asyA Class ii aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA asp (see paper)
36% identity, 97% coverage: 16:434/434 of query aligns to 42:490/490 of 1asyA
- active site: R258 (= R211), E260 (= E213), R266 (= R219), H267 (= H220), E411 (= E357), S414 (= S360), R464 (= R408)
- binding : R52 (= R26), Q53 (≠ D27), Q54 (≠ L28), L58 (≠ I31), F60 (= F33), Q71 (= Q44), L73 (vs. gap), K88 (≠ E58), P111 (≠ E78), I112 (≠ P79), K113 (≠ R80), S114 (≠ A81), E135 (= E90), P138 (≠ D93), A154 (≠ S107), L156 (≠ K109), P157 (≠ V110), V158 (≠ D111), V159 (≠ A112), D162 (≠ S115), T163 (= T116), R258 (= R211), E260 (= E213), N261 (≠ E214), S262 (≠ H215), N263 (= N216), T264 (= T217), H267 (= H220), M268 (≠ L221), F271 (≠ A224), T357 (= T308), E411 (= E357), I412 (≠ L358), L413 (≠ V359), S414 (= S360), G459 (= G403), R464 (= R408), K486 (≠ Q430)
O74407 Aspartate--tRNA ligase, cytoplasmic; Aspartyl-tRNA synthetase; AspRS; EC 6.1.1.12 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
33% identity, 99% coverage: 4:434/434 of query aligns to 90:580/580 of O74407
- S282 (≠ V162) modified: Phosphoserine
- S307 (= S187) modified: Phosphoserine
8tc8A Human asparaginyl-tRNA synthetase bound to adenosine 5'-sulfamate (see paper)
31% identity, 97% coverage: 13:434/434 of query aligns to 16:435/435 of 8tc8A
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E166 (= E167), S186 (= S187), Q188 (= Q189), R209 (= R211), E211 (= E213), H218 (= H220), L219 (= L221), Y222 (≠ A224), H224 (≠ S226), E226 (≠ D228), E358 (= E357), I359 (≠ L358), V360 (= V359), R365 (= R364), Y403 (≠ F402), G404 (= G403), G406 (= G405)
8h53A Human asparaginyl-tRNA synthetase in complex with asparagine-amp (see paper)
31% identity, 97% coverage: 13:434/434 of query aligns to 14:427/427 of 8h53A
- binding imidodiphosphoric acid: R209 (= R219), H210 (= H220), E350 (= E357), R401 (= R408)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E158 (= E167), S178 (= S187), Q180 (= Q189), R201 (= R211), L211 (= L221), Y214 (≠ A224), H216 (≠ S226), E218 (≠ D228), E350 (= E357), I351 (≠ L358), V352 (= V359), R357 (= R364), Y395 (≠ F402), G396 (= G403), G398 (= G405), R401 (= R408)
8tc9A Human asparaginyl-tRNA synthetase bound to osm-s-106 (see paper)
31% identity, 97% coverage: 13:434/434 of query aligns to 16:434/434 of 8tc9A
- binding N~1~-[(3M)-3-(4-aminothieno[3,2-d]pyrimidin-6-yl)benzene-1-sulfonyl]-L-aspartamide: E165 (= E167), S185 (= S187), Q187 (= Q189), R208 (= R211), H217 (= H220), L218 (= L221), Y221 (≠ A224), H223 (≠ S226), E225 (≠ D228), R364 (= R364), Y402 (≠ F402), G403 (= G403), R408 (= R408)
3kfuC Crystal structure of the transamidosome (see paper)
35% identity, 98% coverage: 1:427/434 of query aligns to 1:377/377 of 3kfuC
- active site: E307 (= E357), S310 (= S360), R358 (= R408)
- binding : W24 (≠ E24), R26 (= R26), L28 (= L28), R30 (≠ G30), F33 (= F33), Q44 (= Q44), N68 (≠ E78), K70 (≠ R80), E76 (= E86), P93 (= P103), E95 (≠ D105), R102 (≠ D111), N104 (≠ E113), T107 (= T116)
2xgtB Asparaginyl-tRNA synthetase from brugia malayi complexed with the sulphamoyl analogue of asparaginyl-adenylate (see paper)
31% identity, 97% coverage: 16:434/434 of query aligns to 14:433/433 of 2xgtB
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E163 (= E167), S183 (= S187), Q185 (= Q189), R206 (= R211), E208 (= E213), H215 (= H220), L216 (= L221), Y219 (≠ A224), H221 (≠ S226), E223 (≠ D228), E356 (= E357), I357 (≠ L358), V358 (= V359), G359 (≠ S360), R363 (= R364), Y401 (≠ F402), G402 (= G403), G404 (= G405)
3m4pA Entamoeba histolytica asparaginyl-tRNA synthetase (asnrs) in complex with asparaginyl-adenylate
30% identity, 97% coverage: 13:434/434 of query aligns to 15:435/435 of 3m4pA
- active site: R211 (= R211), E213 (= E213), R219 (= R219), H220 (= H220), E358 (= E357), G361 (≠ S360), R409 (= R408)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: S188 (= S187), Q190 (= Q189), R211 (= R211), H220 (= H220), L221 (= L221), Y224 (≠ A224), H226 (≠ S226), E358 (= E357), I359 (≠ L358), V360 (= V359), R365 (= R364), Y403 (≠ F402), G404 (= G403), G406 (= G405), R409 (= R408)
2xtiA Asparaginyl-tRNA synthetase from brugia malayi complexed with atp:mg and l-asp-beta-noh adenylate:ppi:mg (see paper)
31% identity, 97% coverage: 16:434/434 of query aligns to 16:433/433 of 2xtiA
- binding 5'-O-[(R)-{[(2S)-2-amino-4-(hydroxyamino)-4-oxobutanoyl]oxy}(hydroxy)phosphoryl]adenosine: E163 (= E167), S183 (= S187), Q185 (= Q189), R206 (= R211), E208 (= E213), H215 (= H220), L216 (= L221), Y219 (≠ A224), H221 (≠ S226), E223 (≠ D228), Y333 (= Y335), E356 (= E357), I357 (≠ L358), V358 (= V359), G359 (≠ S360), R363 (= R364), Y401 (≠ F402), G402 (= G403), G404 (= G405), R407 (= R408)
- binding pyrophosphate 2-: R214 (= R219), H215 (= H220), E356 (= E357), R407 (= R408)
Query Sequence
>WP_004044258.1 NCBI__GCF_000337315.1:WP_004044258.1
MRNRTYTADAEPGDTVTVAGWVHEVRDLGGIAFLILRDTSGKIQVKFEKDEMDDDLVETG
LGVHRESVISVTGEVDEEPRAPTGVEVTPESLDVIAEAEAQLPLDPSGKVDAELSTRLDN
RTLDLRKDEVKAIFEIRAEVQRAVRDKFRDLRATEINTPKIVATGTEGGTELFPITYFGQ
EAFMNQSPQLFKQLMVGSGLERVFEVGPIFRAEEHNTPRHLNEATSIDFESAFIDHTEAM
DVCEAVVTAAYEAVEENCQDELEALGLEEEFEAPSGEFPRLTYEEAIERINATGELDEQL
VWGDDLPTEGEKALGEDVGEHYFITDWPSEIKPFYIKDHDDDETLSTGFDMMHPNMELVS
GGQREHRFDHLVAGFEQQGLDPDAFEYYTKMFKYGMPPHAGFGLGGERLIMTMLGLENIR
EAVLFPRDRQRLSP
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