SitesBLAST
Comparing 350400 FitnessBrowser__Btheta:350400 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)
49% identity, 99% coverage: 1:581/587 of query aligns to 1:577/580 of 1g51B
- active site: R223 (= R219), E225 (= E221), R231 (= R227), Q232 (= Q228), E476 (= E480), G479 (= G483), R531 (= R535)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E173), S199 (= S195), Q201 (= Q197), K204 (= K200), R223 (= R219), Q232 (= Q228), F235 (= F231), Q237 (= Q233), H442 (= H446), E476 (= E480), G478 (= G482), G479 (= G483), G480 (= G484), R483 (= R487), I525 (≠ L529), A526 (= A530), G528 (= G532), R531 (= R535)
- binding adenosine monophosphate: V313 (= V309), Q347 (≠ K347), G348 (= G348), L349 (≠ M349), A350 (≠ V350), V389 (≠ L391), A390 (≠ S392)
1g51A Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
49% identity, 99% coverage: 1:581/587 of query aligns to 1:577/580 of 1g51A
- active site: R223 (= R219), E225 (= E221), R231 (= R227), Q232 (= Q228), E476 (= E480), G479 (= G483), R531 (= R535)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E173), Q201 (= Q197), K204 (= K200), R223 (= R219), R231 (= R227), Q232 (= Q228), F235 (= F231), Q237 (= Q233), H442 (= H446), H443 (= H447), E476 (= E480), G478 (= G482), G479 (= G483), G480 (= G484), R483 (= R487), I525 (≠ L529), A526 (= A530), G528 (= G532), R531 (= R535)
1efwA Crystal structure of aspartyl-tRNA synthetase from thermus thermophilus complexed to trnaasp from escherichia coli (see paper)
49% identity, 99% coverage: 1:581/587 of query aligns to 1:577/580 of 1efwA
- active site: R223 (= R219), E225 (= E221), R231 (= R227), Q232 (= Q228), E476 (= E480), G479 (= G483), R531 (= R535)
- binding : R27 (= R27), R29 (= R29), D30 (≠ K30), L31 (≠ M31), G32 (= G32), G33 (= G33), L34 (≠ M34), F36 (= F36), Q47 (= Q47), H51 (≠ N51), P52 (≠ E52), R64 (≠ G66), R78 (= R80), E80 (≠ S82), N82 (= N84), R84 (≠ N86), E91 (= E93), T105 (= T107), P107 (= P109), E125 (vs. gap), R343 (≠ K341)
6sjcB Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)adenosine (see paper)
49% identity, 99% coverage: 1:581/587 of query aligns to 2:578/581 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 (= E480), V478 (= V481), G479 (= G482), G480 (= G483), G481 (= G484), R484 (= R487), I526 (≠ L529), A527 (= A530), G529 (= G532), R532 (= R535)
1c0aA Crystal structure of the e. Coli aspartyl-tRNA synthetase : trnaasp : aspartyl-adenylate complex (see paper)
48% identity, 99% coverage: 3:581/587 of query aligns to 2:583/585 of 1c0aA
- active site: E482 (= E480), G485 (= G483), R537 (= R535)
- binding aspartyl-adenosine-5'-monophosphate: S193 (= S195), Q195 (= Q197), K198 (= K200), R217 (= R219), Q226 (= Q228), F229 (= F231), Q231 (= Q233), H448 (= H446), E482 (= E480), V483 (= V481), G484 (= G482), G485 (= G483), G486 (= G484), R489 (= R487), L531 (= L529), A532 (= A530), G534 (= G532), R537 (= R535)
- binding adenosine monophosphate: F304 (= F307), V306 (= V309), K347 (= K347), G348 (= G348), A350 (≠ V350)
- binding : R26 (= R27), R28 (= R29), D29 (≠ K30), L30 (≠ M31), G31 (= G32), S32 (≠ G33), L33 (≠ M34), F35 (= F36), Q46 (= Q47), F48 (≠ V49), D50 (≠ N51), P51 (≠ E52), R64 (≠ G66), R76 (≠ N78), R78 (= R80), N82 (= N84), N84 (= N86), M87 (≠ I87), E93 (= E93), P109 (= P109), D111 (≠ E113), N113 (= N115), H114 (≠ T116), N116 (≠ G118), T117 (≠ G119), E119 (≠ D121), 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 (≠ K341), H448 (= H446), H449 (= H447), F514 (= F512), R549 (= R547), T557 (≠ N555), T558 (≠ N556), A559 (≠ S557)
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)
48% identity, 99% coverage: 1:579/587 of query aligns to 1:582/591 of Q51422
- H31 (≠ M31) 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 (≠ F81) 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.
4rmfA Biochemical and structural characterization of mycobacterial aspartyl- tRNA synthetase asps, a promising tb drug target (see paper)
47% identity, 98% coverage: 2:576/587 of query aligns to 1:577/579 of 4rmfA
- active site: R215 (= R219), E217 (= E221), R223 (= R227), Q224 (= Q228), E481 (= E480), G484 (= G483), R536 (= R535)
- binding 2,2-bis(hydroxymethyl)propane-1,3-diol: H447 (= H446), D474 (= D473), E481 (= E480)
4wj3M Crystal structure of the asparagine transamidosome from pseudomonas aeruginosa (see paper)
48% identity, 98% coverage: 3:579/587 of query aligns to 2:581/589 of 4wj3M
- active site: R219 (= R219), E221 (= E221), R227 (= R227), Q228 (= Q228), E482 (= E480), G485 (= G483), R537 (= R535)
- binding : R28 (= R29), D29 (≠ K30), H30 (≠ M31), G32 (= G33), V33 (≠ M34), F35 (= F36), Q46 (= Q47), R64 (≠ G66), R76 (≠ N78), R78 (= R80), A82 (≠ S82), N84 (= N84), E93 (= E93), T107 (= T107), D113 (≠ E113), V118 (≠ G118)
4wj4A Crystal structure of non-discriminating aspartyl-tRNA synthetase from pseudomonas aeruginosa complexed with tRNA(asn) and aspartic acid (see paper)
48% identity, 98% coverage: 3:579/587 of query aligns to 2:581/585 of 4wj4A
- active site: R219 (= R219), E221 (= E221), R227 (= R227), Q228 (= Q228), E482 (= E480), G485 (= G483), R537 (= R535)
- binding aspartic acid: S195 (= S195), Q197 (= Q197), H450 (= H447), R489 (= R487), L531 (= L529)
- binding : R26 (= R27), R28 (= R29), D29 (≠ K30), H30 (≠ M31), G31 (= G32), G32 (= G33), V33 (≠ M34), F35 (= F36), Q46 (= Q47), R64 (≠ G66), R76 (≠ N78), P79 (vs. gap), A82 (≠ S82), N84 (= N84), E93 (= E93), T107 (= T107), P109 (= P109), D113 (≠ E113), E114 (≠ D114), D117 (= D117), E121 (≠ D121), A175 (= A175), E221 (= E221), D222 (= D222), R224 (= R224), A225 (= A225), R227 (= R227), Y346 (≠ I344), A447 (= A444), H449 (= H446), H450 (= H447), R549 (= R547), T557 (≠ N555), Q558 (≠ N556), S559 (= S557)
6hhxA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)cytidine (see paper)
48% identity, 99% coverage: 1:581/587 of query aligns to 2:573/574 of 6hhxA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)cytidine: Q202 (= Q197), K205 (= K200), R224 (= R219), F236 (= F231), Q238 (= Q233), H438 (= H446), E472 (= E480), V473 (= V481), G474 (= G482), G475 (= G483), G476 (= G484), R479 (= R487), I521 (≠ L529), A522 (= A530), G524 (= G532)
6hhwA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)uridine (see paper)
48% identity, 99% coverage: 1:581/587 of query aligns to 2:573/574 of 6hhwA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)uridine: Q202 (= Q197), K205 (= K200), R224 (= R219), F236 (= F231), Q238 (= Q233), H438 (= H446), E472 (= E480), V473 (= V481), G474 (= G482), G475 (= G483), G476 (= G484), R479 (= R487), I521 (≠ L529), A522 (= A530), G524 (= G532)
6hhvA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)n3-methyluridine (see paper)
48% identity, 99% coverage: 1:581/587 of query aligns to 2:573/574 of 6hhvA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)N3-methyluridine: Q202 (= Q197), R224 (= R219), F236 (= F231), Q238 (= Q233), H438 (= H446), E472 (= E480), V473 (= V481), G474 (= G482), G475 (= G483), G476 (= G484), R479 (= R487), I521 (≠ L529), A522 (= A530), G524 (= G532), R527 (= R535)
4o2dA Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
46% identity, 99% coverage: 1:579/587 of query aligns to 1:579/580 of 4o2dA
- active site: R216 (= R219), E218 (= E221), R222 (= R227), Q223 (= Q228), E480 (= E480), G483 (= G483), R535 (= R535)
- binding aspartic acid: E170 (= E173), S192 (= S195), Q194 (= Q197), Q228 (= Q233), H446 (= H446), H447 (= H447), G483 (= G483), R487 (= R487), I529 (≠ L529), A530 (= A530)
5w25A Crystal structure of aspartyl-tRNA synthetase from mycobacterium tuberculosis complexed with l-aspartic acid
45% identity, 98% coverage: 1:576/587 of query aligns to 2:582/583 of 5w25A
- active site: R220 (= R219), E222 (= E221), R228 (= R227), Q229 (= Q228), E486 (= E480), G489 (= G483), R541 (= R535)
- binding aspartic acid: E174 (= E173), Q198 (= Q197), R220 (= R219), H452 (= H446), H453 (= H447), G489 (= G483), R493 (= R487)
- binding lysine: D159 (≠ G158), R211 (= R210)
7ap4A Thermus thermophilus aspartyl-tRNA synthetase in complex with compound asps7hmdda (see paper)
48% identity, 99% coverage: 1:581/587 of query aligns to 2:572/573 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 (= E480), G473 (= G482), G474 (= G483), G475 (= G484), R478 (= R487), I520 (≠ L529), A521 (= A530), G523 (= G532)
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)
44% identity, 98% coverage: 3:579/587 of query aligns to 2:573/577 of P56459
- L81 (vs. gap) mutation to N: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by reducing enzyme's ability to misacylate tRNA(Asn).
- L86 (≠ I87) mutation to M: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by reducing enzyme's ability to misacylate tRNA(Asn).
4o2dB Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
43% identity, 99% coverage: 1:579/587 of query aligns to 1:514/515 of 4o2dB
- active site: R216 (= R219), E218 (= E221), R222 (= R227), Q223 (= Q228), E415 (= E480), G418 (= G483), R470 (= R535)
- binding aspartic acid: E170 (= E173), S192 (= S195), Q194 (= Q197), Q228 (= Q233), H382 (= H447), G418 (= G483), R422 (= R487), I464 (≠ L529), A465 (= A530)
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: 1:582/587 of query aligns to 48:634/645 of Q6PI48
- R58 (= R11) mutation to G: No effect on its mitochondria localization.
- T136 (= T89) mutation to S: No effect on its mitochondria localization.
- Q184 (≠ R137) to K: in LBSL; Significant impairment of its mitochondrial matrix localization; dbSNP:rs1469160736
- R263 (≠ K216) to Q: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918207
- G338 (= G292) mutation to E: No effect on its mitochondria localization.
- L613 (≠ V561) to F: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918212
- L626 (= L574) 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)
31% identity, 50% coverage: 1:292/587 of query aligns to 1:302/438 of 3nemB
Sites not aligning to the query:
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
31% identity, 50% coverage: 1:292/587 of query aligns to 1:302/438 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
>350400 FitnessBrowser__Btheta:350400
MFRTHTCGELRISDVNKQITLSGWVQRSRKMGGMTFIDLRDRYGITQLVFNEEINAELCD
RANKLGREFVIQITGTVNERFSKNANIPTGDIEIIVSELNVLNTAMTPPFTIEDNTDGGD
DIRMKYRYLDLRRNAVRSNLELRHKMTIEVRKYLDSLGFIEVETPVLIGSTPEGARDFVV
PSRMNPGQFYALPQSPQTLKQLLMVSGFDRYFQIAKCFRDEDLRADRQPEFTQIDCEMSF
VEQEDIISTFEGMAKHLFKTLRGVELTEPFQRMPWADAMKYYGSDKPDLRFGMKFVELMD
IMKGHGFSVFDNAAYVGGICAEGAATYTRKQLDALTEFVKKPQIGAKGMVYARVEADGTV
KSSVDKFYTQEVLQQMKEAFGAKPGDLILILSGDDVMKTRKQLCELRLEMGSQLGLRDKN
KFVCLWVIDFPMFEWSEEEGRLMAMHHPFTHPKEEDIPLLDTDPAAVRADAYDMVVNGVE
VGGGSIRIHDAQLQARMFEILGFTPEKAQAQFGFLMNAFKYGAPPHGGLAYGLDRWVSLF
AGLDSIRDCIAFPKNNSGRDVMLDAPSEIDQTQLDELNLIVDIKENK
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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