SitesBLAST
Comparing RR42_RS02445 FitnessBrowser__Cup4G11:RR42_RS02445 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)
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)
64% identity, 99% coverage: 4:600/601 of query aligns to 2:590/591 of Q51422
- H31 (= H33) 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 (= G84) 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)
64% identity, 98% coverage: 4:594/601 of query aligns to 1:584/585 of 4wj4A
- active site: R219 (= R221), E221 (= E223), R227 (= R229), Q228 (= Q230), E482 (= E492), G485 (= G495), R537 (= R547)
- binding aspartic acid: S195 (= S197), Q197 (= Q199), H450 (= H459), R489 (= R499), L531 (= L541)
- binding : R26 (= R29), R28 (= R31), D29 (= D32), H30 (= H33), G31 (= G34), G32 (= G35), V33 (= V36), F35 (= F38), Q46 (= Q49), R64 (= R67), R76 (= R79), P79 (= P82), A82 (≠ T85), N84 (= N87), E93 (= E96), T107 (= T110), P109 (= P112), D113 (= D116), E114 (≠ D117), D117 (≠ N119), E121 (≠ T123), A175 (= A177), E221 (= E223), D222 (= D224), R224 (= R226), A225 (= A227), R227 (= R229), Y346 (= Y349), A447 (= A456), H449 (= H458), H450 (= H459), R549 (= R559), T557 (= T567), Q558 (= Q568), S559 (≠ R569)
4wj3M Crystal structure of the asparagine transamidosome from pseudomonas aeruginosa (see paper)
64% identity, 99% coverage: 4:600/601 of query aligns to 1:589/589 of 4wj3M
- active site: R219 (= R221), E221 (= E223), R227 (= R229), Q228 (= Q230), E482 (= E492), G485 (= G495), R537 (= R547)
- binding : R28 (= R31), D29 (= D32), H30 (= H33), G32 (= G35), V33 (= V36), F35 (= F38), Q46 (= Q49), R64 (= R67), R76 (= R79), R78 (= R81), A82 (≠ T85), N84 (= N87), E93 (= E96), T107 (= T110), D113 (= D116), V118 (≠ L120)
1c0aA Crystal structure of the e. Coli aspartyl-tRNA synthetase : trnaasp : aspartyl-adenylate complex (see paper)
57% identity, 98% coverage: 4:593/601 of query aligns to 1:583/585 of 1c0aA
- active site: E482 (= E492), G485 (= G495), R537 (= R547)
- binding aspartyl-adenosine-5'-monophosphate: S193 (= S197), Q195 (= Q199), K198 (= K202), R217 (= R221), Q226 (= Q230), F229 (= F233), Q231 (= Q235), H448 (= H458), E482 (= E492), V483 (≠ M493), G484 (= G494), G485 (= G495), G486 (= G496), R489 (= R499), L531 (= L541), A532 (= A542), G534 (= G544), R537 (= R547)
- binding adenosine monophosphate: F304 (= F309), V306 (= V311), K347 (= K352), G348 (= G353), A350 (= A355)
- binding : R26 (= R29), R28 (= R31), D29 (= D32), L30 (≠ H33), G31 (= G34), S32 (≠ G35), L33 (≠ V36), F35 (= F38), Q46 (= Q49), F48 (≠ V51), D50 (= D53), P51 (= P54), R64 (= R67), R76 (= R79), R78 (= R81), N82 (≠ T85), N84 (= N87), M87 (≠ L90), E93 (= E96), P109 (= P112), D111 (≠ Q114), N113 (≠ D116), H114 (≠ D117), N116 (= N119), T117 (≠ S121), E119 (≠ T123), T169 (= T173), P170 (= P174), E171 (= E175), G172 (= G176), A173 (= A177), S193 (= S197), R217 (= R221), E219 (= E223), D220 (= D224), R222 (= R226), A223 (= A227), R225 (= R229), I343 (= I348), H448 (= H458), H449 (= H459), F514 (= F524), R549 (= R559), T557 (= T567), T558 (≠ Q568), A559 (≠ R569)
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)
50% identity, 98% coverage: 4:594/601 of query aligns to 1:576/577 of P56459
- L81 (≠ T85) mutation to N: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by reducing enzyme's ability to misacylate tRNA(Asn).
- L86 (= L90) 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)
50% identity, 98% coverage: 5:591/601 of query aligns to 3:575/580 of 1g51B
- active site: R223 (= R221), E225 (= E223), R231 (= R229), Q232 (= Q230), E476 (= E492), G479 (= G495), R531 (= R547)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E175), S199 (= S197), Q201 (= Q199), K204 (= K202), R223 (= R221), Q232 (= Q230), F235 (= F233), Q237 (= Q235), H442 (= H458), E476 (= E492), G478 (= G494), G479 (= G495), G480 (= G496), R483 (= R499), I525 (≠ L541), A526 (= A542), G528 (= G544), R531 (= R547)
- binding adenosine monophosphate: V313 (= V311), Q347 (≠ K352), G348 (= G353), L349 (= L354), A350 (= A355), V389 (≠ G400), A390 (= A401)
1g51A Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
50% identity, 98% coverage: 5:591/601 of query aligns to 3:575/580 of 1g51A
- active site: R223 (= R221), E225 (= E223), R231 (= R229), Q232 (= Q230), E476 (= E492), G479 (= G495), R531 (= R547)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E175), Q201 (= Q199), K204 (= K202), R223 (= R221), R231 (= R229), Q232 (= Q230), F235 (= F233), Q237 (= Q235), H442 (= H458), H443 (= H459), E476 (= E492), G478 (= G494), G479 (= G495), G480 (= G496), R483 (= R499), I525 (≠ L541), A526 (= A542), G528 (= G544), R531 (= R547)
1efwA Crystal structure of aspartyl-tRNA synthetase from thermus thermophilus complexed to trnaasp from escherichia coli (see paper)
50% identity, 98% coverage: 5:591/601 of query aligns to 3:575/580 of 1efwA
- active site: R223 (= R221), E225 (= E223), R231 (= R229), Q232 (= Q230), E476 (= E492), G479 (= G495), R531 (= R547)
- binding : R27 (= R29), R29 (= R31), D30 (= D32), L31 (≠ H33), G32 (= G34), G33 (= G35), L34 (≠ V36), F36 (= F38), Q47 (= Q49), H51 (≠ D53), P52 (= P54), R64 (= R67), R78 (= R81), E80 (≠ T85), N82 (= N87), R84 (≠ N89), E91 (= E96), T105 (= T110), P107 (= P112), E125 (≠ T123), R343 (≠ I348)
6sjcB Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)adenosine (see paper)
50% identity, 98% coverage: 5:591/601 of query aligns to 4:576/581 of 6sjcB
- binding 5'-O-(L-alpha-aspartylsulfamoyl)adenosine: E178 (= E175), Q202 (= Q199), K205 (= K202), R224 (= R221), R232 (= R229), Q233 (= Q230), F236 (= F233), Q238 (= Q235), E477 (= E492), V478 (≠ M493), G479 (= G494), G480 (= G495), G481 (= G496), R484 (= R499), I526 (≠ L541), A527 (= A542), G529 (= G544), R532 (= R547)
4rmfA Biochemical and structural characterization of mycobacterial aspartyl- tRNA synthetase asps, a promising tb drug target (see paper)
48% identity, 97% coverage: 4:588/601 of query aligns to 1:577/579 of 4rmfA
- active site: R215 (= R221), E217 (= E223), R223 (= R229), Q224 (= Q230), E481 (= E492), G484 (= G495), R536 (= R547)
- binding 2,2-bis(hydroxymethyl)propane-1,3-diol: H447 (= H458), D474 (= D485), E481 (= E492)
4o2dA Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
47% identity, 98% coverage: 4:591/601 of query aligns to 2:579/580 of 4o2dA
- active site: R216 (= R221), E218 (= E223), R222 (= R229), Q223 (= Q230), E480 (= E492), G483 (= G495), R535 (= R547)
- binding aspartic acid: E170 (= E175), S192 (= S197), Q194 (= Q199), Q228 (= Q235), H446 (= H458), H447 (= H459), G483 (= G495), R487 (= R499), I529 (≠ L541), A530 (= A542)
6hhxA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)cytidine (see paper)
49% identity, 98% coverage: 5:591/601 of query aligns to 4:571/574 of 6hhxA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)cytidine: Q202 (= Q199), K205 (= K202), R224 (= R221), F236 (= F233), Q238 (= Q235), H438 (= H458), E472 (= E492), V473 (≠ M493), G474 (= G494), G475 (= G495), G476 (= G496), R479 (= R499), I521 (≠ L541), A522 (= A542), G524 (= G544)
6hhwA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)uridine (see paper)
49% identity, 98% coverage: 5:591/601 of query aligns to 4:571/574 of 6hhwA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)uridine: Q202 (= Q199), K205 (= K202), R224 (= R221), F236 (= F233), Q238 (= Q235), H438 (= H458), E472 (= E492), V473 (≠ M493), G474 (= G494), G475 (= G495), G476 (= G496), R479 (= R499), I521 (≠ L541), A522 (= A542), G524 (= G544)
6hhvA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)n3-methyluridine (see paper)
49% identity, 98% coverage: 5:591/601 of query aligns to 4:571/574 of 6hhvA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)N3-methyluridine: Q202 (= Q199), R224 (= R221), F236 (= F233), Q238 (= Q235), H438 (= H458), E472 (= E492), V473 (≠ M493), G474 (= G494), G475 (= G495), G476 (= G496), R479 (= R499), I521 (≠ L541), A522 (= A542), G524 (= G544), R527 (= R547)
7ap4A Thermus thermophilus aspartyl-tRNA synthetase in complex with compound asps7hmdda (see paper)
49% identity, 98% coverage: 5:591/601 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 (= Q199), R222 (= R221), R230 (= R229), Q231 (= Q230), F234 (= F233), Q236 (= Q235), E471 (= E492), G473 (= G494), G474 (= G495), G475 (= G496), R478 (= R499), I520 (≠ L541), A521 (= A542), G523 (= G544)
5w25A Crystal structure of aspartyl-tRNA synthetase from mycobacterium tuberculosis complexed with l-aspartic acid
46% identity, 97% coverage: 4:588/601 of query aligns to 3:582/583 of 5w25A
- active site: R220 (= R221), E222 (= E223), R228 (= R229), Q229 (= Q230), E486 (= E492), G489 (= G495), R541 (= R547)
- binding aspartic acid: E174 (= E175), Q198 (= Q199), R220 (= R221), H452 (= H458), H453 (= H459), G489 (= G495), R493 (= R499)
- binding lysine: D159 (≠ G160), R211 (= R212)
Q6PI48 Aspartate--tRNA ligase, mitochondrial; Aspartyl-tRNA synthetase; AspRS; EC 6.1.1.12 from Homo sapiens (Human) (see 2 papers)
39% identity, 98% coverage: 4:593/601 of query aligns to 49:633/645 of Q6PI48
- R58 (≠ T13) mutation to G: No effect on its mitochondria localization.
- T136 (≠ S92) mutation to S: No effect on its mitochondria localization.
- Q184 (= Q139) to K: in LBSL; Significant impairment of its mitochondrial matrix localization; dbSNP:rs1469160736
- R263 (≠ K218) to Q: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918207
- G338 (≠ K294) mutation to E: No effect on its mitochondria localization.
- L613 (= L573) to F: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918212
- L626 (= L586) 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)
52% identity, 50% coverage: 4:302/601 of query aligns to 2:294/515 of 4o2dB
Sites not aligning to the query:
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
34% identity, 47% coverage: 5:288/601 of query aligns to 3:287/438 of 3nemB
Sites not aligning to the query:
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
34% identity, 47% coverage: 5:288/601 of query aligns to 3:287/438 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
>RR42_RS02445 FitnessBrowser__Cup4G11:RR42_RS02445
MSSMRTHYCGLVTEQLSGQEVALTGWVQRRRDHGGVIFIDLRDREGLVQVVCDPDRPEMF
KAAEEIRNEFCVRITGKVRPRPAGTENANLTSGKIEVLCHELTVLNPSVTPPFQLDDDNL
SETTRLTHRVLDLRRPQMQYNLRLRYKVAMEVRKYLDAQGFIDIETPMLGKSTPEGARDY
LVPSRTNPGHFFALPQSPQIFKQMLMVSGFDRYYQITKCFRDEDLRADRQPEFTQIDCET
SFLNEQEIRDLFEDMMRTVFKNAIDVDLDASFPVMEFREAMARFGSDKPDLRVKLEFTEL
TDAMKDVDFKVFSGPANSENGRVVGLCVPGGAAISRSEIDAYTQFVAIYGAKGLAWIKVN
EVAKGRDGLQSPIVKNLHDAAIAEILKRTGAKDGDIIFFGADKAKVVNDAIGGLRLKIGH
SEFGKTHGLFEDVWKPLWVIDFPMFEYDEEDARWVAMHHPFTSPKDEHLQYLETDPGKCI
AKAYDMVLNGWEMGGGSVRIFREDVQSKVFRALKIGEEEARAKFGYLLDALQYGAPPHGG
LAFGLDRIVTMMAGADSIRDVIAFPKTQRAQDLLTQAPSSVDEKQLRELHIRLRAAEPKT
A
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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