SitesBLAST
Comparing WP_012674475.1 NCBI__GCF_000021545.1:WP_012674475.1 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)
51% identity, 98% coverage: 10:597/602 of query aligns to 2:575/577 of P56459
- L81 (≠ T92) mutation to N: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by reducing enzyme's ability to misacylate tRNA(Asn).
- L86 (≠ M97) mutation to M: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by reducing enzyme's ability to misacylate tRNA(Asn).
4wj3M Crystal structure of the asparagine transamidosome from pseudomonas aeruginosa (see paper)
51% identity, 98% coverage: 10:600/602 of query aligns to 2:586/589 of 4wj3M
- active site: R219 (= R229), E221 (= E231), R227 (= R237), Q228 (= Q238), E482 (= E496), G485 (= G499), R537 (= R551)
- binding : R28 (= R36), D29 (= D37), H30 (= H38), G32 (= G40), V33 (= V41), F35 (= F43), Q46 (= Q54), R64 (≠ K74), R76 (≠ S86), R78 (= R88), A82 (≠ T92), N84 (= N94), E93 (= E103), T107 (≠ V117), D113 (≠ E123), V118 (= V128)
4wj4A Crystal structure of non-discriminating aspartyl-tRNA synthetase from pseudomonas aeruginosa complexed with tRNA(asn) and aspartic acid (see paper)
51% identity, 98% coverage: 10:599/602 of query aligns to 2:585/585 of 4wj4A
- active site: R219 (= R229), E221 (= E231), R227 (= R237), Q228 (= Q238), E482 (= E496), G485 (= G499), R537 (= R551)
- binding aspartic acid: S195 (= S205), Q197 (= Q207), H450 (= H457), R489 (= R503), L531 (= L545)
- binding : R26 (≠ T34), R28 (= R36), D29 (= D37), H30 (= H38), G31 (= G39), G32 (= G40), V33 (= V41), F35 (= F43), Q46 (= Q54), R64 (≠ K74), R76 (≠ S86), P79 (= P89), A82 (≠ T92), N84 (= N94), E93 (= E103), T107 (≠ V117), P109 (= P119), D113 (≠ E123), E114 (≠ D124), D117 (≠ K127), E121 (= E131), A175 (= A185), E221 (= E231), D222 (= D232), R224 (= R234), A225 (= A235), R227 (= R237), Y346 (≠ F356), A447 (= A454), H449 (= H456), H450 (= H457), R549 (= R563), T557 (= T571), Q558 (= Q572), S559 (≠ K573)
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)
51% identity, 98% coverage: 10:600/602 of query aligns to 3:587/591 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 (= G91) 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.
1c0aA Crystal structure of the e. Coli aspartyl-tRNA synthetase : trnaasp : aspartyl-adenylate complex (see paper)
51% identity, 98% coverage: 10:597/602 of query aligns to 2:583/585 of 1c0aA
- active site: E482 (= E496), G485 (= G499), R537 (= R551)
- binding aspartyl-adenosine-5'-monophosphate: S193 (= S205), Q195 (= Q207), K198 (= K210), R217 (= R229), Q226 (= Q238), F229 (= F241), Q231 (= Q243), H448 (= H456), E482 (= E496), V483 (≠ I497), G484 (= G498), G485 (= G499), G486 (= G500), R489 (= R503), L531 (= L545), A532 (= A546), G534 (= G548), R537 (= R551)
- binding adenosine monophosphate: F304 (= F317), V306 (= V319), K347 (= K359), G348 (= G360), A350 (= A362)
- binding : R26 (≠ T34), R28 (= R36), D29 (= D37), L30 (≠ H38), G31 (= G39), S32 (≠ G40), L33 (≠ V41), F35 (= F43), Q46 (= Q54), F48 (≠ V56), D50 (= D58), P51 (= P59), R64 (≠ K74), R76 (≠ S86), R78 (= R88), N82 (≠ T92), N84 (= N94), M87 (= M97), E93 (= E103), P109 (= P119), D111 (≠ E123), N113 (= N125), H114 (≠ I126), N116 (≠ V128), T117 (≠ S129), E119 (= E131), T169 (= T181), P170 (= P182), E171 (= E183), G172 (= G184), A173 (= A185), S193 (= S205), R217 (= R229), E219 (= E231), D220 (= D232), R222 (= R234), A223 (= A235), R225 (= R237), I343 (≠ K355), H448 (= H456), H449 (= H457), F514 (= F528), R549 (= R563), T557 (= T571), T558 (≠ Q572), A559 (≠ K573)
6sjcB Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)adenosine (see paper)
52% identity, 98% coverage: 8:597/602 of query aligns to 2:578/581 of 6sjcB
- binding 5'-O-(L-alpha-aspartylsulfamoyl)adenosine: E178 (= E183), Q202 (= Q207), K205 (= K210), R224 (= R229), R232 (= R237), Q233 (= Q238), F236 (= F241), Q238 (= Q243), E477 (= E496), V478 (≠ I497), G479 (= G498), G480 (= G499), G481 (= G500), R484 (= R503), I526 (≠ L545), A527 (= A546), G529 (= G548), R532 (= R551)
1g51B Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
52% identity, 98% coverage: 8:597/602 of query aligns to 1:577/580 of 1g51B
- active site: R223 (= R229), E225 (= E231), R231 (= R237), Q232 (= Q238), E476 (= E496), G479 (= G499), R531 (= R551)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E183), S199 (= S205), Q201 (= Q207), K204 (= K210), R223 (= R229), Q232 (= Q238), F235 (= F241), Q237 (= Q243), H442 (= H456), E476 (= E496), G478 (= G498), G479 (= G499), G480 (= G500), R483 (= R503), I525 (≠ L545), A526 (= A546), G528 (= G548), R531 (= R551)
- binding adenosine monophosphate: V313 (= V319), Q347 (≠ K359), G348 (= G360), L349 (≠ M361), A350 (= A362), V389 (≠ I402), A390 (= A403)
1g51A Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
52% identity, 98% coverage: 8:597/602 of query aligns to 1:577/580 of 1g51A
- active site: R223 (= R229), E225 (= E231), R231 (= R237), Q232 (= Q238), E476 (= E496), G479 (= G499), R531 (= R551)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E183), Q201 (= Q207), K204 (= K210), R223 (= R229), R231 (= R237), Q232 (= Q238), F235 (= F241), Q237 (= Q243), H442 (= H456), H443 (= H457), E476 (= E496), G478 (= G498), G479 (= G499), G480 (= G500), R483 (= R503), I525 (≠ L545), A526 (= A546), G528 (= G548), R531 (= R551)
1efwA Crystal structure of aspartyl-tRNA synthetase from thermus thermophilus complexed to trnaasp from escherichia coli (see paper)
52% identity, 98% coverage: 8:597/602 of query aligns to 1:577/580 of 1efwA
- active site: R223 (= R229), E225 (= E231), R231 (= R237), Q232 (= Q238), E476 (= E496), G479 (= G499), R531 (= R551)
- binding : R27 (≠ T34), R29 (= R36), D30 (= D37), L31 (≠ H38), G32 (= G39), G33 (= G40), L34 (≠ V41), F36 (= F43), Q47 (= Q54), H51 (≠ D58), P52 (= P59), R64 (≠ K74), R78 (= R88), E80 (≠ T92), N82 (= N94), R84 (≠ K96), E91 (= E103), T105 (≠ V117), P107 (= P119), E125 (= E131), R343 (≠ K355)
6hhxA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)cytidine (see paper)
51% identity, 98% coverage: 8:597/602 of query aligns to 2:573/574 of 6hhxA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)cytidine: Q202 (= Q207), K205 (= K210), R224 (= R229), F236 (= F241), Q238 (= Q243), H438 (= H456), E472 (= E496), V473 (≠ I497), G474 (= G498), G475 (= G499), G476 (= G500), R479 (= R503), I521 (≠ L545), A522 (= A546), G524 (= G548)
6hhwA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)uridine (see paper)
51% identity, 98% coverage: 8:597/602 of query aligns to 2:573/574 of 6hhwA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)uridine: Q202 (= Q207), K205 (= K210), R224 (= R229), F236 (= F241), Q238 (= Q243), H438 (= H456), E472 (= E496), V473 (≠ I497), G474 (= G498), G475 (= G499), G476 (= G500), R479 (= R503), I521 (≠ L545), A522 (= A546), G524 (= G548)
6hhvA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)n3-methyluridine (see paper)
51% identity, 98% coverage: 8:597/602 of query aligns to 2:573/574 of 6hhvA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)N3-methyluridine: Q202 (= Q207), R224 (= R229), F236 (= F241), Q238 (= Q243), H438 (= H456), E472 (= E496), V473 (≠ I497), G474 (= G498), G475 (= G499), G476 (= G500), R479 (= R503), I521 (≠ L545), A522 (= A546), G524 (= G548), R527 (= R551)
7ap4A Thermus thermophilus aspartyl-tRNA synthetase in complex with compound asps7hmdda (see paper)
51% identity, 98% coverage: 8:597/602 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 (= Q207), R222 (= R229), R230 (= R237), Q231 (= Q238), F234 (= F241), Q236 (= Q243), E471 (= E496), G473 (= G498), G474 (= G499), G475 (= G500), R478 (= R503), I520 (≠ L545), A521 (= A546), G523 (= G548)
4rmfA Biochemical and structural characterization of mycobacterial aspartyl- tRNA synthetase asps, a promising tb drug target (see paper)
48% identity, 97% coverage: 10:594/602 of query aligns to 2:579/579 of 4rmfA
- active site: R215 (= R229), E217 (= E231), R223 (= R237), Q224 (= Q238), E481 (= E496), G484 (= G499), R536 (= R551)
- binding 2,2-bis(hydroxymethyl)propane-1,3-diol: H447 (= H456), D474 (= D489), E481 (= E496)
4o2dA Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
47% identity, 97% coverage: 10:595/602 of query aligns to 3:579/580 of 4o2dA
- active site: R216 (= R229), E218 (= E231), R222 (= R237), Q223 (= Q238), E480 (= E496), G483 (= G499), R535 (= R551)
- binding aspartic acid: E170 (= E183), S192 (= S205), Q194 (= Q207), Q228 (= Q243), H446 (= H456), H447 (= H457), G483 (= G499), R487 (= R503), I529 (≠ L545), A530 (= A546)
5w25A Crystal structure of aspartyl-tRNA synthetase from mycobacterium tuberculosis complexed with l-aspartic acid
47% identity, 97% coverage: 10:592/602 of query aligns to 4:582/583 of 5w25A
- active site: R220 (= R229), E222 (= E231), R228 (= R237), Q229 (= Q238), E486 (= E496), G489 (= G499), R541 (= R551)
- binding aspartic acid: E174 (= E183), Q198 (= Q207), R220 (= R229), H452 (= H456), H453 (= H457), G489 (= G499), R493 (= R503)
- binding lysine: D159 (≠ G168), R211 (= R220)
4o2dB Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
45% identity, 97% coverage: 10:595/602 of query aligns to 3:514/515 of 4o2dB
- active site: R216 (= R229), E218 (= E231), R222 (= R237), Q223 (= Q238), E415 (= E496), G418 (= G499), R470 (= R551)
- binding aspartic acid: E170 (= E183), S192 (= S205), Q194 (= Q207), Q228 (= Q243), H382 (= H457), G418 (= G499), R422 (= R503), I464 (≠ L545), A465 (= A546)
Q6PI48 Aspartate--tRNA ligase, mitochondrial; Aspartyl-tRNA synthetase; AspRS; EC 6.1.1.12 from Homo sapiens (Human) (see 2 papers)
44% identity, 98% coverage: 10:599/602 of query aligns to 50:635/645 of Q6PI48
- R58 (≠ N18) mutation to G: No effect on its mitochondria localization.
- T136 (= T99) mutation to S: No effect on its mitochondria localization.
- Q184 (= Q147) to K: in LBSL; Significant impairment of its mitochondrial matrix localization; dbSNP:rs1469160736
- R263 (≠ K226) to Q: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918207
- G338 (= G302) mutation to E: No effect on its mitochondria localization.
- L613 (≠ P577) to F: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918212
- L626 (= L590) 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)
36% identity, 49% coverage: 10:302/602 of query aligns to 3:302/438 of 3nemB
Sites not aligning to the query:
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
36% identity, 49% coverage: 10:302/602 of query aligns to 3:302/438 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
>WP_012674475.1 NCBI__GCF_000021545.1:WP_012674475.1
MTDQLRDFKRDYYCGDLNEGNIGEEVRLLGWVDTVRDHGGVLFINLRDREGIVQVVFDPS
KISHEVYNKAKKLKSEYVIGVKGIVSRRPVGTENSKMKTGNIEVLAHYLIILNTSEVLPF
QIEDNIKVSEEVRLKYRYLDLRRPSMQRNIILRHEVYQAVREFLVGNGFIEVETPMLTKS
TPEGARDFLVPSRLEKGKFYALPQSPQLFKQILMVAGLERYFQIVKCFRDEDLRADRQPE
FTQIDLEMSFVSEEDVMSLSEALIQHVYKKVLGIDIKIPFKRMSYEEAINKYGTDKPDLR
YGLELIDITDLALEVEFKVFNDVAKSGGLVKGINVKGGAKFSRKEIDDLTEYAKKFGAKG
MAWIKLENGEATSPILKFFTDDQKQRLFQKMQAQDGDLLVFIADKKEITHRVLGFLRKHL
AEKLNLIDKNKLEFLWVVDFPLFEWDEEENRLVAIHHPFTSPKDEDIEKLDQALENPEIA
LSFKSKAYDMVLNGEEIGGGSIRIHTPYLQQKIFKLLNISEEEAKEKFGFLIEALSYGAP
PHGGLAFGLDRILALMTGSESIRDVIAFPKTQKGVCPLTGAPDYVEEKQLKELGIKIEEE
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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