SitesBLAST
Comparing CA265_RS05115 FitnessBrowser__Pedo557:CA265_RS05115 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
54% identity, 99% coverage: 7:482/482 of query aligns to 6:466/466 of P0A8M0
- Y426 (≠ F442) 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)
31% identity, 95% coverage: 19:477/482 of query aligns to 18:429/434 of 1x55A
- active site: R211 (= R228), E213 (= E230), R219 (= R236), H220 (= H237), E357 (= E405), G360 (= G408), R408 (= R456)
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E168 (= E165), S188 (= S205), Q190 (= Q207), R211 (= R228), H220 (= H237), L221 (= L238), F224 (= F241), H226 (≠ M243), E228 (= E245), E357 (= E405), I358 (≠ M406), I359 (= I407), R364 (= R412), F402 (= F450), G403 (= G451), G405 (= G453), R408 (= R456)
1x54A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate (see paper)
31% identity, 95% coverage: 19:477/482 of query aligns to 18:429/434 of 1x54A
- active site: R211 (= R228), E213 (= E230), R219 (= R236), H220 (= H237), E357 (= E405), G360 (= G408), R408 (= R456)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E168 (= E165), S188 (= S205), Q190 (= Q207), R211 (= R228), H220 (= H237), L221 (= L238), F224 (= F241), H226 (≠ M243), E228 (= E245), E357 (= E405), I358 (≠ M406), I359 (= I407), R364 (= R412), F402 (= F450), G403 (= G451), G405 (= G453), R408 (= R456)
2xtiA Asparaginyl-tRNA synthetase from brugia malayi complexed with atp:mg and l-asp-beta-noh adenylate:ppi:mg (see paper)
27% identity, 98% coverage: 6:476/482 of query aligns to 4:427/433 of 2xtiA
- binding 5'-O-[(R)-{[(2S)-2-amino-4-(hydroxyamino)-4-oxobutanoyl]oxy}(hydroxy)phosphoryl]adenosine: E163 (= E165), S183 (= S205), Q185 (= Q207), R206 (= R228), E208 (= E230), H215 (= H237), L216 (= L238), Y219 (≠ F241), H221 (≠ M243), E223 (= E245), Y333 (= Y379), E356 (= E405), I357 (≠ M406), V358 (≠ I407), G359 (= G408), R363 (= R412), Y401 (≠ F450), G402 (= G451), G404 (= G453), R407 (= R456)
- binding pyrophosphate 2-: R214 (= R236), H215 (= H237), E356 (= E405), R407 (= R456)
2xgtB Asparaginyl-tRNA synthetase from brugia malayi complexed with the sulphamoyl analogue of asparaginyl-adenylate (see paper)
27% identity, 98% coverage: 6:476/482 of query aligns to 2:427/433 of 2xgtB
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E163 (= E165), S183 (= S205), Q185 (= Q207), R206 (= R228), E208 (= E230), H215 (= H237), L216 (= L238), Y219 (≠ F241), H221 (≠ M243), E223 (= E245), E356 (= E405), I357 (≠ M406), V358 (≠ I407), G359 (= G408), R363 (= R412), Y401 (≠ F450), G402 (= G451), G404 (= G453)
2xtiB Asparaginyl-tRNA synthetase from brugia malayi complexed with atp:mg and l-asp-beta-noh adenylate:ppi:mg (see paper)
27% identity, 98% coverage: 6:476/482 of query aligns to 3:423/429 of 2xtiB
- binding adenosine-5'-triphosphate: R202 (= R228), E204 (= E230), R210 (= R236), H211 (= H237), L212 (= L238), Y215 (≠ F241), E352 (= E405), I353 (≠ M406), V354 (≠ I407), G400 (= G453), R403 (= R456)
3m4pA Entamoeba histolytica asparaginyl-tRNA synthetase (asnrs) in complex with asparaginyl-adenylate
27% identity, 96% coverage: 20:481/482 of query aligns to 18:434/435 of 3m4pA
- active site: R211 (= R228), E213 (= E230), R219 (= R236), H220 (= H237), E358 (= E405), G361 (= G408), R409 (= R456)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: S188 (= S205), Q190 (= Q207), R211 (= R228), H220 (= H237), L221 (= L238), Y224 (≠ F241), H226 (≠ M243), E358 (= E405), I359 (≠ M406), V360 (≠ I407), R365 (= R412), Y403 (≠ F450), G404 (= G451), G406 (= G453), R409 (= R456)
1b8aA Aspartyl-tRNA synthetase (see paper)
29% identity, 95% coverage: 19:475/482 of query aligns to 18:431/438 of 1b8aA
- binding adenosine-5'-triphosphate: R214 (= R228), E216 (= E230), H223 (= H237), L224 (= L238), E361 (= E405), I362 (≠ M406), S363 (≠ I407), S364 (≠ G408), G409 (= G453), R412 (= R456)
- binding manganese (ii) ion: E361 (= E405), S364 (≠ G408)
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
28% identity, 95% coverage: 19:475/482 of query aligns to 18:431/438 of 3nemB
- active site: R214 (= R228), E216 (= E230), R222 (= R236), H223 (= H237), E361 (= E405), S364 (≠ G408), R412 (= R456)
- binding adenosine-5'-triphosphate: R214 (= R228), E216 (= E230), H223 (= H237), L224 (= L238), E361 (= E405), I362 (≠ M406), S363 (≠ I407), S364 (≠ G408), G407 (= G451), G409 (= G453), R412 (= R456)
- binding magnesium ion: E361 (= E405), S364 (≠ G408)
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
28% identity, 95% coverage: 19:475/482 of query aligns to 18:431/438 of 3nemA
- active site: R214 (= R228), E216 (= E230), R222 (= R236), H223 (= H237), E361 (= E405), S364 (≠ G408), R412 (= R456)
- binding aspartyl-adenosine-5'-monophosphate: E170 (= E165), Q192 (= Q207), K195 (≠ G210), R214 (= R228), E216 (= E230), H223 (= H237), L224 (= L238), Y339 (= Y379), E361 (= E405), I362 (≠ M406), S363 (≠ I407), S364 (≠ G408), G365 (= G409), R368 (= R412), F406 (= F450), G407 (= G451), G409 (= G453), R412 (= R456)
3nelA Aspartyl-tRNA synthetase complexed with aspartic acid (see paper)
28% identity, 95% coverage: 19:475/482 of query aligns to 18:431/438 of 3nelA
- active site: R214 (= R228), E216 (= E230), R222 (= R236), H223 (= H237), E361 (= E405), S364 (≠ G408), R412 (= R456)
- binding aspartic acid: E170 (= E165), Q192 (= Q207), K195 (≠ G210), Y339 (= Y379), S364 (≠ G408), R368 (= R412), F406 (= F450), G407 (= G451)
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)
28% identity, 95% coverage: 19:475/482 of query aligns to 18:431/438 of Q52428
- W26 (vs. gap) 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 (≠ G82) 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
26% identity, 95% coverage: 20:476/482 of query aligns to 17:421/427 of 8h53A
- binding imidodiphosphoric acid: R209 (= R236), H210 (= H237), E350 (= E405), R401 (= R456)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E158 (= E165), S178 (= S205), Q180 (= Q207), R201 (= R228), L211 (= L238), Y214 (≠ F241), H216 (≠ M243), E218 (= E245), E350 (= E405), I351 (≠ M406), V352 (≠ I407), R357 (= R412), Y395 (≠ F450), G396 (= G451), G398 (= G453), R401 (= R456)
8tc9A Human asparaginyl-tRNA synthetase bound to osm-s-106 (see paper)
26% identity, 95% coverage: 20:476/482 of query aligns to 19:428/434 of 8tc9A
- binding N~1~-[(3M)-3-(4-aminothieno[3,2-d]pyrimidin-6-yl)benzene-1-sulfonyl]-L-aspartamide: E165 (= E165), S185 (= S205), Q187 (= Q207), R208 (= R228), H217 (= H237), L218 (= L238), Y221 (≠ F241), H223 (≠ M243), E225 (= E245), R364 (= R412), Y402 (≠ F450), G403 (= G451), R408 (= R456)
8tc8A Human asparaginyl-tRNA synthetase bound to adenosine 5'-sulfamate (see paper)
26% identity, 95% coverage: 20:476/482 of query aligns to 19:429/435 of 8tc8A
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E166 (= E165), S186 (= S205), Q188 (= Q207), R209 (= R228), E211 (= E230), H218 (= H237), L219 (= L238), Y222 (≠ F241), H224 (≠ M243), E226 (= E245), E358 (= E405), I359 (≠ M406), V360 (≠ I407), R365 (= R412), Y403 (≠ F450), G404 (= G451), G406 (= G453)
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)
25% identity, 100% coverage: 1:481/482 of query aligns to 1:435/436 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 (≠ G82) 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)
27% identity, 74% coverage: 121:478/482 of query aligns to 243:576/580 of O74407
- S282 (≠ T160) modified: Phosphoserine
- S307 (= S205) modified: Phosphoserine
1aszA The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction (see paper)
27% identity, 74% coverage: 123:478/482 of query aligns to 172:486/490 of 1aszA
- active site: R258 (= R228), E260 (= E230), R266 (= R236), H267 (= H237), E411 (= E405), S414 (≠ G408), R464 (= R456)
- binding adenosine-5'-triphosphate: R258 (= R228), M268 (≠ L238), F271 (= F241), E411 (= E405), I412 (≠ M406), L413 (≠ I407), G459 (= G451), R464 (= R456)
- binding : S213 (≠ A164), E214 (= E165), G215 (= G166), G216 (≠ A167), S217 (≠ G168), Q233 (≠ V204), F237 (≠ L208), E260 (= E230), N261 (= N231), S262 (= S232), N263 (= N233), H267 (= H237), S356 (≠ Q350), T357 (≠ S351), F388 (= F378), K486 (= K478)
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
1asyA Class ii aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA asp (see paper)
27% identity, 74% coverage: 123:478/482 of query aligns to 172:486/490 of 1asyA
- active site: R258 (= R228), E260 (= E230), R266 (= R236), H267 (= H237), E411 (= E405), S414 (≠ G408), R464 (= R456)
- binding : R258 (= R228), E260 (= E230), N261 (= N231), S262 (= S232), N263 (= N233), T264 (= T234), H267 (= H237), M268 (≠ L238), F271 (= F241), T357 (≠ S351), E411 (= E405), I412 (≠ M406), L413 (≠ I407), S414 (≠ G408), G459 (= G451), R464 (= R456), K486 (= K478)
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
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)
27% identity, 74% coverage: 123:478/482 of query aligns to 239:553/557 of P04802
- P273 (= P157) 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
>CA265_RS05115 FitnessBrowser__Pedo557:CA265_RS05115
MIKRQQIKDLLKSTAFDTEVTVMGWVRTFRNNQFIALNDGSCMSNIQVVIDFNNLPDELL
KRITTGAAISATGKLIESLGKGQSVEIKATSVEILGDSDPEKFPLQPKKHSLEFLREIAH
LRFRTNTFNAVFKVRHALAFAIHQFYNERGFVYMHTPVITASDAEGAGEMFKVTTLDFDN
TPRSEDGKVDFSQDFFARATNLTVSGQLEGELAAMAFGQIYTFGPTFRAENSNTTRHLAE
FWMIEPEVAFADLEDNMQLAEDMMKYVIKYALDHCKDELEFLNTRLAEEDKQKPQNERSE
FSLLEKLDFCLANEFERLTYTEAIRILKSSKPNQKKQFKYLIDEWGADLQSEHERYLVEK
HFKKPVILTDYPADIKSFYMRQNEPDAEGRQTVAAMDILFPGIGEMIGGSQREERLDRLT
KRMEDLNIPQDELWWYLDTRRFGSAPHSGFGLGFERLVLFVTGMTNIRDVIAFPRFPKNA
EF
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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