SitesBLAST
Comparing H281DRAFT_04620 FitnessBrowser__Burk376:H281DRAFT_04620 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)
63% identity, 100% coverage: 3:599/599 of query aligns to 2:590/591 of Q51422
- H31 (= H32) 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 (= G83) 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)
63% identity, 100% coverage: 3:599/599 of query aligns to 1:589/589 of 4wj3M
- active site: R219 (= R220), E221 (= E222), R227 (= R228), Q228 (= Q229), E482 (= E491), G485 (= G494), R537 (= R546)
- binding : R28 (= R30), D29 (= D31), H30 (= H32), G32 (= G34), V33 (= V35), F35 (= F37), Q46 (= Q48), R64 (= R66), R76 (= R78), R78 (= R80), A82 (≠ T84), N84 (= N86), E93 (= E95), T107 (= T109), D113 (= D115), V118 (≠ L119)
4wj4A Crystal structure of non-discriminating aspartyl-tRNA synthetase from pseudomonas aeruginosa complexed with tRNA(asn) and aspartic acid (see paper)
64% identity, 99% coverage: 3:593/599 of query aligns to 1:584/585 of 4wj4A
- active site: R219 (= R220), E221 (= E222), R227 (= R228), Q228 (= Q229), E482 (= E491), G485 (= G494), R537 (= R546)
- binding aspartic acid: S195 (= S196), Q197 (= Q198), H450 (= H458), R489 (= R498), L531 (≠ I540)
- binding : R26 (= R28), R28 (= R30), D29 (= D31), H30 (= H32), G31 (= G33), G32 (= G34), V33 (= V35), F35 (= F37), Q46 (= Q48), R64 (= R66), R76 (= R78), P79 (= P81), A82 (≠ T84), N84 (= N86), E93 (= E95), T107 (= T109), P109 (= P111), D113 (= D115), E114 (≠ D116), D117 (≠ N118), E121 (≠ T122), A175 (= A176), E221 (= E222), D222 (= D223), R224 (= R225), A225 (= A226), R227 (= R228), Y346 (= Y348), A447 (= A455), H449 (= H457), H450 (= H458), R549 (= R558), T557 (= T566), Q558 (= Q567), S559 (≠ R568)
1c0aA Crystal structure of the e. Coli aspartyl-tRNA synthetase : trnaasp : aspartyl-adenylate complex (see paper)
58% identity, 98% coverage: 3:592/599 of query aligns to 1:583/585 of 1c0aA
- active site: E482 (= E491), G485 (= G494), R537 (= R546)
- binding aspartyl-adenosine-5'-monophosphate: S193 (= S196), Q195 (= Q198), K198 (= K201), R217 (= R220), Q226 (= Q229), F229 (= F232), Q231 (= Q234), H448 (= H457), E482 (= E491), V483 (≠ I492), G484 (= G493), G485 (= G494), G486 (= G495), R489 (= R498), L531 (≠ I540), A532 (= A541), G534 (= G543), R537 (= R546)
- binding adenosine monophosphate: F304 (= F308), V306 (= V310), K347 (= K351), G348 (= G352), A350 (= A354)
- binding : R26 (= R28), R28 (= R30), D29 (= D31), L30 (≠ H32), G31 (= G33), S32 (≠ G34), L33 (≠ V35), F35 (= F37), Q46 (= Q48), F48 (≠ V50), D50 (= D52), P51 (= P53), R64 (= R66), R76 (= R78), R78 (= R80), N82 (≠ T84), N84 (= N86), M87 (≠ L89), E93 (= E95), P109 (= P111), D111 (≠ Q113), N113 (≠ D115), H114 (≠ D116), N116 (= N118), T117 (≠ S120), E119 (≠ T122), 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 (= I347), H448 (= H457), H449 (= H458), F514 (= F523), R549 (= R558), T557 (= T566), T558 (≠ Q567), A559 (≠ R568)
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: 3:593/599 of query aligns to 1:576/577 of P56459
- L81 (≠ T84) mutation to N: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by reducing enzyme's ability to misacylate tRNA(Asn).
- L86 (= L89) 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: 3:587/599 of query aligns to 1:577/579 of 4rmfA
- active site: R215 (= R220), E217 (= E222), R223 (= R228), Q224 (= Q229), E481 (= E491), G484 (= G494), R536 (= R546)
- binding 2,2-bis(hydroxymethyl)propane-1,3-diol: H447 (= H457), D474 (= D484), E481 (= E491)
1g51B Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
50% identity, 99% coverage: 4:595/599 of query aligns to 3:580/580 of 1g51B
- active site: R223 (= R220), E225 (= E222), R231 (= R228), Q232 (= Q229), E476 (= E491), G479 (= G494), R531 (= R546)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E174), S199 (= S196), Q201 (= Q198), K204 (= K201), R223 (= R220), Q232 (= Q229), F235 (= F232), Q237 (= Q234), H442 (= H457), E476 (= E491), G478 (= G493), G479 (= G494), G480 (= G495), R483 (= R498), I525 (= I540), A526 (= A541), G528 (= G543), R531 (= R546)
- binding adenosine monophosphate: V313 (= V310), Q347 (≠ K351), G348 (= G352), L349 (= L353), A350 (= A354), V389 (≠ A399), A390 (= A400)
1g51A Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
50% identity, 99% coverage: 4:595/599 of query aligns to 3:580/580 of 1g51A