SitesBLAST
Comparing WP_013721500.1 NCBI__GCF_000204645.1:WP_013721500.1 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)
4wj4A Crystal structure of non-discriminating aspartyl-tRNA synthetase from pseudomonas aeruginosa complexed with tRNA(asn) and aspartic acid (see paper)
62% identity, 99% coverage: 3:593/599 of query aligns to 1:585/585 of 4wj4A
- active site: R219 (= R220), E221 (= E222), R227 (= R228), Q228 (= Q229), E482 (= E490), G485 (= G493), R537 (= R545)
- binding aspartic acid: S195 (= S196), Q197 (= Q198), H450 (= H457), R489 (= R497), L531 (= L539)
- 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 (= Y347), A447 (= A454), H449 (= H456), H450 (= H457), R549 (= R557), T557 (= T565), Q558 (= Q566), S559 (≠ R567)
4wj3M Crystal structure of the asparagine transamidosome from pseudomonas aeruginosa (see paper)
62% identity, 99% coverage: 3:593/599 of query aligns to 1:585/589 of 4wj3M
- active site: R219 (= R220), E221 (= E222), R227 (= R228), Q228 (= Q229), E482 (= E490), G485 (= G493), R537 (= R545)
- 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)
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)
62% identity, 99% coverage: 3:593/599 of query aligns to 2:586/591 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.
1c0aA Crystal structure of the e. Coli aspartyl-tRNA synthetase : trnaasp : aspartyl-adenylate complex (see paper)
57% identity, 98% coverage: 3:591/599 of query aligns to 1:583/585 of 1c0aA
- active site: E482 (= E490), G485 (= G493), R537 (= R545)
- binding aspartyl-adenosine-5'-monophosphate: S193 (= S196), Q195 (= Q198), K198 (= K201), R217 (= R220), Q226 (= Q229), F229 (= F232), Q231 (= Q234), H448 (= H456), E482 (= E490), V483 (≠ L491), G484 (= G492), G485 (= G493), G486 (= G494), R489 (= R497), L531 (= L539), A532 (= A540), G534 (= G542), R537 (= R545)
- binding adenosine monophosphate: F304 (= F307), V306 (= V309), K347 (= K350), G348 (= G351), A350 (= A353)
- 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 (= I346), H448 (= H456), H449 (= H457), F514 (= F522), R549 (= R557), T557 (= T565), T558 (≠ Q566), A559 (≠ R567)
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)
51% identity, 98% coverage: 3:592/599 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).
6sjcB Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)adenosine (see paper)
49% identity, 99% coverage: 4:594/599 of query aligns to 4:581/581 of 6sjcB
- binding 5'-O-(L-alpha-aspartylsulfamoyl)adenosine: E178 (= E174), Q202 (= Q198), K205 (= K201), R224 (= R220), R232 (= R228), Q233 (= Q229), F236 (= F232), Q238 (= Q234), E477 (= E490), V478 (≠ L491), G479 (= G492), G480 (= G493), G481 (= G494), R484 (= R497), I526 (≠ L539), A527 (= A540), G529 (= G542), R532 (= R545)
1g51B Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
49% identity, 99% coverage: 4:594/599 of query aligns to 3:580/580 of 1g51B
- active site: R223 (= R220), E225 (= E222), R231 (= R228), Q232 (= Q229), E476 (= E490), G479 (= G493), R531 (= R545)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E174), S199 (= S196), Q201 (= Q198), K204 (= K201), R223 (= R220), Q232 (= Q229), F235 (= F232), Q237 (= Q234), H442 (= H456), E476 (= E490), G478 (= G492), G479 (= G493), G480 (= G494), R483 (= R497), I525 (≠ L539), A526 (= A540), G528 (= G542), R531 (= R545)
- binding adenosine monophosphate: V313 (= V309), Q347 (≠ K350), G348 (= G351), L349 (= L352), A350 (= A353), V389 (≠ G398), A390 (= A399)
1g51A Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
49% identity, 99% coverage: 4:594/599 of query aligns to 3:580/580 of 1g51A
- active site: R223 (= R220), E225 (= E222), R231 (= R228), Q232 (= Q229), E476 (= E490), G479 (= G493), R531 (= R545)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E174), Q201 (= Q198), K204 (= K201), R223 (= R220), R231 (= R228), Q232 (= Q229), F235 (= F232), Q237 (= Q234), H442 (= H456), H443 (= H457), E476 (= E490), G478 (= G492), G479 (= G493), G480 (= G494), R483 (= R497), I525 (≠ L539), A526 (= A540), G528 (= G542), R531 (= R545)
1efwA Crystal structure of aspartyl-tRNA synthetase from thermus thermophilus complexed to trnaasp from escherichia coli (see paper)
49% identity, 99% coverage: 4:594/599 of query aligns to 3:580/580 of 1efwA
- active site: R223 (= R220), E225 (= E222), R231 (= R228), Q232 (= Q229), E476 (= E490), G479 (= G493), R531 (= R545)
- binding : R27 (= R28), R29 (= R30), D30 (= D31), L31 (≠ H32), G32 (= G33), G33 (= G34), L34 (≠ V35), F36 (= F37), Q47 (= Q48), H51 (≠ D52), P52 (= P53), R64 (= R66), R78 (= R80), E80 (≠ T84), N82 (= N86), R84 (≠ K88), E91 (= E95), T105 (= T109), P107 (= P111), E125 (≠ T122), R343 (≠ I346)
4rmfA Biochemical and structural characterization of mycobacterial aspartyl- tRNA synthetase asps, a promising tb drug target (see paper)
48% identity, 97% coverage: 3:586/599 of query aligns to 1:577/579 of 4rmfA
- active site: R215 (= R220), E217 (= E222), R223 (= R228), Q224 (= Q229), E481 (= E490), G484 (= G493), R536 (= R545)
- binding 2,2-bis(hydroxymethyl)propane-1,3-diol: H447 (= H456), D474 (= D483), E481 (= E490)
6hhxA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)cytidine (see paper)
49% identity, 98% coverage: 4:589/599 of query aligns to 4:571/574 of 6hhxA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)cytidine: Q202 (= Q198), K205 (= K201), R224 (= R220), F236 (= F232), Q238 (= Q234), H438 (= H456), E472 (= E490), V473 (≠ L491), G474 (= G492), G475 (= G493), G476 (= G494), R479 (= R497), I521 (≠ L539), A522 (= A540), G524 (= G542)
6hhwA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)uridine (see paper)
49% identity, 98% coverage: 4:589/599 of query aligns to 4:571/574 of 6hhwA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)uridine: Q202 (= Q198), K205 (= K201), R224 (= R220), F236 (= F232), Q238 (= Q234), H438 (= H456), E472 (= E490), V473 (≠ L491), G474 (= G492), G475 (= G493), G476 (= G494), R479 (= R497), I521 (≠ L539), A522 (= A540), G524 (= G542)
6hhvA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)n3-methyluridine (see paper)
49% identity, 98% coverage: 4:589/599 of query aligns to 4:571/574 of 6hhvA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)N3-methyluridine: Q202 (= Q198), R224 (= R220), F236 (= F232), Q238 (= Q234), H438 (= H456), E472 (= E490), V473 (≠ L491), G474 (= G492), G475 (= G493), G476 (= G494), R479 (= R497), I521 (≠ L539), A522 (= A540), G524 (= G542), R527 (= R545)
4o2dA Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
47% identity, 98% coverage: 3:589/599 of query aligns to 2:579/580 of 4o2dA
- active site: R216 (= R220), E218 (= E222), R222 (= R228), Q223 (= Q229), E480 (= E490), G483 (= G493), R535 (= R545)
- binding aspartic acid: E170 (= E174), S192 (= S196), Q194 (= Q198), Q228 (= Q234), H446 (= H456), H447 (= H457), G483 (= G493), R487 (= R497), I529 (≠ L539), A530 (= A540)
7ap4A Thermus thermophilus aspartyl-tRNA synthetase in complex with compound asps7hmdda (see paper)
49% identity, 98% coverage: 4:589/599 of query aligns to 4:570/573 of 7ap4A
- binding (3~{S})-3-azanyl-4-[[(2~{R},3~{S},4~{R},5~{R})-5-[7-azanyl-5-(hydroxymethyl)benzimidazol-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxysulfonylamino]-4-oxidanylidene-butanoic acid: Q200 (= Q198), R222 (= R220), R230 (= R228), Q231 (= Q229), F234 (= F232), Q236 (= Q234), E471 (= E490), G473 (= G492), G474 (= G493), G475 (= G494), R478 (= R497), I520 (≠ L539), A521 (= A540), G523 (= G542)
5w25A Crystal structure of aspartyl-tRNA synthetase from mycobacterium tuberculosis complexed with l-aspartic acid
47% identity, 97% coverage: 3:586/599 of query aligns to 3:582/583 of 5w25A
- active site: R220 (= R220), E222 (= E222), R228 (= R228), Q229 (= Q229), E486 (= E490), G489 (= G493), R541 (= R545)
- binding aspartic acid: E174 (= E174), Q198 (= Q198), R220 (= R220), H452 (= H456), H453 (= H457), G489 (= G493), R493 (= R497)
- binding lysine: D159 (≠ G159), R211 (= R211)
4o2dB Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
42% identity, 98% coverage: 3:589/599 of query aligns to 2:514/515 of 4o2dB
- active site: R216 (= R220), E218 (= E222), R222 (= R228), Q223 (= Q229), E415 (= E490), G418 (= G493), R470 (= R545)
- binding aspartic acid: E170 (= E174), S192 (= S196), Q194 (= Q198), Q228 (= Q234), H382 (= H457), G418 (= G493), R422 (= R497), I464 (≠ L539), A465 (= A540)
Q6PI48 Aspartate--tRNA ligase, mitochondrial; Aspartyl-tRNA synthetase; AspRS; EC 6.1.1.12 from Homo sapiens (Human) (see 2 papers)
38% identity, 99% coverage: 1:595/599 of query aligns to 47:637/645 of Q6PI48
- R58 (≠ T12) mutation to G: No effect on its mitochondria localization.
- T136 (≠ S91) mutation to S: No effect on its mitochondria localization.
- Q184 (= Q138) to K: in LBSL; Significant impairment of its mitochondrial matrix localization; dbSNP:rs1469160736
- R263 (≠ K217) to Q: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918207
- G338 (≠ K292) mutation to E: No effect on its mitochondria localization.
- L613 (= L571) to F: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918212
- L626 (= L584) to Q: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918213
Sites not aligning to the query:
- 45 S → G: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918209
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
36% identity, 47% coverage: 4:283/599 of query aligns to 3:293/438 of 3nemB
Sites not aligning to the query:
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
36% identity, 47% coverage: 4:283/599 of query aligns to 3:293/438 of 3nemA
Sites not aligning to the query:
- active site: 361, 364, 412
- binding aspartyl-adenosine-5'-monophosphate: 339, 361, 362, 363, 364, 365, 368, 406, 407, 409, 412
Query Sequence
>WP_013721500.1 NCBI__GCF_000204645.1:WP_013721500.1
MAMRSHYCGLVTEALMGQTVSLCGWVNRRRDHGGVIFIDLRDREGYVQVVCDPDRPEMFK
VAEDIRNEFCVRVQGVVRARPAGTTNDKLKSGQIEVLCHELDVLNPSVTPPFQMDDDNLS
ETTRLTHRVMDLRRPAMQRNLMLRYKTAIQVRNFLDKEGFVDIETPMLGKSTPEGARDYL
VPSRVHDGQFFALPQSPQLYKQMLMVAGYDRYYQITKCFRDEDLRADRQPEFTQIDCETS
FLNEEEIRAIFQRMIVEVFKQQLDVDLGEFPTMAYAEAMHRFGSDKPDLRVKLEFTELTD
VMRDVDFKVFSTPATTKGGRVVALRVPGGAAISRGEIDQYTEFVKIYGAKGLAWIKVNEA
AKGRDGLQSPIVKNIHDAAIAEILKRTGAQDGDLVFFGADKEKIVNDSIGALRLKVGHSE
FGRQNGLFENRWAPLWVVDFPMFEHDEDEDRWVAVHHPFTSPKDGHEDLMDTDPGKCIAK
AYDMVLNGWELGGGSVRIHRADVQSKVFSALKIGPEDARAKFGYLLDALQYGAPPHGGLA
FGLDRLITLMTGAESIRDVIAFPKTQRAQDLLTQAPSPVDEKQLRELHIRLRNPVPAVG
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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