SitesBLAST
Comparing CA265_RS19975 FitnessBrowser__Pedo557:CA265_RS19975 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)
1g51B Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
51% identity, 99% coverage: 1:577/581 of query aligns to 1:575/580 of 1g51B
- active site: R223 (= R219), E225 (= E221), R231 (= R227), Q232 (= Q228), E476 (= E478), G479 (= G481), R531 (= R533)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E173), S199 (= S195), Q201 (= Q197), K204 (= K200), R223 (= R219), Q232 (= Q228), F235 (= F231), Q237 (= Q233), H442 (= H444), E476 (= E478), G478 (= G480), G479 (= G481), G480 (= G482), R483 (= R485), I525 (= I527), A526 (= A528), G528 (= G530), R531 (= R533)
- binding adenosine monophosphate: V313 (= V308), Q347 (≠ T346), G348 (= G347), L349 (= L348), A350 (≠ I349), V389 (≠ L390), A390 (= A391)
1g51A Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
51% identity, 99% coverage: 1:577/581 of query aligns to 1:575/580 of 1g51A
- active site: R223 (= R219), E225 (= E221), R231 (= R227), Q232 (= Q228), E476 (= E478), G479 (= G481), R531 (= R533)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E173), Q201 (= Q197), K204 (= K200), R223 (= R219), R231 (= R227), Q232 (= Q228), F235 (= F231), Q237 (= Q233), H442 (= H444), H443 (= H445), E476 (= E478), G478 (= G480), G479 (= G481), G480 (= G482), R483 (= R485), I525 (= I527), A526 (= A528), G528 (= G530), R531 (= R533)
1efwA Crystal structure of aspartyl-tRNA synthetase from thermus thermophilus complexed to trnaasp from escherichia coli (see paper)
51% identity, 99% coverage: 1:577/581 of query aligns to 1:575/580 of 1efwA
- active site: R223 (= R219), E225 (= E221), R231 (= R227), Q232 (= Q228), E476 (= E478), G479 (= G481), R531 (= R533)
- binding : R27 (≠ K27), R29 (= R29), D30 (= D30), L31 (= L31), G32 (= G32), G33 (= G33), L34 (≠ M34), F36 (= F36), Q47 (= Q47), H51 (≠ N51), P52 (≠ D54), R64 (≠ G66), R78 (= R80), E80 (≠ N82), N82 (= N84), R84 (≠ K86), E91 (= E93), T105 (≠ L107), P107 (= P109), E125 (vs. gap), R343 (= R340)
6sjcB Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)adenosine (see paper)
51% identity, 99% coverage: 1:577/581 of query aligns to 2:576/581 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 (= E478), V478 (= V479), G479 (= G480), G480 (= G481), G481 (= G482), R484 (= R485), I526 (= I527), A527 (= A528), G529 (= G530), R532 (= R533)
1c0aA Crystal structure of the e. Coli aspartyl-tRNA synthetase : trnaasp : aspartyl-adenylate complex (see paper)
48% identity, 99% coverage: 2:579/581 of query aligns to 1:583/585 of 1c0aA
- active site: E482 (= E478), G485 (= G481), R537 (= R533)
- binding aspartyl-adenosine-5'-monophosphate: S193 (= S195), Q195 (= Q197), K198 (= K200), R217 (= R219), Q226 (= Q228), F229 (= F231), Q231 (= Q233), H448 (= H444), E482 (= E478), V483 (= V479), G484 (= G480), G485 (= G481), G486 (= G482), R489 (= R485), L531 (≠ I527), A532 (= A528), G534 (= G530), R537 (= R533)
- binding adenosine monophosphate: F304 (= F306), V306 (= V308), K347 (≠ T346), G348 (= G347), A350 (≠ I349)
- binding : R26 (≠ K27), R28 (= R29), D29 (= D30), L30 (= L31), G31 (= G32), S32 (≠ G33), L33 (≠ M34), F35 (= F36), Q46 (= Q47), F48 (≠ V49), D50 (≠ N51), P51 (≠ D53), R64 (≠ G66), R76 (≠ V78), R78 (= R80), N82 (= N84), N84 (≠ K86), M87 (= M87), E93 (= E93), P109 (= P109), D111 (= D113), N113 (≠ E115), H114 (≠ T116), N116 (≠ G118), T117 (≠ G119), E119 (= E121), 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 (≠ Q342), H448 (= H444), H449 (= H445), F514 (= F510), R549 (= R545), T557 (≠ N553), T558 (≠ N554), A559 (≠ S555)
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)
47% identity, 99% coverage: 1:578/581 of query aligns to 1:583/591 of Q51422
- H31 (≠ L31) 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 (vs. gap) 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)
47% identity, 99% coverage: 2:578/581 of query aligns to 1:582/585 of 4wj4A
- active site: R219 (= R219), E221 (= E221), R227 (= R227), Q228 (= Q228), E482 (= E478), G485 (= G481), R537 (= R533)
- binding aspartic acid: S195 (= S195), Q197 (= Q197), H450 (= H445), R489 (= R485), L531 (≠ I527)
- binding : R26 (≠ K27), R28 (= R29), D29 (= D30), H30 (≠ L31), G31 (= G32), G32 (= G33), V33 (≠ M34), F35 (= F36), Q46 (= Q47), R64 (≠ L65), R76 (≠ V78), P79 (≠ S81), A82 (vs. gap), N84 (= N84), E93 (= E93), T107 (≠ L107), P109 (= P109), D113 (= D113), E114 (≠ D114), D117 (= D117), E121 (= E121), A175 (= A175), E221 (= E221), D222 (= D222), R224 (= R224), A225 (= A225), R227 (= R227), Y346 (≠ I343), A447 (= A442), H449 (= H444), H450 (= H445), R549 (= R545), T557 (≠ N553), Q558 (≠ N554), S559 (= S555)
4wj3M Crystal structure of the asparagine transamidosome from pseudomonas aeruginosa (see paper)
47% identity, 99% coverage: 2:578/581 of query aligns to 1:582/589 of 4wj3M
- active site: R219 (= R219), E221 (= E221), R227 (= R227), Q228 (= Q228), E482 (= E478), G485 (= G481), R537 (= R533)
- binding : R28 (= R29), D29 (= D30), H30 (≠ L31), G32 (= G33), V33 (≠ M34), F35 (= F36), Q46 (= Q47), R64 (≠ L65), R76 (≠ V78), R78 (= R80), A82 (vs. gap), N84 (= N84), E93 (= E93), T107 (≠ L107), D113 (= D113), V118 (≠ G118)
4rmfA Biochemical and structural characterization of mycobacterial aspartyl- tRNA synthetase asps, a promising tb drug target (see paper)
46% identity, 99% coverage: 2:574/581 of query aligns to 1:577/579 of 4rmfA
- active site: R215 (= R219), E217 (= E221), R223 (= R227), Q224 (= Q228), E481 (= E478), G484 (= G481), R536 (= R533)
- binding 2,2-bis(hydroxymethyl)propane-1,3-diol: H447 (= H444), D474 (= D471), E481 (= E478)
6hhxA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)cytidine (see paper)
50% identity, 99% coverage: 1:577/581 of query aligns to 2:571/574 of 6hhxA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)cytidine: Q202 (= Q197), K205 (= K200), R224 (= R219), F236 (= F231), Q238 (= Q233), H438 (= H444), E472 (= E478), V473 (= V479), G474 (= G480), G475 (= G481), G476 (= G482), R479 (= R485), I521 (= I527), A522 (= A528), G524 (= G530)
6hhwA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)uridine (see paper)
50% identity, 99% coverage: 1:577/581 of query aligns to 2:571/574 of 6hhwA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)uridine: Q202 (= Q197), K205 (= K200), R224 (= R219), F236 (= F231), Q238 (= Q233), H438 (= H444), E472 (= E478), V473 (= V479), G474 (= G480), G475 (= G481), G476 (= G482), R479 (= R485), I521 (= I527), A522 (= A528), G524 (= G530)
6hhvA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)n3-methyluridine (see paper)
50% identity, 99% coverage: 1:577/581 of query aligns to 2:571/574 of 6hhvA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)N3-methyluridine: Q202 (= Q197), R224 (= R219), F236 (= F231), Q238 (= Q233), H438 (= H444), E472 (= E478), V473 (= V479), G474 (= G480), G475 (= G481), G476 (= G482), R479 (= R485), I521 (= I527), A522 (= A528), G524 (= G530), R527 (= R533)
7ap4A Thermus thermophilus aspartyl-tRNA synthetase in complex with compound asps7hmdda (see paper)
50% identity, 99% coverage: 1:577/581 of query aligns to 2:570/573 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 (= Q197), R222 (= R219), R230 (= R227), Q231 (= Q228), F234 (= F231), Q236 (= Q233), E471 (= E478), G473 (= G480), G474 (= G481), G475 (= G482), R478 (= R485), I520 (= I527), A521 (= A528), G523 (= G530)
4o2dA Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
45% identity, 99% coverage: 1:577/581 of query aligns to 1:579/580 of 4o2dA
- active site: R216 (= R219), E218 (= E221), R222 (= R227), Q223 (= Q228), E480 (= E478), G483 (= G481), R535 (= R533)
- binding aspartic acid: E170 (= E173), S192 (= S195), Q194 (= Q197), Q228 (= Q233), H446 (= H444), H447 (= H445), G483 (= G481), R487 (= R485), I529 (= I527), A530 (= A528)
5w25A Crystal structure of aspartyl-tRNA synthetase from mycobacterium tuberculosis complexed with l-aspartic acid
45% identity, 99% coverage: 1:574/581 of query aligns to 2:582/583 of 5w25A
- active site: R220 (= R219), E222 (= E221), R228 (= R227), Q229 (= Q228), E486 (= E478), G489 (= G481), R541 (= R533)
- binding aspartic acid: E174 (= E173), Q198 (= Q197), R220 (= R219), H452 (= H444), H453 (= H445), G489 (= G481), R493 (= R485)
- binding lysine: D159 (= D158), R211 (= R210)
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)
45% identity, 99% coverage: 2:578/581 of query aligns to 1:574/577 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 (≠ M87) 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)
42% identity, 99% coverage: 1:577/581 of query aligns to 1:514/515 of 4o2dB
- active site: R216 (= R219), E218 (= E221), R222 (= R227), Q223 (= Q228), E415 (= E478), G418 (= G481), R470 (= R533)
- binding aspartic acid: E170 (= E173), S192 (= S195), Q194 (= Q197), Q228 (= Q233), H382 (= H445), G418 (= G481), R422 (= R485), I464 (= I527), A465 (= A528)
Q6PI48 Aspartate--tRNA ligase, mitochondrial; Aspartyl-tRNA synthetase; AspRS; EC 6.1.1.12 from Homo sapiens (Human) (see 2 papers)
42% identity, 100% coverage: 1:580/581 of query aligns to 48:634/645 of Q6PI48
- R58 (≠ N11) 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 (≠ A291) mutation to E: No effect on its mitochondria localization.
- L613 (≠ V559) to F: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918212
- L626 (= L572) 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
O07683 Aspartate--tRNA(Asp/Asn) ligase; Aspartyl-tRNA synthetase; AspRS; Non-discriminating aspartyl-tRNA synthetase; ND-AspRS; EC 6.1.1.23 from Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium) (see paper)
33% identity, 45% coverage: 1:261/581 of query aligns to 1:257/436 of O07683
- H26 (≠ Q26) mutation H->A,Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn).
- P84 (= P85) mutation P->A,K: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn).
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
31% identity, 49% coverage: 1:282/581 of query aligns to 1:293/438 of 3nemB
Sites not aligning to the query:
Query Sequence
>CA265_RS19975 FitnessBrowser__Pedo557:CA265_RS19975
MLRTVTCGALNLNNLGESVTLCGWVQKSRDLGGMTFIDIRDRYGITQLVFNMDDNRELCE
TARTLGREFVIKAIGTVVERSNKNPKMATGDVEIKISALEILNAAKLPPFMIDDETDGGD
ELRMKYRYLDLRRNPVRNNLVLRHKMAQSVRRYLDALDFIEVETPVLIKSTPEGARDFVV
PSRMNEGEFYALPQSPQTFKQLLMVSGFDRYFQIVKCFRDEDLRADRQPEFTQIDCEMSF
IEQEDILNTFEGLIRTLFKEVRNYDLPEVPRMQYADAMRLYGSDKPDTRFAMQFVELNHL
VKGKGFPVFDNAELVVGINAKGAASYTRKQLDELTDFIKRPQIGATGLIYARHNEDGTIK
SSVDKFFNEEDLKQWSEAFGTEKGDLLLILAGSTDKVRKQLNELRLEMGSRLGLRDKNTF
SALWVLDFPLLEWDEETERYHAMHHPFTSPKPEDIALLDTDPKNVRANAYDMVINGTEVG
GGSIRIHDRALQALMFKHLGFSAEEAQKQFGFLMDAFEFGAPPHGGIAFGFDRLTSIFAG
LDSIRDVIAFPKNNSGRDVMIDSPSTIDEKQLKELKIKTDL
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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