SitesBLAST
Comparing WP_013644957.1 NCBI__GCF_000191585.1:WP_013644957.1 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)
54% identity, 98% coverage: 10:439/439 of query aligns to 3:438/438 of 3nemB
- active site: R214 (= R221), E216 (= E223), R222 (= R229), H223 (= H230), E361 (= E362), S364 (= S365), R412 (= R413)
- binding adenosine-5'-triphosphate: R214 (= R221), E216 (= E223), H223 (= H230), L224 (= L231), E361 (= E362), I362 (= I363), S363 (= S364), S364 (= S365), G407 (= G408), G409 (= G410), R412 (= R413)
- binding magnesium ion: E361 (= E362), S364 (= S365)
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
54% identity, 98% coverage: 10:439/439 of query aligns to 3:438/438 of 3nemA
- active site: R214 (= R221), E216 (= E223), R222 (= R229), H223 (= H230), E361 (= E362), S364 (= S365), R412 (= R413)
- binding aspartyl-adenosine-5'-monophosphate: E170 (= E177), Q192 (= Q199), K195 (= K202), R214 (= R221), E216 (= E223), H223 (= H230), L224 (= L231), Y339 (= Y340), E361 (= E362), I362 (= I363), S363 (= S364), S364 (= S365), G365 (= G366), R368 (= R369), F406 (≠ W407), G407 (= G408), G409 (= G410), R412 (= R413)
3nelA Aspartyl-tRNA synthetase complexed with aspartic acid (see paper)
54% identity, 98% coverage: 10:439/439 of query aligns to 3:438/438 of 3nelA
- active site: R214 (= R221), E216 (= E223), R222 (= R229), H223 (= H230), E361 (= E362), S364 (= S365), R412 (= R413)
- binding aspartic acid: E170 (= E177), Q192 (= Q199), K195 (= K202), Y339 (= Y340), S364 (= S365), R368 (= R369), F406 (≠ W407), G407 (= G408)
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)
54% identity, 98% coverage: 10:439/439 of query aligns to 3:438/438 of Q52428
- W26 (≠ H33) 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 (≠ P92) 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)
53% identity, 98% coverage: 10:439/439 of query aligns to 3:438/438 of 1b8aA
- binding adenosine-5'-triphosphate: R214 (= R221), E216 (= E223), H223 (= H230), L224 (= L231), E361 (= E362), I362 (= I363), S363 (= S364), S364 (= S365), G409 (= G410), R412 (= R413)
- binding manganese (ii) ion: E361 (= E362), S364 (= S365)
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)
39% identity, 97% coverage: 13:439/439 of query aligns to 6:436/436 of O07683
- H26 (= H33) mutation H->A,Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn).
- P84 (= P92) 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)
36% identity, 96% coverage: 19:439/439 of query aligns to 14:435/435 of Q9RVH4
- H28 (= H33) mutation to Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn).
- P77 (= P92) 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, 97% coverage: 13:439/439 of query aligns to 6:434/434 of 1x55A
- active site: R211 (= R221), E213 (= E223), R219 (= R229), H220 (= H230), E357 (= E362), G360 (≠ S365), R408 (= R413)
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E168 (= E177), S188 (= S197), Q190 (= Q199), R211 (= R221), H220 (= H230), L221 (= L231), F224 (≠ V234), H226 (≠ S236), E228 (≠ D238), E357 (= E362), I358 (= I363), I359 (≠ S364), R364 (= R369), F402 (≠ W407), G403 (= G408), G405 (= G410), R408 (= R413)
1x54A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate (see paper)
34% identity, 97% coverage: 13:439/439 of query aligns to 6:434/434 of 1x54A
- active site: R211 (= R221), E213 (= E223), R219 (= R229), H220 (= H230), E357 (= E362), G360 (≠ S365), R408 (= R413)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E168 (= E177), S188 (= S197), Q190 (= Q199), R211 (= R221), H220 (= H230), L221 (= L231), F224 (≠ V234), H226 (≠ S236), E228 (≠ D238), E357 (= E362), I358 (= I363), I359 (≠ S364), R364 (= R369), F402 (≠ W407), G403 (= G408), G405 (= G410), R408 (= R413)
1aszA The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction (see paper)
34% identity, 95% coverage: 23:439/439 of query aligns to 39:490/490 of 1aszA
- active site: R258 (= R221), E260 (= E223), R266 (= R229), H267 (= H230), E411 (= E362), S414 (= S365), R464 (= R413)
- binding adenosine-5'-triphosphate: R258 (= R221), M268 (≠ L231), F271 (≠ V234), E411 (= E362), I412 (= I363), L413 (≠ S364), G459 (= G408), R464 (= R413)
- binding : R52 (= R36), Q53 (≠ D37), Q54 (≠ L38), T57 (≠ I41), L58 (≠ I42), F60 (= F43), Q71 (= Q54), L73 (≠ T56), E110 (= E87), I112 (≠ A89), K113 (= K90), E135 (≠ L110), P138 (= P113), L140 (≠ D115), A154 (vs. gap), L156 (vs. gap), P157 (vs. gap), V158 (vs. gap), N160 (vs. gap), T163 (= T126), S213 (≠ T176), E214 (= E177), G215 (= G178), G216 (= G179), S217 (≠ T180), Q233 (= Q196), F237 (≠ L200), E260 (= E223), N261 (≠ E224), S262 (≠ H225), N263 (≠ D226), H267 (= H230), S356 (= S312), T357 (≠ R313), F388 (= F339), K486 (≠ R435)
1asyA Class ii aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA asp (see paper)
34% identity, 95% coverage: 23:439/439 of query aligns to 39:490/490 of 1asyA
- active site: R258 (= R221), E260 (= E223), R266 (= R229), H267 (= H230), E411 (= E362), S414 (= S365), R464 (= R413)
- binding : R52 (= R36), Q53 (≠ D37), Q54 (≠ L38), L58 (≠ I42), F60 (= F43), Q71 (= Q54), L73 (≠ T56), K88 (≠ E68), P111 (≠ S88), I112 (≠ A89), K113 (= K90), S114 (≠ A91), E135 (≠ L110), P138 (= P113), A154 (vs. gap), L156 (vs. gap), P157 (vs. gap), V158 (vs. gap), V159 (vs. gap), D162 (= D125), T163 (= T126), R258 (= R221), E260 (= E223), N261 (≠ E224), S262 (≠ H225), N263 (≠ D226), T264 (= T227), H267 (= H230), M268 (≠ L231), F271 (≠ V234), T357 (≠ R313), E411 (= E362), I412 (= I363), L413 (≠ S364), S414 (= S365), G459 (= G408), R464 (= R413), K486 (≠ R435)
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)
34% identity, 95% coverage: 23:439/439 of query aligns to 106:557/557 of P04802
- P273 (= P169) mutation to G: Loss of activity; important for dimerization.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
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)
31% identity, 95% coverage: 24:439/439 of query aligns to 105:580/580 of O74407
- S282 (≠ V172) modified: Phosphoserine
- S307 (= S197) modified: Phosphoserine
3kfuC Crystal structure of the transamidosome (see paper)
34% identity, 93% coverage: 24:432/439 of query aligns to 14:377/377 of 3kfuC
- active site: E307 (= E362), S310 (= S365), R358 (= R413)
- binding : W24 (≠ E34), R26 (= R36), L28 (= L38), R30 (≠ G40), F33 (= F43), Q44 (= Q54), N68 (≠ S88), K70 (= K90), E76 (= E96), P93 (= P113), E95 (≠ D115), R102 (= R121), N104 (≠ E123), T107 (= T126)
2xtiA Asparaginyl-tRNA synthetase from brugia malayi complexed with atp:mg and l-asp-beta-noh adenylate:ppi:mg (see paper)
31% identity, 95% coverage: 22:439/439 of query aligns to 12:433/433 of 2xtiA
- binding 5'-O-[(R)-{[(2S)-2-amino-4-(hydroxyamino)-4-oxobutanoyl]oxy}(hydroxy)phosphoryl]adenosine: E163 (= E177), S183 (= S197), Q185 (= Q199), R206 (= R221), E208 (= E223), H215 (= H230), L216 (= L231), Y219 (≠ V234), H221 (≠ S236), E223 (≠ D238), Y333 (= Y340), E356 (= E362), I357 (= I363), V358 (≠ S364), G359 (≠ S365), R363 (= R369), Y401 (≠ W407), G402 (= G408), G404 (= G410), R407 (= R413)
- binding pyrophosphate 2-: R214 (= R229), H215 (= H230), E356 (= E362), R407 (= R413)
2xgtB Asparaginyl-tRNA synthetase from brugia malayi complexed with the sulphamoyl analogue of asparaginyl-adenylate (see paper)
31% identity, 95% coverage: 22:439/439 of query aligns to 10:433/433 of 2xgtB
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E163 (= E177), S183 (= S197), Q185 (= Q199), R206 (= R221), E208 (= E223), H215 (= H230), L216 (= L231), Y219 (≠ V234), H221 (≠ S236), E223 (≠ D238), E356 (= E362), I357 (= I363), V358 (≠ S364), G359 (≠ S365), R363 (= R369), Y401 (≠ W407), G402 (= G408), G404 (= G410)
8tc9A Human asparaginyl-tRNA synthetase bound to osm-s-106 (see paper)
30% identity, 95% coverage: 22:439/439 of query aligns to 15:434/434 of 8tc9A
- binding N~1~-[(3M)-3-(4-aminothieno[3,2-d]pyrimidin-6-yl)benzene-1-sulfonyl]-L-aspartamide: E165 (= E177), S185 (= S197), Q187 (= Q199), R208 (= R221), H217 (= H230), L218 (= L231), Y221 (≠ V234), H223 (≠ S236), E225 (≠ D238), R364 (= R369), Y402 (≠ W407), G403 (= G408), R408 (= R413)
8tc8A Human asparaginyl-tRNA synthetase bound to adenosine 5'-sulfamate (see paper)
30% identity, 95% coverage: 22:439/439 of query aligns to 15:435/435 of 8tc8A
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E166 (= E177), S186 (= S197), Q188 (= Q199), R209 (= R221), E211 (= E223), H218 (= H230), L219 (= L231), Y222 (≠ V234), H224 (≠ S236), E226 (≠ D238), E358 (= E362), I359 (= I363), V360 (≠ S364), R365 (= R369), Y403 (≠ W407), G404 (= G408), G406 (= G410)
8h53A Human asparaginyl-tRNA synthetase in complex with asparagine-amp (see paper)
30% identity, 95% coverage: 22:439/439 of query aligns to 13:427/427 of 8h53A
- binding imidodiphosphoric acid: R209 (= R229), H210 (= H230), E350 (= E362), R401 (= R413)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E158 (= E177), S178 (= S197), Q180 (= Q199), R201 (= R221), L211 (= L231), Y214 (≠ V234), H216 (≠ S236), E218 (≠ D238), E350 (= E362), I351 (= I363), V352 (≠ S364), R357 (= R369), Y395 (≠ W407), G396 (= G408), G398 (= G410), R401 (= R413)
3m4pA Entamoeba histolytica asparaginyl-tRNA synthetase (asnrs) in complex with asparaginyl-adenylate
30% identity, 94% coverage: 26:439/439 of query aligns to 18:435/435 of 3m4pA
- active site: R211 (= R221), E213 (= E223), R219 (= R229), H220 (= H230), E358 (= E362), G361 (≠ S365), R409 (= R413)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: S188 (= S197), Q190 (= Q199), R211 (= R221), H220 (= H230), L221 (= L231), Y224 (≠ V234), H226 (≠ S236), E358 (= E362), I359 (= I363), V360 (≠ S364), R365 (= R369), Y403 (≠ W407), G404 (= G408), G406 (= G410), R409 (= R413)
Query Sequence
>WP_013644957.1 NCBI__GCF_000191585.1:WP_013644957.1
MTDLLEDCRRTHYSKQIKPEMKDEDVVIMGWIHEMRDLGGIIFVLLRDRDGVTQVTAPSK
KIEPELFEELKKLKKESVIAVKGRVQESAKAPGGVEIIPETIKLLSESKLPLPLDTTEKV
RAEIDTRLDSRFIDLRKHSVSAIFKVKSRMLHSVRNFLESENYTEINTPKLVGSATEGGT
ELFPITYFEREAFLGQSPQLYKQMMMASGFDNVYEIAPIFRAEEHDTLRHLNEVISIDVE
TAFTDQIDAMNILEKMVVKAITDVKEHCKDALDTLEFDLQIPETPFPRIEYDEMVEMVNN
KGVKMEHGEDMSRAAEKVMGELMDGYYFITAWPTDIKPFYVQPSAEDPAKSCAFDLMYKD
LEISSGAMRIHNHDLLVEKIKSKGLNPDSFNRYLAAFEYGMPPHAGWGVGAERFTMTMTG
QTNIRETVLFPRDRRRLTP
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