SitesBLAST
Comparing WP_011651287.1 NCBI__GCF_000009265.1:WP_011651287.1 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)
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)
41% identity, 98% coverage: 5:588/596 of query aligns to 2:574/577 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 (≠ M89) mutation to M: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by reducing enzyme's ability to misacylate tRNA(Asn).
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)
43% identity, 98% coverage: 5:588/596 of query aligns to 3:583/591 of Q51422
- H31 (= H33) 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 (≠ D83) 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)
43% identity, 98% coverage: 5:588/596 of query aligns to 2:582/585 of 4wj4A
- active site: R219 (= R221), E221 (= E223), R227 (= R229), Q228 (≠ L230), E482 (= E488), G485 (≠ S491), R537 (= R543)
- binding aspartic acid: S195 (≠ A197), Q197 (= Q199), H450 (≠ N455), R489 (= R495), L531 (≠ A537)
- binding : R26 (= R29), R28 (= R31), D29 (= D32), H30 (= H33), G31 (= G34), G32 (= G35), V33 (= V36), F35 (= F38), Q46 (= Q49), R64 (= R66), R76 (≠ K78), P79 (≠ T81), A82 (≠ T84), N84 (= N86), E93 (= E95), T107 (≠ E109), P109 (= P111), D113 (≠ F115), E114 (≠ G116), D117 (= D119), E121 (≠ D123), A175 (= A177), E221 (= E223), D222 (= D224), R224 (= R226), A225 (= A227), R227 (= R229), Y346 (≠ T350), A447 (≠ F452), H449 (= H454), H450 (≠ N455), R549 (= R555), T557 (≠ N563), Q558 (= Q564), S559 (≠ Q565)
4wj3M Crystal structure of the asparagine transamidosome from pseudomonas aeruginosa (see paper)
43% identity, 98% coverage: 5:588/596 of query aligns to 2:582/589 of 4wj3M
- active site: R219 (= R221), E221 (= E223), R227 (= R229), Q228 (≠ L230), E482 (= E488), G485 (≠ S491), R537 (= R543)
- binding : R28 (= R31), D29 (= D32), H30 (= H33), G32 (= G35), V33 (= V36), F35 (= F38), Q46 (= Q49), R64 (= R66), R76 (≠ K78), R78 (= R80), A82 (≠ T84), N84 (= N86), E93 (= E95), T107 (≠ E109), D113 (≠ F115), V118 (≠ Y120)
1c0aA Crystal structure of the e. Coli aspartyl-tRNA synthetase : trnaasp : aspartyl-adenylate complex (see paper)
41% identity, 98% coverage: 5:590/596 of query aligns to 2:584/585 of 1c0aA
- active site: E482 (= E488), G485 (≠ S491), R537 (= R543)
- binding aspartyl-adenosine-5'-monophosphate: S193 (≠ A197), Q195 (= Q199), K198 (= K202), R217 (= R221), Q226 (≠ L230), F229 (= F234), Q231 (= Q236), H448 (= H454), E482 (= E488), V483 (≠ I489), G484 (≠ A490), G485 (≠ S491), G486 (= G492), R489 (= R495), L531 (≠ A537), A532 (= A538), G534 (= G540), R537 (= R543)
- binding adenosine monophosphate: F304 (= F311), V306 (= V313), K347 (≠ P353), G348 (= G354), A350 (≠ G356)
- binding : R26 (= R29), R28 (= R31), D29 (= D32), L30 (≠ H33), G31 (= G34), S32 (≠ G35), L33 (≠ V36), F35 (= F38), Q46 (= Q49), F48 (≠ V51), D50 (= D53), P51 (= P54), R64 (= R66), R76 (≠ K78), R78 (= R80), N82 (≠ T84), N84 (= N86), M87 (= M89), E93 (= E95), P109 (= P111), D111 (≠ P113), N113 (≠ E117), H114 (≠ P118), N116 (≠ Y120), T117 (≠ P121), E119 (≠ D123), T169 (≠ S173), P170 (= P174), E171 (= E175), G172 (= G176), A173 (= A177), S193 (≠ A197), R217 (= R221), E219 (= E223), D220 (= D224), R222 (= R226), A223 (= A227), R225 (= R229), I343 (≠ S349), H448 (= H454), H449 (≠ N455), F514 (= F520), R549 (= R555), T557 (≠ N563), T558 (≠ Q564), A559 (≠ Q565)
4rmfA Biochemical and structural characterization of mycobacterial aspartyl- tRNA synthetase asps, a promising tb drug target (see paper)
41% identity, 97% coverage: 5:584/596 of query aligns to 2:577/579 of 4rmfA
- active site: R215 (= R221), E217 (= E223), R223 (= R229), Q224 (≠ L230), E481 (= E488), G484 (≠ S491), R536 (= R543)
- binding 2,2-bis(hydroxymethyl)propane-1,3-diol: H447 (= H454), D474 (= D481), E481 (= E488)
1g51B Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
43% identity, 99% coverage: 5:592/596 of query aligns to 3:580/580 of 1g51B
- active site: R223 (= R221), E225 (= E223), R231 (= R229), Q232 (≠ L230), E476 (= E488), G479 (≠ S491), R531 (= R543)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E175), S199 (≠ A197), Q201 (= Q199), K204 (= K202), R223 (= R221), Q232 (≠ L230), F235 (= F234), Q237 (= Q236), H442 (= H454), E476 (= E488), G478 (≠ A490), G479 (≠ S491), G480 (= G492), R483 (= R495), I525 (≠ A537), A526 (= A538), G528 (= G540), R531 (= R543)
- binding adenosine monophosphate: V313 (= V313), Q347 (≠ P353), G348 (= G354), L349 (= L355), A350 (≠ G356), V389 (= V400), A390 (= A401)
1g51A Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
43% identity, 99% coverage: 5:592/596 of query aligns to 3:580/580 of 1g51A
- active site: R223 (= R221), E225 (= E223), R231 (= R229), Q232 (≠ L230), E476 (= E488), G479 (≠ S491), R531 (= R543)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E175), Q201 (= Q199), K204 (= K202), R223 (= R221), R231 (= R229), Q232 (≠ L230), F235 (= F234), Q237 (= Q236), H442 (= H454), H443 (≠ N455), E476 (= E488), G478 (≠ A490), G479 (≠ S491), G480 (= G492), R483 (= R495), I525 (≠ A537), A526 (= A538), G528 (= G540), R531 (= R543)
1efwA Crystal structure of aspartyl-tRNA synthetase from thermus thermophilus complexed to trnaasp from escherichia coli (see paper)
43% identity, 99% coverage: 5:592/596 of query aligns to 3:580/580 of 1efwA
- active site: R223 (= R221), E225 (= E223), R231 (= R229), Q232 (≠ L230), E476 (= E488), G479 (≠ S491), R531 (= R543)
- binding : R27 (= R29), R29 (= R31), D30 (= D32), L31 (≠ H33), G32 (= G34), G33 (= G35), L34 (≠ V36), F36 (= F38), Q47 (= Q49), H51 (≠ D53), P52 (= P54), R64 (= R66), R78 (= R80), E80 (= E82), N82 (= N86), R84 (≠ T88), E91 (= E95), T105 (≠ E109), P107 (= P111), E125 (≠ D123), R343 (≠ S349)
6sjcB Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)adenosine (see paper)
43% identity, 99% coverage: 5:592/596 of query aligns to 4:581/581 of 6sjcB
- binding 5'-O-(L-alpha-aspartylsulfamoyl)adenosine: E178 (= E175), Q202 (= Q199), K205 (= K202), R224 (= R221), R232 (= R229), Q233 (≠ L230), F236 (= F234), Q238 (= Q236), E477 (= E488), V478 (≠ I489), G479 (≠ A490), G480 (≠ S491), G481 (= G492), R484 (= R495), I526 (≠ A537), A527 (= A538), G529 (= G540), R532 (= R543)
5w25A Crystal structure of aspartyl-tRNA synthetase from mycobacterium tuberculosis complexed with l-aspartic acid
41% identity, 97% coverage: 5:584/596 of query aligns to 4:582/583 of 5w25A
- active site: R220 (= R221), E222 (= E223), R228 (= R229), Q229 (≠ L230), E486 (= E488), G489 (≠ S491), R541 (= R543)
- binding aspartic acid: E174 (= E175), Q198 (= Q199), R220 (= R221), H452 (= H454), H453 (≠ N455), G489 (≠ S491), R493 (= R495)
- binding lysine: D159 (≠ G160), R211 (= R212)
4o2dA Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
40% identity, 98% coverage: 5:587/596 of query aligns to 3:579/580 of 4o2dA
- active site: R216 (= R221), E218 (= E223), R222 (= R229), Q223 (≠ L230), E480 (= E488), G483 (≠ S491), R535 (= R543)
- binding aspartic acid: E170 (= E175), S192 (≠ A197), Q194 (= Q199), Q228 (= Q236), H446 (= H454), H447 (≠ N455), G483 (≠ S491), R487 (= R495), I529 (≠ A537), A530 (= A538)
6hhxA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)cytidine (see paper)
43% identity, 98% coverage: 5:587/596 of query aligns to 4:571/574 of 6hhxA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)cytidine: Q202 (= Q199), K205 (= K202), R224 (= R221), F236 (= F234), Q238 (= Q236), H438 (= H454), E472 (= E488), V473 (≠ I489), G474 (≠ A490), G475 (≠ S491), G476 (= G492), R479 (= R495), I521 (≠ A537), A522 (= A538), G524 (= G540)
6hhwA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)uridine (see paper)
43% identity, 98% coverage: 5:587/596 of query aligns to 4:571/574 of 6hhwA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)uridine: Q202 (= Q199), K205 (= K202), R224 (= R221), F236 (= F234), Q238 (= Q236), H438 (= H454), E472 (= E488), V473 (≠ I489), G474 (≠ A490), G475 (≠ S491), G476 (= G492), R479 (= R495), I521 (≠ A537), A522 (= A538), G524 (= G540)
6hhvA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)n3-methyluridine (see paper)
43% identity, 98% coverage: 5:587/596 of query aligns to 4:571/574 of 6hhvA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)N3-methyluridine: Q202 (= Q199), R224 (= R221), F236 (= F234), Q238 (= Q236), H438 (= H454), E472 (= E488), V473 (≠ I489), G474 (≠ A490), G475 (≠ S491), G476 (= G492), R479 (= R495), I521 (≠ A537), A522 (= A538), G524 (= G540), R527 (= R543)
7ap4A Thermus thermophilus aspartyl-tRNA synthetase in complex with compound asps7hmdda (see paper)
43% identity, 98% coverage: 5:587/596 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 (= Q199), R222 (= R221), R230 (= R229), Q231 (≠ L230), F234 (= F234), Q236 (= Q236), E471 (= E488), G473 (≠ A490), G474 (≠ S491), G475 (= G492), R478 (= R495), I520 (≠ A537), A521 (= A538), G523 (= G540)
Q6PI48 Aspartate--tRNA ligase, mitochondrial; Aspartyl-tRNA synthetase; AspRS; EC 6.1.1.12 from Homo sapiens (Human) (see 2 papers)
34% identity, 99% coverage: 5:593/596 of query aligns to 50:637/645 of Q6PI48
- R58 (= R13) mutation to G: No effect on its mitochondria localization.
- T136 (= T91) mutation to S: No effect on its mitochondria localization.
- Q184 (≠ H139) to K: in LBSL; Significant impairment of its mitochondrial matrix localization; dbSNP:rs1469160736
- R263 (≠ P218) to Q: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918207
- G338 (≠ P296) mutation to E: No effect on its mitochondria localization.
- L613 (= L569) to F: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918212
- L626 (= L582) 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)
46% identity, 56% coverage: 5:339/596 of query aligns to 3:327/515 of 4o2dB
Sites not aligning to the query:
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
33% identity, 41% coverage: 4:248/596 of query aligns to 2:241/438 of 3nemB
Sites not aligning to the query:
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
33% identity, 41% coverage: 4:248/596 of query aligns to 2:241/438 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_011651287.1 NCBI__GCF_000009265.1:WP_011651287.1
MHRYRSHTCAALRKSDVGSTVRISGWVHRVRDHGGVLFIDLRDHYGITQVVADPDSPAFQ
MAETVRGEWVIRIDGLVKARTEDTVNKTMATGEIELYAQEIEVLSAAKELPLPVFGEPDY
PEDVRLKYRFLDLRRETLHRNIVKRTQVISAMRREMGNVGFTEYTTPILTASSPEGARDF
LVPSRIHPGTFYALPQAPQQYKQLLMVAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLE
MSFVTQEDVWNTMGPLMTSIFEEFAEGKPVTKEWPRIPYDEAIRKYGSDKPDLRNPIVMQ
AVTEHFAGSGFKVFAGMIASNPKVEIWAIPAKTGGSRAFCDRMNAWAQSTGQPGLGYIFW
RKEGDKLEGAGPLAKNIGEERTDAIRTQLGLDDGDACFFVAGDPAKFYKFAGEARTKAGE
ELNLVDRDRFELCWIVDFPFFEWSEEDKKVDFAHNPFSMPQGGLDALQNQDPLTIKAFQY
DAVCNGFEIASGSIRNQSPETMVAAFEKVGLSQQDVEDRFGGLYRAFQYGAPPHGGAAFG
IDRIVMLLVGAKNLREISLFPMNQQAQDLLMGAPSPAAPTQLRELSIRPIPPVKKD
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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