SitesBLAST
Comparing PfGW456L13_1849 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_1849 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)
Q51422 Aspartate--tRNA(Asp/Asn) ligase; Aspartyl-tRNA synthetase; AspRS; Non-discriminating aspartyl-tRNA synthetase; ND-AspRS; EC 6.1.1.23 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see paper)
89% identity, 100% coverage: 1:591/591 of query aligns to 1:591/591 of Q51422
- H31 (= H31) mutation to L: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn) by 3.5-fold, by reducing enzyme's ability to misacylate tRNA(Asn) when tested against E.coli tRNA, but shows little effect when tested against P.aeruginosa tRNA.
- G82 (= G82) mutation to K: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn) by 4.2-fold, by reducing enzyme's ability to misacylate tRNA(Asn) when tested against E.coli tRNA, but shows little effect when tested against P.aeruginosa tRNA.
4wj3M Crystal structure of the asparagine transamidosome from pseudomonas aeruginosa (see paper)
89% identity, 100% coverage: 2:590/591 of query aligns to 1:589/589 of 4wj3M
- active site: R219 (= R220), E221 (= E222), R227 (= R228), Q228 (= Q229), E482 (= E483), G485 (= G486), R537 (= R538)
- binding : R28 (= R29), D29 (= D30), H30 (= H31), G32 (= G33), V33 (= V34), F35 (= F36), Q46 (= Q47), R64 (= R65), R76 (= R77), R78 (= R79), A82 (= A83), N84 (= N85), E93 (= E94), T107 (= T108), D113 (≠ N114), V118 (= V119)
4wj4A Crystal structure of non-discriminating aspartyl-tRNA synthetase from pseudomonas aeruginosa complexed with tRNA(asn) and aspartic acid (see paper)
89% identity, 99% coverage: 2:586/591 of query aligns to 1:585/585 of 4wj4A
- active site: R219 (= R220), E221 (= E222), R227 (= R228), Q228 (= Q229), E482 (= E483), G485 (= G486), R537 (= R538)
- binding aspartic acid: S195 (= S196), Q197 (= Q198), H450 (= H451), R489 (= R490), L531 (= L532)
- binding : R26 (= R27), R28 (= R29), D29 (= D30), H30 (= H31), G31 (= G32), G32 (= G33), V33 (= V34), F35 (= F36), Q46 (= Q47), R64 (= R65), R76 (= R77), P79 (= P80), A82 (= A83), N84 (= N85), E93 (= E94), T107 (= T108), P109 (= P110), D113 (≠ N114), E114 (= E115), D117 (= D118), E121 (= E122), A175 (= A176), E221 (= E222), D222 (= D223), R224 (= R225), A225 (= A226), R227 (= R228), Y346 (= Y347), A447 (= A448), H449 (= H450), H450 (= H451), R549 (= R550), T557 (= T558), Q558 (= Q559), S559 (= S560)
1c0aA Crystal structure of the e. Coli aspartyl-tRNA synthetase : trnaasp : aspartyl-adenylate complex (see paper)
63% identity, 99% coverage: 2:584/591 of query aligns to 1:583/585 of 1c0aA
- active site: E482 (= E483), G485 (= G486), R537 (= R538)
- binding aspartyl-adenosine-5'-monophosphate: S193 (= S196), Q195 (= Q198), K198 (= K201), R217 (= R220), Q226 (= Q229), F229 (= F232), Q231 (= Q234), H448 (= H450), E482 (= E483), V483 (≠ L484), G484 (= G485), G485 (= G486), G486 (= G487), R489 (= R490), L531 (= L532), A532 (= A533), G534 (= G535), R537 (= R538)
- binding adenosine monophosphate: F304 (= F307), V306 (= V309), K347 (= K350), G348 (= G351), A350 (= A353)
- binding : R26 (= R27), R28 (= R29), D29 (= D30), L30 (≠ H31), G31 (= G32), S32 (≠ G33), L33 (≠ V34), F35 (= F36), Q46 (= Q47), F48 (≠ V49), D50 (= D51), P51 (= P52), R64 (= R65), R76 (= R77), R78 (= R79), N82 (≠ A83), N84 (= N85), M87 (= M88), E93 (= E94), P109 (= P110), D111 (≠ P112), N113 (= N114), H114 (≠ E115), N116 (≠ S117), T117 (≠ D118), E119 (= E122), T169 (= T172), P170 (= P173), E171 (= E174), G172 (= G175), A173 (= A176), S193 (= S196), R217 (= R220), E219 (= E222), D220 (= D223), R222 (= R225), A223 (= A226), R225 (= R228), I343 (= I346), H448 (= H450), H449 (= H451), F514 (= F515), R549 (= R550), T557 (= T558), T558 (≠ Q559), A559 (≠ S560)
P56459 Aspartate--tRNA(Asp/Asn) ligase; Aspartyl-tRNA synthetase; AspRS; Non-discriminating aspartyl-tRNA synthetase; ND-AspRS; EC 6.1.1.23 from Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) (see paper)
52% identity, 99% coverage: 2:586/591 of query aligns to 1:577/577 of P56459
- L81 (≠ A83) mutation to N: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by reducing enzyme's ability to misacylate tRNA(Asn).
- L86 (≠ M88) mutation to M: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by reducing enzyme's ability to misacylate tRNA(Asn).
4rmfA Biochemical and structural characterization of mycobacterial aspartyl- tRNA synthetase asps, a promising tb drug target (see paper)
49% identity, 98% coverage: 2:579/591 of query aligns to 1:577/579 of 4rmfA
- active site: R215 (= R220), E217 (= E222), R223 (= R228), Q224 (= Q229), E481 (= E483), G484 (= G486), R536 (= R538)
- binding 2,2-bis(hydroxymethyl)propane-1,3-diol: H447 (= H450), D474 (= D476), E481 (= E483)
4o2dA Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
49% identity, 98% coverage: 1:582/591 of query aligns to 1:579/580 of 4o2dA
- active site: R216 (= R220), E218 (= E222), R222 (= R228), Q223 (= Q229), E480 (= E483), G483 (= G486), R535 (= R538)
- binding aspartic acid: E170 (= E174), S192 (= S196), Q194 (= Q198), Q228 (= Q234), H446 (= H450), H447 (= H451), G483 (= G486), R487 (= R490), I529 (≠ L532), A530 (= A533)
5w25A Crystal structure of aspartyl-tRNA synthetase from mycobacterium tuberculosis complexed with l-aspartic acid
49% identity, 98% coverage: 1:579/591 of query aligns to 2:582/583 of 5w25A