SitesBLAST
Comparing 201369 FitnessBrowser__MR1:201369 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)
81% identity, 100% coverage: 1:466/466 of query aligns to 1:466/466 of P0A8M0
- M1 (= M1) modified: Initiator methionine, Removed
- Y426 (= Y426) 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, 95% coverage: 17:461/466 of query aligns to 16:429/434 of 1x55A
- active site: R211 (= R234), E213 (= E236), R219 (= R242), H220 (= H243), E357 (= E389), G360 (= G392), R408 (= R440)
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E168 (= E171), S188 (= S211), Q190 (= Q213), R211 (= R234), H220 (= H243), L221 (= L244), F224 (= F247), H226 (≠ M249), E228 (= E251), E357 (= E389), I358 (= I390), I359 (= I391), R364 (= R396), F402 (= F434), G403 (= G435), G405 (= G437), R408 (= R440)
1x54A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate (see paper)
36% identity, 95% coverage: 17:461/466 of query aligns to 16:429/434 of 1x54A
- active site: R211 (= R234), E213 (= E236), R219 (= R242), H220 (= H243), E357 (= E389), G360 (= G392), R408 (= R440)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E168 (= E171), S188 (= S211), Q190 (= Q213), R211 (= R234), H220 (= H243), L221 (= L244), F224 (= F247), H226 (≠ M249), E228 (= E251), E357 (= E389), I358 (= I390), I359 (= I391), R364 (= R396), F402 (= F434), G403 (= G435), G405 (= G437), R408 (= R440)
2xgtB Asparaginyl-tRNA synthetase from brugia malayi complexed with the sulphamoyl analogue of asparaginyl-adenylate (see paper)
29% identity, 94% coverage: 20:459/466 of query aligns to 14:426/433 of 2xgtB
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E163 (= E171), S183 (= S211), Q185 (= Q213), R206 (= R234), E208 (= E236), H215 (= H243), L216 (= L244), Y219 (≠ F247), H221 (≠ M249), E223 (= E251), E356 (= E389), I357 (= I390), V358 (≠ I391), G359 (= G392), R363 (= R396), Y401 (≠ F434), G402 (= G435), G404 (= G437)
2xtiA Asparaginyl-tRNA synthetase from brugia malayi complexed with atp:mg and l-asp-beta-noh adenylate:ppi:mg (see paper)
29% identity, 94% coverage: 20:459/466 of query aligns to 16:426/433 of 2xtiA
- binding 5'-O-[(R)-{[(2S)-2-amino-4-(hydroxyamino)-4-oxobutanoyl]oxy}(hydroxy)phosphoryl]adenosine: E163 (= E171), S183 (= S211), Q185 (= Q213), R206 (= R234), E208 (= E236), H215 (= H243), L216 (= L244), Y219 (≠ F247), H221 (≠ M249), E223 (= E251), Y333 (= Y367), E356 (= E389), I357 (= I390), V358 (≠ I391), G359 (= G392), R363 (= R396), Y401 (≠ F434), G402 (= G435), G404 (= G437), R407 (= R440)
- binding pyrophosphate 2-: R214 (= R242), H215 (= H243), E356 (= E389), R407 (= R440)
2xtiB Asparaginyl-tRNA synthetase from brugia malayi complexed with atp:mg and l-asp-beta-noh adenylate:ppi:mg (see paper)
29% identity, 94% coverage: 20:459/466 of query aligns to 15:422/429 of 2xtiB
- binding adenosine-5'-triphosphate: R202 (= R234), E204 (= E236), R210 (= R242), H211 (= H243), L212 (= L244), Y215 (≠ F247), E352 (= E389), I353 (= I390), V354 (≠ I391), G400 (= G437), R403 (= R440)
1b8aA Aspartyl-tRNA synthetase (see paper)
31% identity, 97% coverage: 13:462/466 of query aligns to 12:434/438 of 1b8aA
- binding adenosine-5'-triphosphate: R214 (= R234), E216 (= E236), H223 (= H243), L224 (= L244), E361 (= E389), I362 (= I390), S363 (≠ I391), S364 (≠ G392), G409 (= G437), R412 (= R440)
- binding manganese (ii) ion: E361 (= E389), S364 (≠ G392)
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
31% identity, 97% coverage: 13:462/466 of query aligns to 12:434/438 of 3nemB
- active site: R214 (= R234), E216 (= E236), R222 (= R242), H223 (= H243), E361 (= E389), S364 (≠ G392), R412 (= R440)
- binding adenosine-5'-triphosphate: R214 (= R234), E216 (= E236), H223 (= H243), L224 (= L244), E361 (= E389), I362 (= I390), S363 (≠ I391), S364 (≠ G392), G407 (= G435), G409 (= G437), R412 (= R440)
- binding magnesium ion: E361 (= E389), S364 (≠ G392)
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
31% identity, 97% coverage: 13:462/466 of query aligns to 12:434/438 of 3nemA
- active site: R214 (= R234), E216 (= E236), R222 (= R242), H223 (= H243), E361 (= E389), S364 (≠ G392), R412 (= R440)
- binding aspartyl-adenosine-5'-monophosphate: E170 (= E171), Q192 (= Q213), K195 (≠ G216), R214 (= R234), E216 (= E236), H223 (= H243), L224 (= L244), Y339 (= Y367), E361 (= E389), I362 (= I390), S363 (≠ I391), S364 (≠ G392), G365 (= G393), R368 (= R396), F406 (= F434), G407 (= G435), G409 (= G437), R412 (= R440)
3nelA Aspartyl-tRNA synthetase complexed with aspartic acid (see paper)
31% identity, 97% coverage: 13:462/466 of query aligns to 12:434/438 of 3nelA
- active site: R214 (= R234), E216 (= E236), R222 (= R242), H223 (= H243), E361 (= E389), S364 (≠ G392), R412 (= R440)
- binding aspartic acid: E170 (= E171), Q192 (= Q213), K195 (≠ G216), Y339 (= Y367), S364 (≠ G392), R368 (= R396), F406 (= F434), G407 (= G435)
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)
31% identity, 97% coverage: 13:462/466 of query aligns to 12:434/438 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 (≠ G87) 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
29% identity, 95% coverage: 17:459/466 of query aligns to 14:420/427 of 8h53A
- binding imidodiphosphoric acid: R209 (= R242), H210 (= H243), E350 (= E389), R401 (= R440)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E158 (= E171), S178 (= S211), Q180 (= Q213), R201 (= R234), L211 (= L244), Y214 (≠ F247), H216 (≠ M249), E218 (= E251), E350 (= E389), I351 (= I390), V352 (≠ I391), R357 (= R396), Y395 (≠ F434), G396 (= G435), G398 (= G437), R401 (= R440)
3m4pA Entamoeba histolytica asparaginyl-tRNA synthetase (asnrs) in complex with asparaginyl-adenylate
28% identity, 95% coverage: 17:459/466 of query aligns to 15:428/435 of 3m4pA
- active site: R211 (= R234), E213 (= E236), R219 (= R242), H220 (= H243), E358 (= E389), G361 (= G392), R409 (= R440)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: S188 (= S211), Q190 (= Q213), R211 (= R234), H220 (= H243), L221 (= L244), Y224 (≠ F247), H226 (≠ M249), E358 (= E389), I359 (= I390), V360 (≠ I391), R365 (= R396), Y403 (≠ F434), G404 (= G435), G406 (= G437), R409 (= R440)
8tc9A Human asparaginyl-tRNA synthetase bound to osm-s-106 (see paper)
29% identity, 95% coverage: 17:459/466 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 (= E171), S185 (= S211), Q187 (= Q213), R208 (= R234), H217 (= H243), L218 (= L244), Y221 (≠ F247), H223 (≠ M249), E225 (= E251), R364 (= R396), Y402 (≠ F434), G403 (= G435), R408 (= R440)
8tc8A Human asparaginyl-tRNA synthetase bound to adenosine 5'-sulfamate (see paper)
29% identity, 95% coverage: 17:459/466 of query aligns to 16:428/435 of 8tc8A
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E166 (= E171), S186 (= S211), Q188 (= Q213), R209 (= R234), E211 (= E236), H218 (= H243), L219 (= L244), Y222 (≠ F247), H224 (≠ M249), E226 (= E251), E358 (= E389), I359 (= I390), V360 (≠ I391), R365 (= R396), Y403 (≠ F434), G404 (= G435), G406 (= G437)
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)
27% identity, 95% coverage: 17:461/466 of query aligns to 16:431/436 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 (≠ G87) 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)
27% identity, 95% coverage: 17:459/466 of query aligns to 18:428/435 of Q9RVH4
- H28 (≠ R27) mutation to Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn).
- P77 (≠ G87) 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)
25% identity, 95% coverage: 20:462/466 of query aligns to 42:486/490 of 1aszA
- active site: R258 (= R234), E260 (= E236), R266 (= R242), H267 (= H243), E411 (= E389), S414 (≠ G392), R464 (= R440)
- binding adenosine-5'-triphosphate: R258 (= R234), M268 (≠ L244), F271 (= F247), E411 (= E389), I412 (= I390), L413 (≠ I391), G459 (= G435), R464 (= R440)
- binding : R52 (= R30), Q53 (≠ D31), Q54 (≠ S32), T57 (≠ G35), L58 (≠ I36), F60 (= F38), Q71 (= Q51), L73 (≠ V53), E110 (= E82), I112 (≠ P84), K113 (≠ G85), E135 (≠ D107), P138 (= P110), L140 (≠ A112), A154 (≠ H126), L156 (≠ R128), P157 (= P129), V158 (≠ R130), N160 (= N132), T163 (≠ G135), S213 (≠ C170), E214 (= E171), G215 (= G172), G216 (≠ A173), S217 (≠ G174), Q233 (≠ V210), F237 (≠ L214), E260 (= E236), N261 (= N237), S262 (= S238), N263 (= N239), H267 (= H243), S356 (= S338), T357 (≠ S339), F388 (= F366), K486 (≠ R462)
1asyA Class ii aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA asp (see paper)
25% identity, 95% coverage: 20:462/466 of query aligns to 42:486/490 of 1asyA
- active site: R258 (= R234), E260 (= E236), R266 (= R242), H267 (= H243), E411 (= E389), S414 (≠ G392), R464 (= R440)
- binding : R52 (= R30), Q53 (≠ D31), Q54 (≠ S32), L58 (≠ I36), F60 (= F38), Q71 (= Q51), L73 (≠ V53), K88 (≠ L68), P111 (≠ S83), I112 (≠ P84), K113 (≠ G85), S114 (≠ A86), E135 (≠ D107), P138 (= P110), A154 (≠ H126), L156 (≠ R128), P157 (= P129), V158 (≠ R130), V159 (≠ T131), D162 (≠ I134), T163 (≠ G135), R258 (= R234), E260 (= E236), N261 (= N237), S262 (= S238), N263 (= N239), T264 (= T240), H267 (= H243), M268 (≠ L244), F271 (= F247), T357 (≠ S339), E411 (= E389), I412 (= I390), L413 (≠ I391), S414 (≠ G392), G459 (= G435), R464 (= R440), K486 (≠ R462)
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)
25% identity, 95% coverage: 20:462/466 of query aligns to 109:553/557 of P04802
- P273 (= P163) 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
>201369 FitnessBrowser__MR1:201369
MSIASVASVFKGEHAVGSTVTVRGWVRTRRDSKAGISFLAVYDGSCFNPIQGVVPNSLEN
YDNEVLKLTAGCSVIVTGDIVESPGAGQAYELQVTAVEVTGWVEDPDTYPMAAKRHSIEH
LRELAHLRPRTNIIGAVARVRNCLSQAIHRFYHENGFVWVSTPLITASDCEGAGEMFRVS
TLDMENLPRTSDGKVDYDKDFFGKEAFLTVSGQLNGETYACALSKIYTFGPTFRAENSNT
SRHLAEFWMVEPEVAFATLNDIAGLAEGMLKYAFNAVLTERMDDLQFFAQHVDKTVIERL
QSFVSSDFAQVDYTDAVEILQKSGREFEFPVSWGIDLSSEHERYLAEEHFKAPVVVKNYP
KDIKAFYMRLNEDGKTVAAMDVLAPGIGEIIGGSQREERLDVLDMRLEEMDLNKEDYWWY
RDLRRYGTVPHAGFGLGFERLVSYVTGVSNIRDVIPFPRAPRTANF
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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