SitesBLAST
Comparing BWI76_RS18170 FitnessBrowser__Koxy:BWI76_RS18170 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)
1c0aA Crystal structure of the e. Coli aspartyl-tRNA synthetase : trnaasp : aspartyl-adenylate complex (see paper)
94% identity, 98% coverage: 1:584/595 of query aligns to 1:584/585 of 1c0aA
- active site: E482 (= E482), G485 (= G485), R537 (= R537)
- binding aspartyl-adenosine-5'-monophosphate: S193 (= S193), Q195 (= Q195), K198 (= K198), R217 (= R217), Q226 (= Q226), F229 (= F229), Q231 (= Q231), H448 (= H448), E482 (= E482), V483 (= V483), G484 (= G484), G485 (= G485), G486 (= G486), R489 (= R489), L531 (= L531), A532 (= A532), G534 (= G534), R537 (= R537)
- binding adenosine monophosphate: F304 (= F304), V306 (= V306), K347 (= K347), G348 (= G348), A350 (= A350)
- binding : R26 (= R26), R28 (= R28), D29 (= D29), L30 (= L30), G31 (= G31), S32 (= S32), L33 (= L33), F35 (= F35), Q46 (= Q46), F48 (= F48), D50 (= D50), P51 (= P51), R64 (= R64), R76 (= R76), R78 (= R78), N82 (= N82), N84 (= N84), M87 (= M87), E93 (= E93), P109 (= P109), D111 (= D111), N113 (= N113), H114 (= H114), N116 (= N116), T117 (= T117), E119 (= E119), T169 (= T169), P170 (= P170), E171 (= E171), G172 (= G172), A173 (= A173), S193 (= S193), R217 (= R217), E219 (= E219), D220 (= D220), R222 (= R222), A223 (= A223), R225 (= R225), I343 (= I343), H448 (= H448), H449 (= H449), F514 (= F514), R549 (= R549), T557 (= T557), T558 (= T558), A559 (= A559)
4wj3M Crystal structure of the asparagine transamidosome from pseudomonas aeruginosa (see paper)
63% identity, 98% coverage: 1:583/595 of query aligns to 1:583/589 of 4wj3M
- active site: R219 (= R217), E221 (= E219), R227 (= R225), Q228 (= Q226), E482 (= E482), G485 (= G485), R537 (= R537)
- binding : R28 (= R28), D29 (= D29), H30 (≠ L30), G32 (≠ S32), V33 (≠ L33), F35 (= F35), Q46 (= Q46), R64 (= R64), R76 (= R76), R78 (= R78), A82 (≠ N82), N84 (= N84), E93 (= E93), T107 (≠ A107), D113 (= D111), V118 (≠ N116)
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)
63% identity, 98% coverage: 1:583/595 of query aligns to 2:584/591 of Q51422
- H31 (≠ L30) 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 (≠ K81) 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)
63% identity, 98% coverage: 1:583/595 of query aligns to 1:583/585 of 4wj4A
- active site: R219 (= R217), E221 (= E219), R227 (= R225), Q228 (= Q226), E482 (= E482), G485 (= G485), R537 (= R537)
- binding aspartic acid: S195 (= S193), Q197 (= Q195), H450 (= H449), R489 (= R489), L531 (= L531)
- binding : R26 (= R26), R28 (= R28), D29 (= D29), H30 (≠ L30), G31 (= G31), G32 (≠ S32), V33 (≠ L33), F35 (= F35), Q46 (= Q46), R64 (= R64), R76 (= R76), P79 (≠ D79), A82 (≠ N82), N84 (= N84), E93 (= E93), T107 (≠ A107), P109 (vs. gap), D113 (= D111), E114 (≠ S112), D117 (≠ V115), E121 (= E119), A175 (= A173), E221 (= E219), D222 (= D220), R224 (= R222), A225 (= A223), R227 (= R225), Y346 (= Y344), A447 (= A446), H449 (= H448), H450 (= H449), R549 (= R549), T557 (= T557), Q558 (≠ T558), S559 (≠ A559)
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, 98% coverage: 1:583/595 of query aligns to 1:575/577 of P56459
- L81 (≠ N82) 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).
4rmfA Biochemical and structural characterization of mycobacterial aspartyl- tRNA synthetase asps, a promising tb drug target (see paper)
48% identity, 97% coverage: 1:580/595 of query aligns to 1:579/579 of 4rmfA
- active site: R215 (= R217), E217 (= E219), R223 (= R225), Q224 (= Q226), E481 (= E482), G484 (= G485), R536 (= R537)
- binding 2,2-bis(hydroxymethyl)propane-1,3-diol: H447 (= H448), D474 (= D475), E481 (= E482)
4o2dA Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
48% identity, 98% coverage: 1:581/595 of query aligns to 2:579/580 of 4o2dA
- active site: R216 (= R217), E218 (= E219), R222 (= R225), Q223 (= Q226), E480 (= E482), G483 (= G485), R535 (= R537)
- binding aspartic acid: E170 (= E171), S192 (= S193), Q194 (= Q195), Q228 (= Q231), H446 (= H448), H447 (= H449), G483 (= G485), R487 (= R489), I529 (≠ L531), A530 (= A532)
5w25A Crystal structure of aspartyl-tRNA synthetase from mycobacterium tuberculosis complexed with l-aspartic acid
46% identity, 96% coverage: 1:569/595 of query aligns to 3:573/583 of 5w25A
- active site: R220 (= R217), E222 (= E219), R228 (= R225), Q229 (= Q226), E486 (= E482), G489 (= G485), R541 (= R537)
- binding aspartic acid: E174 (= E171), Q198 (= Q195), R220 (= R217), H452 (= H448), H453 (= H449), G489 (= G485), R493 (= R489)
- binding lysine: D159 (≠ G156), R211 (= R208)
6sjcB Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)adenosine (see paper)
49% identity, 98% coverage: 2:584/595 of query aligns to 4:579/581 of 6sjcB
- binding 5'-O-(L-alpha-aspartylsulfamoyl)adenosine: E178 (= E171), Q202 (= Q195), K205 (= K198), R224 (= R217), R232 (= R225), Q233 (= Q226), F236 (= F229), Q238 (= Q231), E477 (= E482), V478 (= V483), G479 (= G484), G480 (= G485), G481 (= G486), R484 (= R489), I526 (≠ L531), A527 (= A532), G529 (= G534), R532 (= R537)
1g51B Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
49% identity, 98% coverage: 2:584/595 of query aligns to 3:578/580 of 1g51B
- active site: R223 (= R217), E225 (= E219), R231 (= R225), Q232 (= Q226), E476 (= E482), G479 (= G485), R531 (= R537)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E171), S199 (= S193), Q201 (= Q195), K204 (= K198), R223 (= R217), Q232 (= Q226), F235 (= F229), Q237 (= Q231), H442 (= H448), E476 (= E482), G478 (= G484), G479 (= G485), G480 (= G486), R483 (= R489), I525 (≠ L531), A526 (= A532), G528 (= G534), R531 (= R537)
- binding adenosine monophosphate: V313 (= V306), Q347 (≠ K347), G348 (= G348), L349 (= L349), A350 (= A350), V389 (≠ G395), A390 (= A396)
1g51A Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
49% identity, 98% coverage: 2:584/595 of query aligns to 3:578/580 of 1g51A
- active site: R223 (= R217), E225 (= E219), R231 (= R225), Q232 (= Q226), E476 (= E482), G479 (= G485), R531 (= R537)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E171), Q201 (= Q195), K204 (= K198), R223 (= R217), R231 (= R225), Q232 (= Q226), F235 (= F229), Q237 (= Q231), H442 (= H448), H443 (= H449), E476 (= E482), G478 (= G484), G479 (= G485), G480 (= G486), R483 (= R489), I525 (≠ L531), A526 (= A532), G528 (= G534), R531 (= R537)
1efwA Crystal structure of aspartyl-tRNA synthetase from thermus thermophilus complexed to trnaasp from escherichia coli (see paper)
49% identity, 98% coverage: 2:584/595 of query aligns to 3:578/580 of 1efwA
- active site: R223 (= R217), E225 (= E219), R231 (= R225), Q232 (= Q226), E476 (= E482), G479 (= G485), R531 (= R537)
- binding : R27 (= R26), R29 (= R28), D30 (= D29), L31 (= L30), G32 (= G31), G33 (≠ S32), L34 (= L33), F36 (= F35), Q47 (= Q46), H51 (≠ D50), P52 (= P51), R64 (= R64), R78 (= R78), E80 (= E80), N82 (= N82), R84 (≠ D86), E91 (= E93), T105 (≠ A107), P107 (vs. gap), E125 (vs. gap), R343 (≠ I343)
6hhxA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)cytidine (see paper)
49% identity, 98% coverage: 2:584/595 of query aligns to 4:574/574 of 6hhxA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)cytidine: Q202 (= Q195), K205 (= K198), R224 (= R217), F236 (= F229), Q238 (= Q231), H438 (= H448), E472 (= E482), V473 (= V483), G474 (= G484), G475 (= G485), G476 (= G486), R479 (= R489), I521 (≠ L531), A522 (= A532), G524 (= G534)
6hhwA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)uridine (see paper)
49% identity, 98% coverage: 2:584/595 of query aligns to 4:574/574 of 6hhwA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)uridine: Q202 (= Q195), K205 (= K198), R224 (= R217), F236 (= F229), Q238 (= Q231), H438 (= H448), E472 (= E482), V473 (= V483), G474 (= G484), G475 (= G485), G476 (= G486), R479 (= R489), I521 (≠ L531), A522 (= A532), G524 (= G534)
6hhvA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)n3-methyluridine (see paper)
49% identity, 98% coverage: 2:584/595 of query aligns to 4:574/574 of 6hhvA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)N3-methyluridine: Q202 (= Q195), R224 (= R217), F236 (= F229), Q238 (= Q231), H438 (= H448), E472 (= E482), V473 (= V483), G474 (= G484), G475 (= G485), G476 (= G486), R479 (= R489), I521 (≠ L531), A522 (= A532), G524 (= G534), R527 (= R537)
7ap4A Thermus thermophilus aspartyl-tRNA synthetase in complex with compound asps7hmdda (see paper)
49% identity, 98% coverage: 2:584/595 of query aligns to 4:573/573 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 (= Q195), R222 (= R217), R230 (= R225), Q231 (= Q226), F234 (= F229), Q236 (= Q231), E471 (= E482), G473 (= G484), G474 (= G485), G475 (= G486), R478 (= R489), I520 (≠ L531), A521 (= A532), G523 (= G534)
Q6PI48 Aspartate--tRNA ligase, mitochondrial; Aspartyl-tRNA synthetase; AspRS; EC 6.1.1.12 from Homo sapiens (Human) (see 2 papers)
40% identity, 98% coverage: 1:583/595 of query aligns to 49:633/645 of Q6PI48
- R58 (= R10) mutation to G: No effect on its mitochondria localization.
- T136 (= T89) mutation to S: No effect on its mitochondria localization.
- Q184 (≠ A135) to K: in LBSL; Significant impairment of its mitochondrial matrix localization; dbSNP:rs1469160736
- R263 (≠ K214) to Q: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918207
- G338 (≠ P289) mutation to E: No effect on its mitochondria localization.
- L613 (= L563) to F: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918212
- L626 (= L576) 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, 54% coverage: 1:323/595 of query aligns to 2:333/515 of 4o2dB
Sites not aligning to the query:
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
35% identity, 46% coverage: 2:272/595 of query aligns to 3:271/438 of 3nemB
Sites not aligning to the query:
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
35% identity, 46% coverage: 2:272/595 of query aligns to 3:271/438 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
>BWI76_RS18170 FitnessBrowser__Koxy:BWI76_RS18170
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLA
SELRNEFCIQVTGTVRARDEKNVNSDMATGAIEVLASDLTIINRAEALPLDSNHVNTEEA
RLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPS
RVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMT
AEQVREVMEALVRNLWQEVKGVDLGDFPIMTFAEAERRYGSDKPDLRNPMELVDVADLVK
AVEFAVFAGPANDAKGRVAALRVPGGAALTRKQIDEYGKFVQIYGAKGLAYIKVTERAKG
LEGINSPVAKFLNADIVEAILERTGAQDGDMIFFGADNKKVVADALGALRLKLGKDLNLT
DENKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMSAAELKAAPEDAVANAYDMVING
YEVGGGSVRIHSGEMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTM
LLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPASLSELGIQVVAKEAKESLENK
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