SitesBLAST
Comparing WP_012969945.1 NCBI__GCF_000025485.1:WP_012969945.1 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)
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)
66% identity, 99% coverage: 1:589/592 of query aligns to 2:585/591 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.
4wj4A Crystal structure of non-discriminating aspartyl-tRNA synthetase from pseudomonas aeruginosa complexed with tRNA(asn) and aspartic acid (see paper)
66% identity, 99% coverage: 1:589/592 of query aligns to 1:584/585 of 4wj4A
- active site: R219 (= R220), E221 (= E222), R227 (= R228), Q228 (= Q229), E482 (= E487), G485 (= G490), R537 (= R542)
- binding aspartic acid: S195 (= S196), Q197 (= Q198), H450 (= H454), R489 (= R494), L531 (= L536)
- 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 (≠ S114), D117 (= D118), E121 (= E122), A175 (= A176), E221 (= E222), D222 (= D223), R224 (= R225), A225 (= A226), R227 (= R228), Y346 (= Y348), A447 (= A451), H449 (= H453), H450 (= H454), R549 (= R554), T557 (= T562), Q558 (= Q563), S559 (≠ T564)
4wj3M Crystal structure of the asparagine transamidosome from pseudomonas aeruginosa (see paper)
66% identity, 99% coverage: 1:589/592 of query aligns to 1:584/589 of 4wj3M
- active site: R219 (= R220), E221 (= E222), R227 (= R228), Q228 (= Q229), E482 (= E487), G485 (= G490), R537 (= R542)
- 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 (≠ A119)
1c0aA Crystal structure of the e. Coli aspartyl-tRNA synthetase : trnaasp : aspartyl-adenylate complex (see paper)
61% identity, 99% coverage: 1:588/592 of query aligns to 1:583/585 of 1c0aA
- active site: E482 (= E487), G485 (= G490), R537 (= R542)
- binding aspartyl-adenosine-5'-monophosphate: S193 (= S196), Q195 (= Q198), K198 (= K201), R217 (= R220), Q226 (= Q229), F229 (= F232), Q231 (= Q234), H448 (= H453), E482 (= E487), V483 (≠ L488), G484 (= G489), G485 (= G490), G486 (= G491), R489 (= R494), L531 (= L536), A532 (= A537), G534 (= G539), R537 (= R542)
- binding adenosine monophosphate: F304 (= F308), V306 (= V310), K347 (= K351), G348 (= G352), A350 (= A354)
- 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 (≠ L87), E93 (= E93), P109 (= P109), D111 (= D113), N113 (≠ H115), H114 (≠ A116), N116 (≠ D118), T117 (≠ S120), 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 (= I347), H448 (= H453), H449 (= H454), F514 (= F519), R549 (= R554), T557 (= T562), T558 (≠ Q563), A559 (≠ T564)
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, 99% coverage: 1:589/592 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 (= L87) 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: 1:583/592 of query aligns to 1:577/579 of 4rmfA
- active site: R215 (= R220), E217 (= E222), R223 (= R228), Q224 (= Q229), E481 (= E487), G484 (= G490), R536 (= R542)
- binding 2,2-bis(hydroxymethyl)propane-1,3-diol: H447 (= H453), D474 (= D480), E481 (= E487)
5w25A Crystal structure of aspartyl-tRNA synthetase from mycobacterium tuberculosis complexed with l-aspartic acid
49% identity, 98% coverage: 1:583/592 of query aligns to 3:582/583 of 5w25A
- active site: R220 (= R220), E222 (= E222), R228 (= R228), Q229 (= Q229), E486 (= E487), G489 (= G490), R541 (= R542)
- binding aspartic acid: E174 (= E174), Q198 (= Q198), R220 (= R220), H452 (= H453), H453 (= H454), G489 (= G490), R493 (= R494)
- binding lysine: D159 (≠ G159), R211 (= R211)
4o2dA Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
49% identity, 99% coverage: 1:586/592 of query aligns to 2:579/580 of 4o2dA
- active site: R216 (= R220), E218 (= E222), R222 (= R228), Q223 (= Q229), E480 (= E487), G483 (= G490), R535 (= R542)
- binding aspartic acid: E170 (= E174), S192 (= S196), Q194 (= Q198), Q228 (= Q234), H446 (= H453), H447 (= H454), G483 (= G490), R487 (= R494), I529 (≠ L536), A530 (= A537)
6sjcB Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)adenosine (see paper)
53% identity, 99% coverage: 2:586/592 of query aligns to 4:576/581 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 (= E487), V478 (≠ L488), G479 (= G489), G480 (= G490), G481 (= G491), R484 (= R494), I526 (≠ L536), A527 (= A537), G529 (= G539), R532 (= R542)
1g51B Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
53% identity, 99% coverage: 2:586/592 of query aligns to 3:575/580 of 1g51B
- active site: R223 (= R220), E225 (= E222), R231 (= R228), Q232 (= Q229), E476 (= E487), G479 (= G490), R531 (= R542)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E174), S199 (= S196), Q201 (= Q198), K204 (= K201), R223 (= R220), Q232 (= Q229), F235 (= F232), Q237 (= Q234), H442 (= H453), E476 (= E487), G478 (= G489), G479 (= G490), G480 (= G491), R483 (= R494), I525 (≠ L536), A526 (= A537), G528 (= G539), R531 (= R542)
- binding adenosine monophosphate: V313 (= V310), Q347 (≠ K351), G348 (= G352), L349 (= L353), A350 (= A354), V389 (≠ G400), A390 (= A401)
1g51A Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
53% identity, 99% coverage: 2:586/592 of query aligns to 3:575/580 of 1g51A
- active site: R223 (= R220), E225 (= E222), R231 (= R228), Q232 (= Q229), E476 (= E487), G479 (= G490), R531 (= R542)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E174), Q201 (= Q198), K204 (= K201), R223 (= R220), R231 (= R228), Q232 (= Q229), F235 (= F232), Q237 (= Q234), H442 (= H453), H443 (= H454), E476 (= E487), G478 (= G489), G479 (= G490), G480 (= G491), R483 (= R494), I525 (≠ L536), A526 (= A537), G528 (= G539), R531 (= R542)
1efwA Crystal structure of aspartyl-tRNA synthetase from thermus thermophilus complexed to trnaasp from escherichia coli (see paper)
53% identity, 99% coverage: 2:586/592 of query aligns to 3:575/580 of 1efwA
- active site: R223 (= R220), E225 (= E222), R231 (= R228), Q232 (= Q229), E476 (= E487), G479 (= G490), R531 (= R542)
- 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 (= E122), R343 (≠ I347)
6hhxA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)cytidine (see paper)
53% identity, 99% coverage: 2:586/592 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 (= H453), E472 (= E487), V473 (≠ L488), G474 (= G489), G475 (= G490), G476 (= G491), R479 (= R494), I521 (≠ L536), A522 (= A537), G524 (= G539)
6hhwA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)uridine (see paper)
53% identity, 99% coverage: 2:586/592 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 (= H453), E472 (= E487), V473 (≠ L488), G474 (= G489), G475 (= G490), G476 (= G491), R479 (= R494), I521 (≠ L536), A522 (= A537), G524 (= G539)
6hhvA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)n3-methyluridine (see paper)
53% identity, 99% coverage: 2:586/592 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 (= H453), E472 (= E487), V473 (≠ L488), G474 (= G489), G475 (= G490), G476 (= G491), R479 (= R494), I521 (≠ L536), A522 (= A537), G524 (= G539), R527 (= R542)
7ap4A Thermus thermophilus aspartyl-tRNA synthetase in complex with compound asps7hmdda (see paper)
53% identity, 99% coverage: 2:586/592 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 (= E487), G473 (= G489), G474 (= G490), G475 (= G491), R478 (= R494), I520 (≠ L536), A521 (= A537), G523 (= G539)
4o2dB Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
43% identity, 98% coverage: 1:583/592 of query aligns to 2:511/515 of 4o2dB
- active site: R216 (= R220), E218 (= E222), R222 (= R228), Q223 (= Q229), E415 (= E487), G418 (= G490), R470 (= R542)
- binding aspartic acid: E170 (= E174), S192 (= S196), Q194 (= Q198), Q228 (= Q234), H382 (≠ I397), G418 (= G490), R422 (= R494), I464 (≠ L536), A465 (= A537)
Q6PI48 Aspartate--tRNA ligase, mitochondrial; Aspartyl-tRNA synthetase; AspRS; EC 6.1.1.12 from Homo sapiens (Human) (see 2 papers)
41% identity, 99% coverage: 1:588/592 of query aligns to 49:633/645 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 (= Q138) to K: in LBSL; Significant impairment of its mitochondrial matrix localization; dbSNP:rs1469160736
- R263 (= R217) to Q: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918207
- G338 (≠ P293) mutation to E: No effect on its mitochondria localization.
- L613 (= L568) to F: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918212
- L626 (= L581) 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)
35% identity, 48% coverage: 2:284/592 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, 48% coverage: 2:284/592 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_012969945.1 NCBI__GCF_000025485.1:WP_012969945.1
MRTQYCGDLNSQHTGQEVVLCGWVQRRRDHGGVIFIDLRDREGLVQVVFDPDRAEVFARA
EQVRSEYVLKITGRVRPRPEGTINPDLSTGEIEILGLDLEILNAAETPPIQLDSHAADAS
EELRLRYRYLDLRRPEMQARLRTRSRVTQAMRRFLDERGFLDIETPILTKSTPEGARDYL
VPSRTHPGEFFALPQSPQLFKQLLMMSGLDRYYQIARCFRDEDLRADRQPEFTQLDIEVS
FMSEDELMGLMEGMIRSLFSEVIGVELPDPFPRLTYAEAMRRFGSDRPDLRVPLELIDVA
DLMDGVDFQVFAGPAKDPEGRVVALRLPKGGELSRKEIDGYTQFVGIYGAKGLAYIKVNE
WAAKGREGLQSPILKFLPDATVEGIMARTGAVDGDLIFFGADKARVVNESIGALRVKLGQ
DRGLLEGEWRPLWVVDFPMFEHDPANGRWVALHHPFTAPKDEHLGLLESDPGACLSRAYD
MVLNGTELGGGSIRIHRDAVQRQVFKLLNISDEQAEERFGFLLKALRFGCPPHGGLAFGL
DRLVMLMTGAGSIRDVMAFPKTQTAACLLTDAPSTVDEAQLKELSLRLRTRA
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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