SitesBLAST
Comparing CCNA_01969 FitnessBrowser__Caulo:CCNA_01969 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)
41% identity, 98% coverage: 8:605/612 of query aligns to 2:574/577 of P56459
- L81 (≠ V87) mutation to N: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by reducing enzyme's ability to misacylate tRNA(Asn).
- L86 (= L92) mutation to M: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by reducing enzyme's ability to misacylate tRNA(Asn).
1g51B Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
44% identity, 98% coverage: 8:609/612 of query aligns to 3:580/580 of 1g51B
- active site: R223 (= R224), E225 (= E226), R231 (= R232), Q232 (≠ S233), E476 (= E505), G479 (≠ S508), R531 (= R560)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E178), S199 (≠ A200), Q201 (= Q202), K204 (= K205), R223 (= R224), Q232 (≠ S233), F235 (= F236), Q237 (= Q238), H442 (= H471), E476 (= E505), G478 (≠ C507), G479 (≠ S508), G480 (= G509), R483 (= R512), I525 (≠ L554), A526 (= A555), G528 (= G557), R531 (= R560)
- binding adenosine monophosphate: V313 (≠ L333), Q347 (≠ P373), G348 (= G374), L349 (= L375), A350 (≠ G376), V389 (= V417), A390 (= A418)
1g51A Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
44% identity, 98% coverage: 8:609/612 of query aligns to 3:580/580 of 1g51A
- active site: R223 (= R224), E225 (= E226), R231 (= R232), Q232 (≠ S233), E476 (= E505), G479 (≠ S508), R531 (= R560)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E178), Q201 (= Q202), K204 (= K205), R223 (= R224), R231 (= R232), Q232 (≠ S233), F235 (= F236), Q237 (= Q238), H442 (= H471), H443 (≠ N472), E476 (= E505), G478 (≠ C507), G479 (≠ S508), G480 (= G509), R483 (= R512), I525 (≠ L554), A526 (= A555), G528 (= G557), R531 (= R560)
1efwA Crystal structure of aspartyl-tRNA synthetase from thermus thermophilus complexed to trnaasp from escherichia coli (see paper)
44% identity, 98% coverage: 8:609/612 of query aligns to 3:580/580 of 1efwA
- active site: R223 (= R224), E225 (= E226), R231 (= R232), Q232 (≠ S233), E476 (= E505), G479 (≠ S508), R531 (= R560)
- binding : R27 (= R32), R29 (= R34), D30 (= D35), L31 (≠ H36), G32 (= G37), G33 (= G38), L34 (= L39), F36 (= F41), Q47 (= Q52), H51 (= H56), P52 (= P57), R64 (= R69), R78 (= R83), E80 (≠ A85), N82 (= N89), R84 (≠ N91), E91 (= E98), T105 (≠ E112), P107 (= P114), E125 (= E126), R343 (≠ G369)
6sjcB Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)adenosine (see paper)
44% identity, 98% coverage: 8:609/612 of query aligns to 4:581/581 of 6sjcB
- binding 5'-O-(L-alpha-aspartylsulfamoyl)adenosine: E178 (= E178), Q202 (= Q202), K205 (= K205), R224 (= R224), R232 (= R232), Q233 (≠ S233), F236 (= F236), Q238 (= Q238), E477 (= E505), V478 (≠ L506), G479 (≠ C507), G480 (≠ S508), G481 (= G509), R484 (= R512), I526 (≠ L554), A527 (= A555), G529 (= G557), R532 (= R560)
4rmfA Biochemical and structural characterization of mycobacterial aspartyl- tRNA synthetase asps, a promising tb drug target (see paper)
43% identity, 97% coverage: 8:601/612 of query aligns to 2:577/579 of 4rmfA
- active site: R215 (= R224), E217 (= E226), R223 (= R232), Q224 (≠ S233), E481 (= E505), G484 (≠ S508), R536 (= R560)
- binding 2,2-bis(hydroxymethyl)propane-1,3-diol: H447 (= H471), D474 (= D498), E481 (= E505)
4wj3M Crystal structure of the asparagine transamidosome from pseudomonas aeruginosa (see paper)
40% identity, 98% coverage: 8:605/612 of query aligns to 2:582/589 of 4wj3M
- active site: R219 (= R224), E221 (= E226), R227 (= R232), Q228 (≠ S233), E482 (= E505), G485 (≠ S508), R537 (= R560)
- binding : R28 (= R34), D29 (= D35), H30 (= H36), G32 (= G38), V33 (≠ L39), F35 (= F41), Q46 (= Q52), R64 (= R69), R76 (≠ I81), R78 (= R83), A82 (≠ V87), N84 (= N89), E93 (= E98), T107 (≠ E112), D113 (≠ F118), V118 (≠ Y123)
4o2dA Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
43% identity, 98% coverage: 8:604/612 of query aligns to 3:579/580 of 4o2dA
- active site: R216 (= R224), E218 (= E226), R222 (= R232), Q223 (≠ S233), E480 (= E505), G483 (≠ S508), R535 (= R560)
- binding aspartic acid: E170 (= E178), S192 (≠ A200), Q194 (= Q202), Q228 (= Q238), H446 (= H471), H447 (≠ N472), G483 (≠ S508), R487 (= R512), I529 (≠ L554), A530 (= A555)
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)
40% identity, 98% coverage: 8:605/612 of query aligns to 3:583/591 of Q51422
- H31 (= H36) 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 (≠ S86) 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)
40% identity, 98% coverage: 8:605/612 of query aligns to 2:582/585 of 4wj4A
- active site: R219 (= R224), E221 (= E226), R227 (= R232), Q228 (≠ S233), E482 (= E505), G485 (≠ S508), R537 (= R560)
- binding aspartic acid: S195 (≠ A200), Q197 (= Q202), H450 (≠ N472), R489 (= R512), L531 (= L554)
- binding : R26 (= R32), R28 (= R34), D29 (= D35), H30 (= H36), G31 (= G37), G32 (= G38), V33 (≠ L39), F35 (= F41), Q46 (= Q52), R64 (= R69), R76 (≠ I81), P79 (≠ D84), A82 (≠ V87), N84 (= N89), E93 (= E98), T107 (≠ E112), P109 (= P114), D113 (≠ F118), E114 (≠ G119), D117 (= D122), E121 (= E126), A175 (= A180), E221 (= E226), D222 (= D227), R224 (= R229), A225 (= A230), R227 (= R232), Y346 (≠ E370), A447 (≠ F469), H449 (= H471), H450 (≠ N472), R549 (= R572), T557 (≠ N580), Q558 (= Q581), S559 (≠ Q582)
6hhxA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)cytidine (see paper)
44% identity, 98% coverage: 8:604/612 of query aligns to 4:571/574 of 6hhxA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)cytidine: Q202 (= Q202), K205 (= K205), R224 (= R224), F236 (= F236), Q238 (= Q238), H438 (= H471), E472 (= E505), V473 (≠ L506), G474 (≠ C507), G475 (≠ S508), G476 (= G509), R479 (= R512), I521 (≠ L554), A522 (= A555), G524 (= G557)
6hhwA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)uridine (see paper)
44% identity, 98% coverage: 8:604/612 of query aligns to 4:571/574 of 6hhwA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)uridine: Q202 (= Q202), K205 (= K205), R224 (= R224), F236 (= F236), Q238 (= Q238), H438 (= H471), E472 (= E505), V473 (≠ L506), G474 (≠ C507), G475 (≠ S508), G476 (= G509), R479 (= R512), I521 (≠ L554), A522 (= A555), G524 (= G557)
6hhvA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)n3-methyluridine (see paper)
44% identity, 98% coverage: 8:604/612 of query aligns to 4:571/574 of 6hhvA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)N3-methyluridine: Q202 (= Q202), R224 (= R224), F236 (= F236), Q238 (= Q238), H438 (= H471), E472 (= E505), V473 (≠ L506), G474 (≠ C507), G475 (≠ S508), G476 (= G509), R479 (= R512), I521 (≠ L554), A522 (= A555), G524 (= G557), R527 (= R560)
5w25A Crystal structure of aspartyl-tRNA synthetase from mycobacterium tuberculosis complexed with l-aspartic acid
42% identity, 97% coverage: 8:601/612 of query aligns to 4:582/583 of 5w25A
- active site: R220 (= R224), E222 (= E226), R228 (= R232), Q229 (≠ S233), E486 (= E505), G489 (≠ S508), R541 (= R560)
- binding aspartic acid: E174 (= E178), Q198 (= Q202), R220 (= R224), H452 (= H471), H453 (≠ N472), G489 (≠ S508), R493 (= R512)
- binding lysine: D159 (≠ G163), R211 (= R215)
7ap4A Thermus thermophilus aspartyl-tRNA synthetase in complex with compound asps7hmdda (see paper)
44% identity, 98% coverage: 8:604/612 of query aligns to 4:570/573 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 (= Q202), R222 (= R224), R230 (= R232), Q231 (≠ S233), F234 (= F236), Q236 (= Q238), E471 (= E505), G473 (≠ C507), G474 (≠ S508), G475 (= G509), R478 (= R512), I520 (≠ L554), A521 (= A555), G523 (= G557)
1c0aA Crystal structure of the e. Coli aspartyl-tRNA synthetase : trnaasp : aspartyl-adenylate complex (see paper)
40% identity, 98% coverage: 8:606/612 of query aligns to 2:583/585 of 1c0aA
- active site: E482 (= E505), G485 (≠ S508), R537 (= R560)
- binding aspartyl-adenosine-5'-monophosphate: S193 (≠ A200), Q195 (= Q202), K198 (= K205), R217 (= R224), Q226 (≠ S233), F229 (= F236), Q231 (= Q238), H448 (= H471), E482 (= E505), V483 (≠ L506), G484 (≠ C507), G485 (≠ S508), G486 (= G509), R489 (= R512), L531 (= L554), A532 (= A555), G534 (= G557), R537 (= R560)
- binding adenosine monophosphate: F304 (= F331), V306 (≠ L333), K347 (≠ P373), G348 (= G374), A350 (≠ G376)
- binding : R26 (= R32), R28 (= R34), D29 (= D35), L30 (≠ H36), G31 (= G37), S32 (≠ G38), L33 (= L39), F35 (= F41), Q46 (= Q52), F48 (≠ V54), D50 (≠ H56), P51 (= P57), R64 (= R69), R76 (≠ I81), R78 (= R83), N82 (≠ V87), N84 (= N89), M87 (≠ L92), E93 (= E98), P109 (= P114), D111 (≠ P116), N113 (≠ E120), H114 (≠ P121), N116 (≠ Y123), T117 (≠ P124), E119 (= E126), T169 (≠ S176), P170 (= P177), E171 (= E178), G172 (= G179), A173 (= A180), S193 (≠ A200), R217 (= R224), E219 (= E226), D220 (= D227), R222 (= R229), A223 (= A230), R225 (= R232), I343 (≠ G369), H448 (= H471), H449 (≠ N472), F514 (= F537), R549 (= R572), T557 (≠ N580), T558 (≠ Q581), A559 (≠ Q582)
Q6PI48 Aspartate--tRNA ligase, mitochondrial; Aspartyl-tRNA synthetase; AspRS; EC 6.1.1.12 from Homo sapiens (Human) (see 2 papers)
36% identity, 98% coverage: 8:609/612 of query aligns to 50:636/645 of Q6PI48
- R58 (= R16) mutation to G: No effect on its mitochondria localization.
- T136 (= T94) mutation to S: No effect on its mitochondria localization.
- Q184 (≠ H142) to K: in LBSL; Significant impairment of its mitochondrial matrix localization; dbSNP:rs1469160736
- R263 (≠ P221) to Q: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918207
- G338 (≠ P316) mutation to E: No effect on its mitochondria localization.
- L613 (= L586) to F: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918212
- L626 (= L599) 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)
46% identity, 52% coverage: 8:326/612 of query aligns to 3:296/515 of 4o2dB
Sites not aligning to the query:
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
34% identity, 42% coverage: 7:262/612 of query aligns to 2:255/438 of 3nemB
Sites not aligning to the query:
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
34% identity, 42% coverage: 7:262/612 of query aligns to 2:255/438 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
>CCNA_01969 FitnessBrowser__Caulo:CCNA_01969
MTTMHAYRTHNCGALRASDTGAAVRLSGWIHRKRDHGGLVFIDLRDHYGLTQLVLHPETP
GFNVVERLRAESVIRVDGEVIARDASVVNPNLPTGEIEIRVSAVEVLSEAAELPLPVFGE
PDYPEEIRLKHRYLDLRRETLHKNIVLRSRVIQSIRNRMFAQGFNEFQTPILTASSPEGA
RDFLVPSRLHPEKFYALPQAPQQFKQLLMVSGFDRYFQIAPCFRDEDLRADRSLEFYQLD
VEMSFVTQEDVFAAIEPVMHGVFEEFSNGKPVSPINGTHTFTNDFGQSFEHKGFERLTYA
QSMAWYGSDKPDLRNPIKMANVSEHFRDGGFGLFAKILGADAKNQVWAIPAPTGGSRAFC
DRMNSWAQGEGQPGLGYVFWSEDQGGWGGPIAKNLGEPTQALMESLGLGAGDAAFFVAGD
PAVFAKFAGLARTRVGTELKLVDENQFKFCWIVDFPMFEWNEEEKKVDFSHNPFSMPQGG
LEALETQDPLTIRAYQYDIVCNGYELCSGAIRNHKPEIMLKAFATAGYGPEVVEEQFGGM
LNAFRYGAPPHGGLAPGIDRIVMLLADQVAIREVIAFPLNQQGQDLLMNAPANVLDKQLK
ELHIRTAPPIKV
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