SitesBLAST
Comparing WP_057507926.1 NCBI__GCF_001431535.1:WP_057507926.1 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)
68% identity, 100% coverage: 1:464/464 of query aligns to 1:466/466 of P0A8M0
- M1 (= M1) modified: Initiator methionine, Removed
- Y426 (= Y424) mutation to F: No effect.; mutation to S: 15-fold increase in Km for ATP.
1x55A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate analogue (see paper)
36% identity, 96% coverage: 16:460/464 of query aligns to 15:430/434 of 1x55A
- active site: R211 (= R232), E213 (= E234), R219 (= R240), H220 (= H241), E357 (= E387), G360 (= G390), R408 (= R438)
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E168 (= E169), S188 (= S209), Q190 (= Q211), R211 (= R232), H220 (= H241), L221 (= L242), F224 (= F245), H226 (≠ M247), E228 (= E249), E357 (= E387), I358 (= I388), I359 (= I389), R364 (= R394), F402 (= F432), G403 (= G433), G405 (= G435), R408 (= R438)
1x54A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate (see paper)
36% identity, 96% coverage: 16:460/464 of query aligns to 15:430/434 of 1x54A
- active site: R211 (= R232), E213 (= E234), R219 (= R240), H220 (= H241), E357 (= E387), G360 (= G390), R408 (= R438)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E168 (= E169), S188 (= S209), Q190 (= Q211), R211 (= R232), H220 (= H241), L221 (= L242), F224 (= F245), H226 (≠ M247), E228 (= E249), E357 (= E387), I358 (= I388), I359 (= I389), R364 (= R394), F402 (= F432), G403 (= G433), G405 (= G435), R408 (= R438)
3m4pA Entamoeba histolytica asparaginyl-tRNA synthetase (asnrs) in complex with asparaginyl-adenylate
30% identity, 95% coverage: 16:457/464 of query aligns to 14:428/435 of 3m4pA
- active site: R211 (= R232), E213 (= E234), R219 (= R240), H220 (= H241), E358 (= E387), G361 (= G390), R409 (= R438)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: S188 (= S209), Q190 (= Q211), R211 (= R232), H220 (= H241), L221 (= L242), Y224 (≠ F245), H226 (≠ M247), E358 (= E387), I359 (= I388), V360 (≠ I389), R365 (= R394), Y403 (≠ F432), G404 (= G433), G406 (= G435), R409 (= R438)
1b8aA Aspartyl-tRNA synthetase (see paper)
30% identity, 95% coverage: 17:457/464 of query aligns to 16:431/438 of 1b8aA
- binding adenosine-5'-triphosphate: R214 (= R232), E216 (= E234), H223 (= H241), L224 (= L242), E361 (= E387), I362 (= I388), S363 (≠ I389), S364 (≠ G390), G409 (= G435), R412 (= R438)
- binding manganese (ii) ion: E361 (= E387), S364 (≠ G390)
8tc9A Human asparaginyl-tRNA synthetase bound to osm-s-106 (see paper)
28% identity, 95% coverage: 17:457/464 of query aligns to 16:427/434 of 8tc9A
- binding N~1~-[(3M)-3-(4-aminothieno[3,2-d]pyrimidin-6-yl)benzene-1-sulfonyl]-L-aspartamide: E165 (= E169), S185 (= S209), Q187 (= Q211), R208 (= R232), H217 (= H241), L218 (= L242), Y221 (≠ F245), H223 (≠ M247), E225 (= E249), R364 (= R394), Y402 (≠ F432), G403 (= G433), R408 (= R438)
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
30% identity, 95% coverage: 17:457/464 of query aligns to 16:431/438 of 3nemB
- active site: R214 (= R232), E216 (= E234), R222 (= R240), H223 (= H241), E361 (= E387), S364 (≠ G390), R412 (= R438)
- binding adenosine-5'-triphosphate: R214 (= R232), E216 (= E234), H223 (= H241), L224 (= L242), E361 (= E387), I362 (= I388), S363 (≠ I389), S364 (≠ G390), G407 (= G433), G409 (= G435), R412 (= R438)
- binding magnesium ion: E361 (= E387), S364 (≠ G390)
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
30% identity, 95% coverage: 17:457/464 of query aligns to 16:431/438 of 3nemA
- active site: R214 (= R232), E216 (= E234), R222 (= R240), H223 (= H241), E361 (= E387), S364 (≠ G390), R412 (= R438)
- binding aspartyl-adenosine-5'-monophosphate: E170 (= E169), Q192 (= Q211), K195 (≠ V214), R214 (= R232), E216 (= E234), H223 (= H241), L224 (= L242), Y339 (= Y365), E361 (= E387), I362 (= I388), S363 (≠ I389), S364 (≠ G390), G365 (= G391), R368 (= R394), F406 (= F432), G407 (= G433), G409 (= G435), R412 (= R438)
3nelA Aspartyl-tRNA synthetase complexed with aspartic acid (see paper)
30% identity, 95% coverage: 17:457/464 of query aligns to 16:431/438 of 3nelA
- active site: R214 (= R232), E216 (= E234), R222 (= R240), H223 (= H241), E361 (= E387), S364 (≠ G390), R412 (= R438)
- binding aspartic acid: E170 (= E169), Q192 (= Q211), K195 (≠ V214), Y339 (= Y365), S364 (≠ G390), R368 (= R394), F406 (= F432), G407 (= G433)
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, 95% coverage: 17:457/464 of query aligns to 16:431/438 of Q52428
- W26 (≠ R27) 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 (≠ G85) 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).
2xtiA Asparaginyl-tRNA synthetase from brugia malayi complexed with atp:mg and l-asp-beta-noh adenylate:ppi:mg (see paper)
29% identity, 95% coverage: 20:462/464 of query aligns to 16:431/433 of 2xtiA
- binding 5'-O-[(R)-{[(2S)-2-amino-4-(hydroxyamino)-4-oxobutanoyl]oxy}(hydroxy)phosphoryl]adenosine: E163 (= E169), S183 (= S209), Q185 (= Q211), R206 (= R232), E208 (= E234), H215 (= H241), L216 (= L242), Y219 (≠ F245), H221 (≠ M247), E223 (= E249), Y333 (= Y365), E356 (= E387), I357 (= I388), V358 (≠ I389), G359 (= G390), R363 (= R394), Y401 (≠ F432), G402 (= G433), G404 (= G435), R407 (= R438)
- binding pyrophosphate 2-: R214 (= R240), H215 (= H241), E356 (= E387), R407 (= R438)
8h53A Human asparaginyl-tRNA synthetase in complex with asparagine-amp
28% identity, 95% coverage: 17:457/464 of query aligns to 14:420/427 of 8h53A
- binding imidodiphosphoric acid: R209 (= R240), H210 (= H241), E350 (= E387), R401 (= R438)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E158 (= E169), S178 (= S209), Q180 (= Q211), R201 (= R232), L211 (= L242), Y214 (≠ F245), H216 (≠ M247), E218 (= E249), E350 (= E387), I351 (= I388), V352 (≠ I389), R357 (= R394), Y395 (≠ F432), G396 (= G433), G398 (= G435), R401 (= R438)
2xgtB Asparaginyl-tRNA synthetase from brugia malayi complexed with the sulphamoyl analogue of asparaginyl-adenylate (see paper)
28% identity, 95% coverage: 20:462/464 of query aligns to 14:431/433 of 2xgtB
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E163 (= E169), S183 (= S209), Q185 (= Q211), R206 (= R232), E208 (= E234), H215 (= H241), L216 (= L242), Y219 (≠ F245), H221 (≠ M247), E223 (= E249), E356 (= E387), I357 (= I388), V358 (≠ I389), G359 (= G390), R363 (= R394), Y401 (≠ F432), G402 (= G433), G404 (= G435)
8tc8A Human asparaginyl-tRNA synthetase bound to adenosine 5'-sulfamate (see paper)
28% identity, 95% coverage: 17:457/464 of query aligns to 16:428/435 of 8tc8A
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E166 (= E169), S186 (= S209), Q188 (= Q211), R209 (= R232), E211 (= E234), H218 (= H241), L219 (= L242), Y222 (≠ F245), H224 (≠ M247), E226 (= E249), E358 (= E387), I359 (= I388), V360 (≠ I389), R365 (= R394), Y403 (≠ F432), G404 (= G433), G406 (= G435)
2xtiB Asparaginyl-tRNA synthetase from brugia malayi complexed with atp:mg and l-asp-beta-noh adenylate:ppi:mg (see paper)
29% identity, 95% coverage: 20:462/464 of query aligns to 15:427/429 of 2xtiB
- binding adenosine-5'-triphosphate: R202 (= R232), E204 (= E234), R210 (= R240), H211 (= H241), L212 (= L242), Y215 (≠ F245), E352 (= E387), I353 (= I388), V354 (≠ I389), G400 (= G435), R403 (= R438)
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)
30% identity, 96% coverage: 16:459/464 of query aligns to 15:431/436 of O07683
- H26 (≠ R27) mutation H->A,Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn).
- P84 (≠ G85) mutation P->A,K: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn).
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)
26% identity, 96% coverage: 16:459/464 of query aligns to 103:575/580 of O74407
- S282 (≠ T164) modified: Phosphoserine
- S307 (= S209) modified: Phosphoserine
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: 16:457/464 of query aligns to 17:428/435 of Q9RVH4
- H28 (≠ R27) mutation to Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn).
- P77 (≠ Q86) 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)
29% identity, 73% coverage: 122:459/464 of query aligns to 169:485/490 of 1aszA
- active site: R258 (= R232), E260 (= E234), R266 (= R240), H267 (= H241), E411 (= E387), S414 (≠ G390), R464 (= R438)
- binding adenosine-5'-triphosphate: R258 (= R232), M268 (≠ L242), F271 (= F245), E411 (= E387), I412 (= I388), L413 (≠ I389), G459 (= G433), R464 (= R438)
- binding : S213 (≠ A168), E214 (= E169), G215 (= G170), G216 (≠ A171), S217 (≠ G172), Q233 (≠ V208), F237 (≠ L212), E260 (= E234), N261 (= N235), S262 (= S236), N263 (= N237), H267 (= H241), S356 (≠ Q336), T357 (= T337), F388 (= F364)
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)
29% identity, 73% coverage: 122:459/464 of query aligns to 169:485/490 of 1asyA
- active site: R258 (= R232), E260 (= E234), R266 (= R240), H267 (= H241), E411 (= E387), S414 (≠ G390), R464 (= R438)
- binding : R258 (= R232), E260 (= E234), N261 (= N235), S262 (= S236), N263 (= N237), T264 (= T238), H267 (= H241), M268 (≠ L242), F271 (= F245), T357 (= T337), E411 (= E387), I412 (= I388), L413 (≠ I389), S414 (≠ G390), G459 (= G433), R464 (= R438)
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
Query Sequence
>WP_057507926.1 NCBI__GCF_001431535.1:WP_057507926.1
MTVVSVEHALAGKIPEGGEVTVRGWVRTVRGSANLAFINVTDGSCFAPIQVVAAESLANF
DAVKRLTSGCSLIAKGTLVKSQGKGQSFEIQASDVEVVGWVEDPLTYPIQPKPMSPEFLR
EVAHLRPRTNLFGAVTRIRNCLSQAVHRFFHQNGFNWISTPIITTSDAEGAGQMFRVSTL
DMVNLPRTERGEVDFSRDFFGKETFLTVSGQLNVEAYCLALSKVYTFGPTFRAENSNTTR
HLAEFWMIEPEIAFADLAEDARLAEEFLKYLFRAVLDERGDDLAFLAERVDKNAISKLEN
FINAPFEQIDYTEAVKLLQNSGRKFDFPVEWGLDLQTEHERWLTEEHIGRPVVVTNYPEH
IKAFYMRLNDDGKTVAAMDVLAPGIGEIIGGSQREERLDVLDARMAQFGLDREHYGWYRD
FRRYGSVPHAGFGLGFERLVVYVCGLSNIRDAIAYPRAPGNADF
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