SitesBLAST
Comparing WP_010531090.1 NCBI__GCF_000224785.1:WP_010531090.1 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)
1c0aA Crystal structure of the e. Coli aspartyl-tRNA synthetase : trnaasp : aspartyl-adenylate complex (see paper)
51% identity, 98% coverage: 7:584/588 of query aligns to 6:583/585 of 1c0aA
- active site: E482 (= E483), G485 (= G486), R537 (= R538)
- binding aspartyl-adenosine-5'-monophosphate: S193 (= S197), Q195 (= Q199), K198 (= K202), R217 (= R221), Q226 (= Q230), F229 (= F233), Q231 (= Q235), H448 (= H449), E482 (= E483), V483 (≠ L484), G484 (= G485), G485 (= G486), G486 (= G487), R489 (= R490), L531 (≠ I532), A532 (= A533), G534 (= G535), R537 (= R538)
- binding adenosine monophosphate: F304 (= F309), V306 (= V311), K347 (= K352), G348 (= G353), A350 (= A355)
- binding : R26 (≠ T27), R28 (= R29), D29 (= D30), L30 (= L31), G31 (= G32), S32 (≠ G33), L33 (= L34), F35 (= F36), Q46 (= Q47), F48 (≠ V49), D50 (≠ N51), P51 (= P52), R64 (= R66), R76 (≠ V78), R78 (= R80), N82 (≠ T84), N84 (= N86), M87 (= M89), E93 (= E95), P109 (= P111), D111 (≠ Q115), N113 (≠ E117), H114 (≠ T118), N116 (≠ V120), T117 (≠ A121), E119 (≠ D123), 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 (= H449), H449 (= H450), F514 (= F515), R549 (= R550), T557 (= T558), T558 (≠ A559), A559 (≠ S560)
4wj3M Crystal structure of the asparagine transamidosome from pseudomonas aeruginosa (see paper)
52% identity, 99% coverage: 7:587/588 of query aligns to 6:586/589 of 4wj3M
- active site: R219 (= R221), E221 (= E223), R227 (= R229), Q228 (= Q230), E482 (= E483), G485 (= G486), R537 (= R538)
- binding : R28 (= R29), D29 (= D30), H30 (≠ L31), G32 (= G33), V33 (≠ L34), F35 (= F36), Q46 (= Q47), R64 (= R66), R76 (≠ V78), R78 (= R80), A82 (≠ T84), N84 (= N86), E93 (= E95), T107 (= T109), D113 (≠ Q115), V118 (= V120)
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)
52% identity, 99% coverage: 7:587/588 of query aligns to 7:587/591 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 (= G83) 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)
52% identity, 99% coverage: 7:586/588 of query aligns to 6:585/585 of 4wj4A
- active site: R219 (= R221), E221 (= E223), R227 (= R229), Q228 (= Q230), E482 (= E483), G485 (= G486), R537 (= R538)
- binding aspartic acid: S195 (= S197), Q197 (= Q199), H450 (= H450), R489 (= R490), L531 (≠ I532)
- binding : R26 (≠ T27), R28 (= R29), D29 (= D30), H30 (≠ L31), G31 (= G32), G32 (= G33), V33 (≠ L34), F35 (= F36), Q46 (= Q47), R64 (= R66), R76 (≠ V78), P79 (≠ D81), A82 (≠ T84), N84 (= N86), E93 (= E95), T107 (= T109), P109 (= P111), D113 (≠ Q115), E114 (= E116), D117 (= D119), E121 (≠ D123), A175 (= A177), E221 (= E223), D222 (= D224), R224 (= R226), A225 (= A227), R227 (= R229), Y346 (= Y349), A447 (= A447), H449 (= H449), H450 (= H450), R549 (= R550), T557 (= T558), Q558 (≠ A559), S559 (= S560)
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: 10:584/588 of query aligns to 9:575/577 of P56459
- L81 (≠ T84) mutation to N: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by reducing enzyme's ability to misacylate tRNA(Asn).
- L86 (≠ M89) 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)
51% identity, 98% coverage: 7:584/588 of query aligns to 7:577/580 of 1g51B
- active site: R223 (= R221), E225 (= E223), R231 (= R229), Q232 (= Q230), E476 (= E483), G479 (= G486), R531 (= R538)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E175), S199 (= S197), Q201 (= Q199), K204 (= K202), R223 (= R221), Q232 (= Q230), F235 (= F233), Q237 (= Q235), H442 (= H449), E476 (= E483), G478 (= G485), G479 (= G486), G480 (= G487), R483 (= R490), I525 (= I532), A526 (= A533), G528 (= G535), R531 (= R538)
- binding adenosine monophosphate: V313 (= V311), Q347 (≠ K352), G348 (= G353), L349 (≠ M354), A350 (= A355), V389 (≠ G395), A390 (≠ S396)
1g51A Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
51% identity, 98% coverage: 7:584/588 of query aligns to 7:577/580 of 1g51A
- active site: R223 (= R221), E225 (= E223), R231 (= R229), Q232 (= Q230), E476 (= E483), G479 (= G486), R531 (= R538)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E175), Q201 (= Q199), K204 (= K202), R223 (= R221), R231 (= R229), Q232 (= Q230), F235 (= F233), Q237 (= Q235), H442 (= H449), H443 (= H450), E476 (= E483), G478 (= G485), G479 (= G486), G480 (= G487), R483 (= R490), I525 (= I532), A526 (= A533), G528 (= G535), R531 (= R538)
1efwA Crystal structure of aspartyl-tRNA synthetase from thermus thermophilus complexed to trnaasp from escherichia coli (see paper)
51% identity, 98% coverage: 7:584/588 of query aligns to 7:577/580 of 1efwA
- active site: R223 (= R221), E225 (= E223), R231 (= R229), Q232 (= Q230), E476 (= E483), G479 (= G486), R531 (= R538)
- binding : R27 (≠ T27), R29 (= R29), D30 (= D30), L31 (= L31), G32 (= G32), G33 (= G33), L34 (= L34), F36 (= F36), Q47 (= Q47), H51 (≠ N51), P52 (= P52), R64 (= R66), R78 (= R80), E80 (= E82), N82 (= N86), R84 (≠ A88), E91 (= E95), T105 (= T109), P107 (= P111), E125 (≠ D123), R343 (≠ I348)
6sjcB Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)adenosine (see paper)
51% identity, 98% coverage: 7:584/588 of query aligns to 8:578/581 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 (= E483), V478 (≠ L484), G479 (= G485), G480 (= G486), G481 (= G487), R484 (= R490), I526 (= I532), A527 (= A533), G529 (= G535), R532 (= R538)
6hhxA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)cytidine (see paper)
51% identity, 98% coverage: 7:584/588 of query aligns to 8:573/574 of 6hhxA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)cytidine: Q202 (= Q199), K205 (= K202), R224 (= R221), F236 (= F233), Q238 (= Q235), H438 (= H449), E472 (= E483), V473 (≠ L484), G474 (= G485), G475 (= G486), G476 (= G487), R479 (= R490), I521 (= I532), A522 (= A533), G524 (= G535)
6hhwA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)uridine (see paper)
51% identity, 98% coverage: 7:584/588 of query aligns to 8:573/574 of 6hhwA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)uridine: Q202 (= Q199), K205 (= K202), R224 (= R221), F236 (= F233), Q238 (= Q235), H438 (= H449), E472 (= E483), V473 (≠ L484), G474 (= G485), G475 (= G486), G476 (= G487), R479 (= R490), I521 (= I532), A522 (= A533), G524 (= G535)
6hhvA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)n3-methyluridine (see paper)
51% identity, 98% coverage: 7:584/588 of query aligns to 8:573/574 of 6hhvA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)N3-methyluridine: Q202 (= Q199), R224 (= R221), F236 (= F233), Q238 (= Q235), H438 (= H449), E472 (= E483), V473 (≠ L484), G474 (= G485), G475 (= G486), G476 (= G487), R479 (= R490), I521 (= I532), A522 (= A533), G524 (= G535), R527 (= R538)
7ap4A Thermus thermophilus aspartyl-tRNA synthetase in complex with compound asps7hmdda (see paper)
50% identity, 98% coverage: 7:584/588 of query aligns to 8:572/573 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 (= Q199), R222 (= R221), R230 (= R229), Q231 (= Q230), F234 (= F233), Q236 (= Q235), E471 (= E483), G473 (= G485), G474 (= G486), G475 (= G487), R478 (= R490), I520 (= I532), A521 (= A533), G523 (= G535)
4rmfA Biochemical and structural characterization of mycobacterial aspartyl- tRNA synthetase asps, a promising tb drug target (see paper)
46% identity, 97% coverage: 7:579/588 of query aligns to 6:577/579 of 4rmfA
- active site: R215 (= R221), E217 (= E223), R223 (= R229), Q224 (= Q230), E481 (= E483), G484 (= G486), R536 (= R538)
- binding 2,2-bis(hydroxymethyl)propane-1,3-diol: H447 (= H449), D474 (= D476), E481 (= E483)
4o2dA Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
46% identity, 98% coverage: 7:582/588 of query aligns to 7:579/580 of 4o2dA
- active site: R216 (= R221), E218 (= E223), R222 (= R229), Q223 (= Q230), E480 (= E483), G483 (= G486), R535 (= R538)
- binding aspartic acid: E170 (= E175), S192 (= S197), Q194 (= Q199), Q228 (= Q235), H446 (= H449), H447 (= H450), G483 (= G486), R487 (= R490), I529 (= I532), A530 (= A533)
5w25A Crystal structure of aspartyl-tRNA synthetase from mycobacterium tuberculosis complexed with l-aspartic acid
46% identity, 97% coverage: 7:579/588 of query aligns to 8:582/583 of 5w25A
- active site: R220 (= R221), E222 (= E223), R228 (= R229), Q229 (= Q230), E486 (= E483), G489 (= G486), R541 (= R538)
- binding aspartic acid: E174 (= E175), Q198 (= Q199), R220 (= R221), H452 (= H449), H453 (= H450), G489 (= G486), R493 (= R490)
- binding lysine: D159 (≠ G160), R211 (≠ K212)
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: 7:585/588 of query aligns to 54:634/645 of Q6PI48
- R58 (≠ S11) mutation to G: No effect on its mitochondria localization.
- T136 (= T91) 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 (= R218) to Q: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918207
- G338 (= G294) mutation to E: No effect on its mitochondria localization.
- L613 (= L564) to F: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918212
- L626 (= L577) 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: 7:302/588 of query aligns to 7:294/515 of 4o2dB
Sites not aligning to the query:
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
31% identity, 47% coverage: 7:285/588 of query aligns to 7:293/438 of 3nemB
Sites not aligning to the query:
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
31% identity, 47% coverage: 7:285/588 of query aligns to 7:293/438 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_010531090.1 NCBI__GCF_000224785.1:WP_010531090.1
MSERVLAGTLSENDVDQSVLLKGWVQTRRDLGGLIFIDLRDRSGLVQVVFNPDHSKAALE
AAEAVRTEYVLEITGSVVKRDEGTVNPAMGTGRIEVIAKDLTILNKAKTPPFLIQEETDV
AEDLRLKYRYIDLRRNKLQETFKMRHRTTQAIRNFLNDDGFLEMETPILTKSTPEGARDY
LVPSRVHHGQFYALPQSPQLFKQLIMMGGFEKYYQIARCFRDEDLRADRQPEFTQVDIET
SFLTSDEIMDMTEQMMRHVLKEVKNVDISLPLPRMPYDEAMSRFGSDKPDTRFGMELIHV
SDIVKDSSFKVFKGAVESGGKVCLLNAKGQAANYSRKDIDQLTDFVKIYDAKGMAWLKVD
GGQLTGPIAKFLSDDETNGLIERSAAEDGDLLLFGSDKSSVVYDSLGALRLKLGRELNLI
DETKFNFLWVTDWPLLEYDEDLERYFAAHHPFTMPVEEDLDKLDMDPSDVRANAYDLVLN
GYELGGGSLRIHKKDQQMKMLDVLGFTQEEADEQFGFLLEALEYGAPPHGGIALGLDRIV
MLLAGSSNLRDTILFPKTASASDLLTDAPNDVSKGQLDELAIQINDEK
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