SitesBLAST
Comparing WP_029132131.1 NCBI__GCF_000428045.1:WP_029132131.1 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)
4wj4A Crystal structure of non-discriminating aspartyl-tRNA synthetase from pseudomonas aeruginosa complexed with tRNA(asn) and aspartic acid (see paper)
67% identity, 99% coverage: 1:588/596 of query aligns to 1:584/585 of 4wj4A
- active site: R219 (= R219), E221 (= E221), R227 (= R227), Q228 (= Q228), E482 (= E486), G485 (= G489), R537 (= R541)
- binding aspartic acid: S195 (= S195), Q197 (= Q197), H450 (= H453), R489 (= R493), L531 (= L535)
- binding : R26 (= R26), R28 (= R28), D29 (= D29), H30 (= H30), G31 (= G31), G32 (= G32), V33 (= V33), F35 (= F35), Q46 (= Q46), R64 (= R64), R76 (= R76), P79 (= P79), A82 (≠ T82), N84 (= N84), E93 (= E93), T107 (= T107), P109 (= P109), D113 (= D113), E114 (= E114), D117 (≠ R117), E121 (= E121), A175 (= A175), E221 (= E221), D222 (= D222), R224 (= R224), A225 (= A225), R227 (= R227), Y346 (= Y347), A447 (= A450), H449 (= H452), H450 (= H453), R549 (= R553), T557 (= T561), Q558 (= Q562), S559 (≠ T563)
4wj3M Crystal structure of the asparagine transamidosome from pseudomonas aeruginosa (see paper)
67% identity, 99% coverage: 1:588/596 of query aligns to 1:584/589 of 4wj3M
- active site: R219 (= R219), E221 (= E221), R227 (= R227), Q228 (= Q228), E482 (= E486), G485 (= G489), R537 (= R541)
- binding : R28 (= R28), D29 (= D29), H30 (= H30), G32 (= G32), V33 (= V33), F35 (= F35), Q46 (= Q46), R64 (= R64), R76 (= R76), R78 (= R78), A82 (≠ T82), N84 (= N84), E93 (= E93), T107 (= T107), D113 (= D113), V118 (= V118)
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)
67% identity, 99% coverage: 1:593/596 of query aligns to 2:591/591 of Q51422
- H31 (= H30) 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 (= G81) 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)
61% identity, 98% coverage: 1:587/596 of query aligns to 1:583/585 of 1c0aA
- active site: E482 (= E486), G485 (= G489), R537 (= R541)
- binding aspartyl-adenosine-5'-monophosphate: S193 (= S195), Q195 (= Q197), K198 (= K200), R217 (= R219), Q226 (= Q228), F229 (= F231), Q231 (= Q233), H448 (= H452), E482 (= E486), V483 (= V487), G484 (= G488), G485 (= G489), G486 (= G490), R489 (= R493), L531 (= L535), A532 (= A536), G534 (= G538), R537 (= R541)
- binding adenosine monophosphate: F304 (= F307), V306 (= V309), K347 (≠ R350), G348 (= G351), A350 (= A353)
- binding : R26 (= R26), R28 (= R28), D29 (= D29), L30 (≠ H30), G31 (= G31), S32 (≠ G32), L33 (≠ V33), F35 (= F35), Q46 (= Q46), F48 (≠ V48), D50 (= D50), P51 (= P51), R64 (= R64), R76 (= R76), R78 (= R78), N82 (≠ T82), N84 (= N84), M87 (= M87), E93 (= E93), P109 (= P109), D111 (= D113), N113 (≠ H115), H114 (≠ E116), N116 (≠ V118), T117 (≠ S119), E119 (= E121), T169 (= T171), P170 (= P172), E171 (= E173), G172 (= G174), A173 (= A175), S193 (= S195), R217 (= R219), E219 (= E221), D220 (= D222), R222 (= R224), A223 (= A225), R225 (= R227), I343 (= I346), H448 (= H452), H449 (= H453), F514 (= F518), R549 (= R553), T557 (= T561), T558 (≠ Q562), A559 (≠ T563)
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)
49% identity, 99% coverage: 1:588/596 of query aligns to 1:576/577 of P56459
- L81 (≠ T82) mutation to N: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by reducing enzyme's ability to misacylate tRNA(Asn).
- L86 (≠ M87) 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)
52% identity, 99% coverage: 2:590/596 of query aligns to 4:581/581 of 6sjcB
- binding 5'-O-(L-alpha-aspartylsulfamoyl)adenosine: E178 (= E173), Q202 (= Q197), K205 (= K200), R224 (= R219), R232 (= R227), Q233 (= Q228), F236 (= F231), Q238 (= Q233), E477 (= E486), V478 (= V487), G479 (= G488), G480 (= G489), G481 (= G490), R484 (= R493), I526 (≠ L535), A527 (= A536), G529 (= G538), R532 (= R541)
1g51B Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
52% identity, 99% coverage: 2:590/596 of query aligns to 3:580/580 of 1g51B
- active site: R223 (= R219), E225 (= E221), R231 (= R227), Q232 (= Q228), E476 (= E486), G479 (= G489), R531 (= R541)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E173), S199 (= S195), Q201 (= Q197), K204 (= K200), R223 (= R219), Q232 (= Q228), F235 (= F231), Q237 (= Q233), H442 (= H452), E476 (= E486), G478 (= G488), G479 (= G489), G480 (= G490), R483 (= R493), I525 (≠ L535), A526 (= A536), G528 (= G538), R531 (= R541)
- binding adenosine monophosphate: V313 (= V309), Q347 (≠ R350), G348 (= G351), L349 (= L352), A350 (= A353), V389 (≠ G399), A390 (= A400)
1g51A Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
52% identity, 99% coverage: 2:590/596 of query aligns to 3:580/580 of 1g51A
- active site: R223 (= R219), E225 (= E221), R231 (= R227), Q232 (= Q228), E476 (= E486), G479 (= G489), R531 (= R541)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E173), Q201 (= Q197), K204 (= K200), R223 (= R219), R231 (= R227), Q232 (= Q228), F235 (= F231), Q237 (= Q233), H442 (= H452), H443 (= H453), E476 (= E486), G478 (= G488), G479 (= G489), G480 (= G490), R483 (= R493), I525 (≠ L535), A526 (= A536), G528 (= G538), R531 (= R541)
1efwA Crystal structure of aspartyl-tRNA synthetase from thermus thermophilus complexed to trnaasp from escherichia coli (see paper)
52% identity, 99% coverage: 2:590/596 of query aligns to 3:580/580 of 1efwA
- active site: R223 (= R219), E225 (= E221), R231 (= R227), Q232 (= Q228), E476 (= E486), G479 (= G489), R531 (= R541)
- binding : R27 (= R26), R29 (= R28), D30 (= D29), L31 (≠ H30), G32 (= G31), G33 (= G32), L34 (≠ V33), F36 (= F35), Q47 (= Q46), H51 (≠ D50), P52 (= P51), R64 (= R64), R78 (= R78), E80 (= E80), N82 (= N84), R84 (≠ D86), E91 (= E93), T105 (= T107), P107 (= P109), E125 (= E121), R343 (≠ I346)
4rmfA Biochemical and structural characterization of mycobacterial aspartyl- tRNA synthetase asps, a promising tb drug target (see paper)
48% identity, 98% coverage: 1:582/596 of query aligns to 1:577/579 of 4rmfA
- active site: R215 (= R219), E217 (= E221), R223 (= R227), Q224 (= Q228), E481 (= E486), G484 (= G489), R536 (= R541)
- binding 2,2-bis(hydroxymethyl)propane-1,3-diol: H447 (= H452), D474 (= D479), E481 (= E486)
4o2dA Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
48% identity, 98% coverage: 1:585/596 of query aligns to 2:579/580 of 4o2dA
- active site: R216 (= R219), E218 (= E221), R222 (= R227), Q223 (= Q228), E480 (= E486), G483 (= G489), R535 (= R541)
- binding aspartic acid: E170 (= E173), S192 (= S195), Q194 (= Q197), Q228 (= Q233), H446 (= H452), H447 (= H453), G483 (= G489), R487 (= R493), I529 (≠ L535), A530 (= A536)
6hhxA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)cytidine (see paper)
51% identity, 98% coverage: 2:587/596 of query aligns to 4:573/574 of 6hhxA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)cytidine: Q202 (= Q197), K205 (= K200), R224 (= R219), F236 (= F231), Q238 (= Q233), H438 (= H452), E472 (= E486), V473 (= V487), G474 (= G488), G475 (= G489), G476 (= G490), R479 (= R493), I521 (≠ L535), A522 (= A536), G524 (= G538)
6hhwA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)uridine (see paper)
51% identity, 98% coverage: 2:587/596 of query aligns to 4:573/574 of 6hhwA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)uridine: Q202 (= Q197), K205 (= K200), R224 (= R219), F236 (= F231), Q238 (= Q233), H438 (= H452), E472 (= E486), V473 (= V487), G474 (= G488), G475 (= G489), G476 (= G490), R479 (= R493), I521 (≠ L535), A522 (= A536), G524 (= G538)
6hhvA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)n3-methyluridine (see paper)
51% identity, 98% coverage: 2:587/596 of query aligns to 4:573/574 of 6hhvA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)N3-methyluridine: Q202 (= Q197), R224 (= R219), F236 (= F231), Q238 (= Q233), H438 (= H452), E472 (= E486), V473 (= V487), G474 (= G488), G475 (= G489), G476 (= G490), R479 (= R493), I521 (≠ L535), A522 (= A536), G524 (= G538), R527 (= R541)
7ap4A Thermus thermophilus aspartyl-tRNA synthetase in complex with compound asps7hmdda (see paper)
51% identity, 98% coverage: 2:587/596 of query aligns to 4:572/573 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 (= Q197), R222 (= R219), R230 (= R227), Q231 (= Q228), F234 (= F231), Q236 (= Q233), E471 (= E486), G473 (= G488), G474 (= G489), G475 (= G490), R478 (= R493), I520 (≠ L535), A521 (= A536), G523 (= G538)
5w25A Crystal structure of aspartyl-tRNA synthetase from mycobacterium tuberculosis complexed with l-aspartic acid
48% identity, 98% coverage: 1:582/596 of query aligns to 3:582/583 of 5w25A
- active site: R220 (= R219), E222 (= E221), R228 (= R227), Q229 (= Q228), E486 (= E486), G489 (= G489), R541 (= R541)
- binding aspartic acid: E174 (= E173), Q198 (= Q197), R220 (= R219), H452 (= H452), H453 (= H453), G489 (= G489), R493 (= R493)
- binding lysine: D159 (≠ G158), R211 (= R210)
Q6PI48 Aspartate--tRNA ligase, mitochondrial; Aspartyl-tRNA synthetase; AspRS; EC 6.1.1.12 from Homo sapiens (Human) (see 2 papers)
39% identity, 99% coverage: 1:590/596 of query aligns to 49:636/645 of Q6PI48
- R58 (≠ N10) mutation to G: No effect on its mitochondria localization.
- T136 (= T89) mutation to S: No effect on its mitochondria localization.
- Q184 (= Q137) to K: in LBSL; Significant impairment of its mitochondrial matrix localization; dbSNP:rs1469160736
- R263 (= R216) to Q: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918207
- G338 (≠ P292) mutation to E: No effect on its mitochondria localization.
- L613 (≠ M567) to F: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918212
- L626 (= L580) 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
4o2dB Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
52% identity, 50% coverage: 1:300/596 of query aligns to 2:294/515 of 4o2dB
Sites not aligning to the query:
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
35% identity, 47% coverage: 2:283/596 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)
35% identity, 47% coverage: 2:283/596 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_029132131.1 NCBI__GCF_000428045.1:WP_029132131.1
MRTHYCGHINASHIDQEVEICGWVHRRRDHGGVIFIDLRDREGLVQVVYDPDLPEIFSTA
EQVRNEYVLKLRGRVRARPEGTVNPDMPTGEIEILGLGLEVLNRADTPPFQLDEHERVSE
EVRLRYRYMDLRRPEMQKRIMLRAAVTRALRSYLDDNGFLDIETPMLTKATPEGARDYLV
PSRTHPGHFFALPQSPQLFKQLLMMSGMDRYYQIVRCFRDEDLRADRQPEFTQLDIETSF
MSESEIMDSMEEMIRGVVKQVLDVELPNPFPHMTYQEAMRRFGSDRPDLRCPLELVDVAD
LMGGVDFKVFSGPAKDPKGRVAALCLPKGCELTRKEIDEYTKYVGIYGARGLAYIKVNDW
AGQGRDGLQSPILKFLPDAAVDGIMQRTGAVDGDLIFFGADKASVVNEALGALRVKLGED
RGLMQPGWHPVWVVDFPMFEWDEGGERWNALHHPFTAPKEDQLELLETDPGACLSRAYDM
VLNGTEVGGGSIRIHNSAVQEKVFRLLGIGEEEAEEKFGFLLSALRYGCPPHGGLAFGLD
RLVMLLAGASSIRDVMAFPKTQTAACMLTSAPSEVSPAQLRELSIRVRTPQVEEKG
Or try a new SitesBLAST search
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