SitesBLAST
Comparing WP_013010726.1 NCBI__GCF_000025725.1:WP_013010726.1 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)
1g51B Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
50% identity, 97% coverage: 9:586/596 of query aligns to 2:573/580 of 1g51B
- active site: R223 (= R228), E225 (= E230), R231 (= R236), Q232 (= Q237), E476 (= E489), G479 (= G492), R531 (= R544)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E182), S199 (= S204), Q201 (= Q206), K204 (= K209), R223 (= R228), Q232 (= Q237), F235 (= F240), Q237 (= Q242), H442 (= H455), E476 (= E489), G478 (= G491), G479 (= G492), G480 (= G493), R483 (= R496), I525 (= I538), A526 (= A539), G528 (= G541), R531 (= R544)
- binding adenosine monophosphate: V313 (= V318), Q347 (≠ G359), G348 (= G360), L349 (= L361), A350 (= A362), V389 (≠ G401), A390 (= A402)
1g51A Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
50% identity, 97% coverage: 9:586/596 of query aligns to 2:573/580 of 1g51A
- active site: R223 (= R228), E225 (= E230), R231 (= R236), Q232 (= Q237), E476 (= E489), G479 (= G492), R531 (= R544)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E182), Q201 (= Q206), K204 (= K209), R223 (= R228), R231 (= R236), Q232 (= Q237), F235 (= F240), Q237 (= Q242), H442 (= H455), H443 (= H456), E476 (= E489), G478 (= G491), G479 (= G492), G480 (= G493), R483 (= R496), I525 (= I538), A526 (= A539), G528 (= G541), R531 (= R544)
1efwA Crystal structure of aspartyl-tRNA synthetase from thermus thermophilus complexed to trnaasp from escherichia coli (see paper)
50% identity, 97% coverage: 9:586/596 of query aligns to 2:573/580 of 1efwA
- active site: R223 (= R228), E225 (= E230), R231 (= R236), Q232 (= Q237), E476 (= E489), G479 (= G492), R531 (= R544)
- binding : R27 (= R34), R29 (= R36), D30 (= D37), L31 (≠ H38), G32 (= G39), G33 (= G40), L34 (≠ V41), F36 (= F43), Q47 (= Q54), H51 (≠ S58), P52 (= P59), R64 (= R73), R78 (= R87), E80 (= E89), N82 (= N93), R84 (≠ K95), E91 (= E102), T105 (= T116), P107 (= P118), E125 (≠ D130), R343 (≠ S355)
6sjcB Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)adenosine (see paper)
50% identity, 97% coverage: 9:586/596 of query aligns to 3:574/581 of 6sjcB
- binding 5'-O-(L-alpha-aspartylsulfamoyl)adenosine: E178 (= E182), Q202 (= Q206), K205 (= K209), R224 (= R228), R232 (= R236), Q233 (= Q237), F236 (= F240), Q238 (= Q242), E477 (= E489), V478 (≠ I490), G479 (= G491), G480 (= G492), G481 (= G493), R484 (= R496), I526 (= I538), A527 (= A539), G529 (= G541), R532 (= R544)
4wj3M Crystal structure of the asparagine transamidosome from pseudomonas aeruginosa (see paper)
49% identity, 97% coverage: 10:590/596 of query aligns to 2:583/589 of 4wj3M
- active site: R219 (= R228), E221 (= E230), R227 (= R236), Q228 (= Q237), E482 (= E489), G485 (= G492), R537 (= R544)
- binding : R28 (= R36), D29 (= D37), H30 (= H38), G32 (= G40), V33 (= V41), F35 (= F43), Q46 (= Q54), R64 (= R73), R76 (≠ G85), R78 (= R87), A82 (≠ T91), N84 (= N93), E93 (= E102), T107 (= T116), D113 (= D122), V118 (≠ A127)
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)
49% identity, 97% coverage: 10:590/596 of query aligns to 3:584/591 of Q51422
- H31 (= H38) 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 (= G90) 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)
49% identity, 97% coverage: 10:590/596 of query aligns to 2:583/585 of 4wj4A
- active site: R219 (= R228), E221 (= E230), R227 (= R236), Q228 (= Q237), E482 (= E489), G485 (= G492), R537 (= R544)
- binding aspartic acid: S195 (= S204), Q197 (= Q206), H450 (= H456), R489 (= R496), L531 (≠ I538)
- binding : R26 (= R34), R28 (= R36), D29 (= D37), H30 (= H38), G31 (= G39), G32 (= G40), V33 (= V41), F35 (= F43), Q46 (= Q54), R64 (= R73), R76 (≠ G85), P79 (= P88), A82 (≠ T91), N84 (= N93), E93 (= E102), T107 (= T116), P109 (= P118), D113 (= D122), E114 (≠ D123), D117 (≠ N126), E121 (≠ D130), A175 (= A184), E221 (= E230), D222 (= D231), R224 (= R233), A225 (= A234), R227 (= R236), Y346 (≠ L356), A447 (= A453), H449 (= H455), H450 (= H456), R549 (= R556), T557 (= T564), Q558 (= Q565), S559 (≠ K566)
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, 97% coverage: 10:590/596 of query aligns to 2:575/577 of P56459
- L81 (≠ T91) mutation to N: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by reducing enzyme's ability to misacylate tRNA(Asn).
- L86 (= L96) mutation to M: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by reducing enzyme's ability to misacylate tRNA(Asn).
6hhxA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)cytidine (see paper)
49% identity, 97% coverage: 9:586/596 of query aligns to 3:569/574 of 6hhxA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)cytidine: Q202 (= Q206), K205 (= K209), R224 (= R228), F236 (= F240), Q238 (= Q242), H438 (= H455), E472 (= E489), V473 (≠ I490), G474 (= G491), G475 (= G492), G476 (= G493), R479 (= R496), I521 (= I538), A522 (= A539), G524 (= G541)
6hhwA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)uridine (see paper)
49% identity, 97% coverage: 9:586/596 of query aligns to 3:569/574 of 6hhwA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)uridine: Q202 (= Q206), K205 (= K209), R224 (= R228), F236 (= F240), Q238 (= Q242), H438 (= H455), E472 (= E489), V473 (≠ I490), G474 (= G491), G475 (= G492), G476 (= G493), R479 (= R496), I521 (= I538), A522 (= A539), G524 (= G541)
6hhvA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)n3-methyluridine (see paper)
49% identity, 97% coverage: 9:586/596 of query aligns to 3:569/574 of 6hhvA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)N3-methyluridine: Q202 (= Q206), R224 (= R228), F236 (= F240), Q238 (= Q242), H438 (= H455), E472 (= E489), V473 (≠ I490), G474 (= G491), G475 (= G492), G476 (= G493), R479 (= R496), I521 (= I538), A522 (= A539), G524 (= G541), R527 (= R544)
7ap4A Thermus thermophilus aspartyl-tRNA synthetase in complex with compound asps7hmdda (see paper)
49% identity, 97% coverage: 9:586/596 of query aligns to 3:568/573 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 (= Q206), R222 (= R228), R230 (= R236), Q231 (= Q237), F234 (= F240), Q236 (= Q242), E471 (= E489), G473 (= G491), G474 (= G492), G475 (= G493), R478 (= R496), I520 (= I538), A521 (= A539), G523 (= G541)
1c0aA Crystal structure of the e. Coli aspartyl-tRNA synthetase : trnaasp : aspartyl-adenylate complex (see paper)
49% identity, 97% coverage: 10:589/596 of query aligns to 2:582/585 of 1c0aA
- active site: E482 (= E489), G485 (= G492), R537 (= R544)
- binding aspartyl-adenosine-5'-monophosphate: S193 (= S204), Q195 (= Q206), K198 (= K209), R217 (= R228), Q226 (= Q237), F229 (= F240), Q231 (= Q242), H448 (= H455), E482 (= E489), V483 (≠ I490), G484 (= G491), G485 (= G492), G486 (= G493), R489 (= R496), L531 (≠ I538), A532 (= A539), G534 (= G541), R537 (= R544)
- binding adenosine monophosphate: F304 (= F316), V306 (= V318), K347 (≠ G359), G348 (= G360), A350 (= A362)
- binding : R26 (= R34), R28 (= R36), D29 (= D37), L30 (≠ H38), G31 (= G39), S32 (≠ G40), L33 (≠ V41), F35 (= F43), Q46 (= Q54), F48 (≠ V56), D50 (≠ S58), P51 (= P59), R64 (= R73), R76 (≠ G85), R78 (= R87), N82 (≠ T91), N84 (= N93), M87 (≠ L96), E93 (= E102), P109 (= P118), D111 (= D122), N113 (≠ F124), H114 (≠ T125), N116 (≠ A127), T117 (≠ N128), E119 (≠ D130), T169 (= T180), P170 (= P181), E171 (= E182), G172 (= G183), A173 (= A184), S193 (= S204), R217 (= R228), E219 (= E230), D220 (= D231), R222 (= R233), A223 (= A234), R225 (= R236), I343 (≠ S355), H448 (= H455), H449 (= H456), F514 (= F521), R549 (= R556), T557 (= T564), T558 (≠ Q565), A559 (≠ K566)
4rmfA Biochemical and structural characterization of mycobacterial aspartyl- tRNA synthetase asps, a promising tb drug target (see paper)
47% identity, 97% coverage: 10:585/596 of query aligns to 2:577/579 of 4rmfA
- active site: R215 (= R228), E217 (= E230), R223 (= R236), Q224 (= Q237), E481 (= E489), G484 (= G492), R536 (= R544)
- binding 2,2-bis(hydroxymethyl)propane-1,3-diol: H447 (= H455), D474 (= D482), E481 (= E489)
4o2dA Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
47% identity, 97% coverage: 10:585/596 of query aligns to 3:576/580 of 4o2dA
- active site: R216 (= R228), E218 (= E230), R222 (= R236), Q223 (= Q237), E480 (= E489), G483 (= G492), R535 (= R544)
- binding aspartic acid: E170 (= E182), S192 (= S204), Q194 (= Q206), Q228 (= Q242), H446 (= H455), H447 (= H456), G483 (= G492), R487 (= R496), I529 (= I538), A530 (= A539)
5w25A Crystal structure of aspartyl-tRNA synthetase from mycobacterium tuberculosis complexed with l-aspartic acid
45% identity, 97% coverage: 10:585/596 of query aligns to 4:582/583 of 5w25A
- active site: R220 (= R228), E222 (= E230), R228 (= R236), Q229 (= Q237), E486 (= E489), G489 (= G492), R541 (= R544)
- binding aspartic acid: E174 (= E182), Q198 (= Q206), R220 (= R228), H452 (= H455), H453 (= H456), G489 (= G492), R493 (= R496)
- binding lysine: D159 (= D167), R211 (≠ K219)
Q6PI48 Aspartate--tRNA ligase, mitochondrial; Aspartyl-tRNA synthetase; AspRS; EC 6.1.1.12 from Homo sapiens (Human) (see 2 papers)
41% identity, 97% coverage: 10:589/596 of query aligns to 50:632/645 of Q6PI48
- R58 (≠ T18) mutation to G: No effect on its mitochondria localization.
- T136 (= T98) mutation to S: No effect on its mitochondria localization.
- Q184 (= Q146) to K: in LBSL; Significant impairment of its mitochondrial matrix localization; dbSNP:rs1469160736
- R263 (≠ K225) to Q: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918207
- G338 (≠ D301) mutation to E: No effect on its mitochondria localization.
- L613 (≠ M570) to F: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918212
- L626 (= L583) 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)
49% identity, 55% coverage: 10:337/596 of query aligns to 3:324/515 of 4o2dB
Sites not aligning to the query:
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
29% identity, 47% coverage: 10:292/596 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)
29% identity, 47% coverage: 10:292/596 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_013010726.1 NCBI__GCF_000025725.1:WP_013010726.1
MLSHMGDWRRSHNCVQLTAKNIGEEVCLMGWVQRRRDHGGVIFVDLRDREGLTQVVMSPE
YNKDVHAVADSIRNEFVIAVKGKVGMRPEGTINTKLPTGEIEVMVDELKILNASQTPPFM
IDDFTNANEDIRLKYRYLDLRRRKIQNNLITRHNIVRTMREYLYARDFLDIETPFLTKST
PEGARDYLVPSRVNPGKCYALPQSPQMFKQLLMVGGYDKYFQIVKCFRDEDLRADRQPEF
TQLDMEMSFIDREDLMELLEGMFIEIFQNIKGIKLERGFPRMSYDNAMEKYGHDAPDTRF
DMFLKTINELVADCGFKVFREVVADGGVVKAINAKGAGEKYSRKNIDELTELAVSLGAGG
LAYIKVNEDSLQSPIVKFLGDSADTIVKAMDGKPGDIIFFGAGKKDIVNLYMSKVRLKLG
KELGLIKEGDYSFVWVLDFPLLDYDAEEKRYVAMHHPFTAPLDEDIPLFDTDPGQMRAKA
YDLVLNGSEIGGGSIRIHRSDVQEKMFNALGFTPEEREYKFGFFIDALKYGTPPHGGIAF
GVDRIATILTGSDSIRDVIAFPKTQKATDMMSEAPSKIDEKQLKELYMKFEVVEND
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