SitesBLAST
Comparing WP_005346630.1 NCBI__GCF_000173975.1:WP_005346630.1 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)
4rmfA Biochemical and structural characterization of mycobacterial aspartyl- tRNA synthetase asps, a promising tb drug target (see paper)
41% identity, 98% coverage: 8:576/583 of query aligns to 2:577/579 of 4rmfA
- active site: R215 (= R221), E217 (= E223), R223 (= R229), Q224 (≠ S230), E481 (= E480), G484 (≠ S483), R536 (= R535)
- binding 2,2-bis(hydroxymethyl)propane-1,3-diol: H447 (= H446), D474 (= D473), E481 (= E480)
4o2dA Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
41% identity, 98% coverage: 6:579/583 of query aligns to 1:579/580 of 4o2dA
- active site: R216 (= R221), E218 (= E223), R222 (= R229), Q223 (≠ S230), E480 (= E480), G483 (≠ S483), R535 (= R535)
- binding aspartic acid: E170 (= E175), S192 (≠ A197), Q194 (= Q199), Q228 (= Q236), H446 (= H446), H447 (≠ N447), G483 (≠ S483), R487 (= R487), I529 (≠ M529), A530 (= A530)
5w25A Crystal structure of aspartyl-tRNA synthetase from mycobacterium tuberculosis complexed with l-aspartic acid
41% identity, 98% coverage: 6:576/583 of query aligns to 2:582/583 of 5w25A
- active site: R220 (= R221), E222 (= E223), R228 (= R229), Q229 (≠ S230), E486 (= E480), G489 (≠ S483), R541 (= R535)
- binding aspartic acid: E174 (= E175), Q198 (= Q199), R220 (= R221), H452 (= H446), H453 (≠ N447), G489 (≠ S483), R493 (= R487)
- binding lysine: D159 (≠ G160), R211 (≠ K212)
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: 15:583/583 of query aligns to 9:577/577 of P56459
- L81 (≠ T83) mutation to N: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by reducing enzyme's ability to misacylate tRNA(Asn).
- L86 (≠ I88) mutation to M: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by reducing enzyme's ability to misacylate tRNA(Asn).
1c0aA Crystal structure of the e. Coli aspartyl-tRNA synthetase : trnaasp : aspartyl-adenylate complex (see paper)
40% identity, 98% coverage: 15:583/583 of query aligns to 9:585/585 of 1c0aA
- active site: E482 (= E480), G485 (≠ S483), R537 (= R535)
- binding aspartyl-adenosine-5'-monophosphate: S193 (≠ A197), Q195 (= Q199), K198 (= K202), R217 (= R221), Q226 (≠ S230), F229 (= F234), Q231 (= Q236), H448 (= H446), E482 (= E480), V483 (≠ L481), G484 (≠ S482), G485 (≠ S483), G486 (= G484), R489 (= R487), L531 (≠ M529), A532 (= A530), G534 (= G532), R537 (= R535)
- binding adenosine monophosphate: F304 (= F313), V306 (≠ P315), K347 (≠ G348), G348 (= G349), A350 (≠ G351)
- binding : R26 (≠ N32), R28 (= R34), D29 (= D35), L30 (≠ H36), G31 (= G37), S32 (≠ G38), L33 (≠ V39), F35 (= F41), Q46 (= Q52), F48 (≠ V54), D50 (≠ R56), P51 (vs. gap), R64 (≠ N65), R76 (≠ E77), R78 (= R79), N82 (≠ T83), N84 (= N85), M87 (≠ I88), E93 (= E94), P109 (= P111), D111 (≠ E113), N113 (≠ S117), H114 (≠ K118), N116 (= N120), T117 (≠ H121), E119 (≠ N123), T169 (≠ S173), P170 (= P174), E171 (= E175), G172 (= G176), A173 (= A177), S193 (≠ A197), R217 (= R221), E219 (= E223), D220 (= D224), R222 (= R226), A223 (= A227), R225 (= R229), I343 (≠ S344), H448 (= H446), H449 (≠ N447), F514 (= F512), R549 (= R547), T557 (≠ N555), T558 (≠ G556), A559 (≠ N557)
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)
38% identity, 99% coverage: 6:583/583 of query aligns to 1:586/591 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 (≠ E82) 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.
4wj3M Crystal structure of the asparagine transamidosome from pseudomonas aeruginosa (see paper)
39% identity, 99% coverage: 8:583/583 of query aligns to 2:585/589 of 4wj3M
- active site: R219 (= R221), E221 (= E223), R227 (= R229), Q228 (≠ S230), E482 (= E480), G485 (≠ S483), R537 (= R535)
- binding : R28 (= R34), D29 (= D35), H30 (= H36), G32 (= G38), V33 (= V39), F35 (= F41), Q46 (= Q52), R64 (≠ N65), R76 (≠ E77), R78 (= R79), A82 (≠ T83), N84 (= N85), E93 (= E94), T107 (≠ Q109), D113 (≠ M115), V118 (≠ N120)
4wj4A Crystal structure of non-discriminating aspartyl-tRNA synthetase from pseudomonas aeruginosa complexed with tRNA(asn) and aspartic acid (see paper)
39% identity, 99% coverage: 8:583/583 of query aligns to 2:585/585 of 4wj4A
- active site: R219 (= R221), E221 (= E223), R227 (= R229), Q228 (≠ S230), E482 (= E480), G485 (≠ S483), R537 (= R535)
- binding aspartic acid: S195 (≠ A197), Q197 (= Q199), H450 (≠ N447), R489 (= R487), L531 (≠ M529)
- binding : R26 (≠ N32), R28 (= R34), D29 (= D35), H30 (= H36), G31 (= G37), G32 (= G38), V33 (= V39), F35 (= F41), Q46 (= Q52), R64 (≠ N65), R76 (≠ E77), P79 (≠ D80), A82 (≠ T83), N84 (= N85), E93 (= E94), T107 (≠ Q109), P109 (= P111), D113 (≠ M115), E114 (≠ T116), D117 (≠ E119), E121 (≠ N123), A175 (= A177), E221 (= E223), D222 (= D224), R224 (= R226), A225 (= A227), R227 (= R229), Y346 (≠ I345), A447 (≠ F444), H449 (= H446), H450 (≠ N447), R549 (= R547), T557 (≠ N555), Q558 (≠ G556), S559 (≠ N557)
1g51B Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
39% identity, 97% coverage: 15:581/583 of query aligns to 10:577/580 of 1g51B
- active site: R223 (= R221), E225 (= E223), R231 (= R229), Q232 (≠ S230), E476 (= E480), G479 (≠ S483), R531 (= R535)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E175), S199 (≠ A197), Q201 (= Q199), K204 (= K202), R223 (= R221), Q232 (≠ S230), F235 (= F234), Q237 (= Q236), H442 (= H446), E476 (= E480), G478 (≠ S482), G479 (≠ S483), G480 (= G484), R483 (= R487), I525 (≠ M529), A526 (= A530), G528 (= G532), R531 (= R535)
- binding adenosine monophosphate: V313 (≠ P315), Q347 (≠ G348), G348 (= G349), L349 (= L350), A350 (≠ G351), V389 (≠ I392), A390 (= A393)
1g51A Aspartyl tRNA synthetase from thermus thermophilus at 2.4 a resolution (see paper)
39% identity, 97% coverage: 15:581/583 of query aligns to 10:577/580 of 1g51A
- active site: R223 (= R221), E225 (= E223), R231 (= R229), Q232 (≠ S230), E476 (= E480), G479 (≠ S483), R531 (= R535)
- binding aspartyl-adenosine-5'-monophosphate: E177 (= E175), Q201 (= Q199), K204 (= K202), R223 (= R221), R231 (= R229), Q232 (≠ S230), F235 (= F234), Q237 (= Q236), H442 (= H446), H443 (≠ N447), E476 (= E480), G478 (≠ S482), G479 (≠ S483), G480 (= G484), R483 (= R487), I525 (≠ M529), A526 (= A530), G528 (= G532), R531 (= R535)
1efwA Crystal structure of aspartyl-tRNA synthetase from thermus thermophilus complexed to trnaasp from escherichia coli (see paper)
39% identity, 97% coverage: 15:581/583 of query aligns to 10:577/580 of 1efwA
- active site: R223 (= R221), E225 (= E223), R231 (= R229), Q232 (≠ S230), E476 (= E480), G479 (≠ S483), R531 (= R535)
- binding : R27 (≠ N32), R29 (= R34), D30 (= D35), L31 (≠ H36), G32 (= G37), G33 (= G38), L34 (≠ V39), F36 (= F41), Q47 (= Q52), H51 (≠ R56), P52 (≠ D57), R64 (≠ N65), R78 (= R79), E80 (= E81), N82 (= N85), R84 (≠ K87), E91 (= E94), T105 (≠ Q109), P107 (= P111), E125 (≠ N123), R343 (≠ S344)
6sjcB Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)adenosine (see paper)
39% identity, 97% coverage: 15:581/583 of query aligns to 11:578/581 of 6sjcB
- binding 5'-O-(L-alpha-aspartylsulfamoyl)adenosine: E178 (= E175), Q202 (= Q199), K205 (= K202), R224 (= R221), R232 (= R229), Q233 (≠ S230), F236 (= F234), Q238 (= Q236), E477 (= E480), V478 (≠ L481), G479 (≠ S482), G480 (≠ S483), G481 (= G484), R484 (= R487), I526 (≠ M529), A527 (= A530), G529 (= G532), R532 (= R535)
6hhxA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)cytidine (see paper)
39% identity, 97% coverage: 15:581/583 of query aligns to 11:573/574 of 6hhxA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)cytidine: Q202 (= Q199), K205 (= K202), R224 (= R221), F236 (= F234), Q238 (= Q236), H438 (= H446), E472 (= E480), V473 (≠ L481), G474 (≠ S482), G475 (≠ S483), G476 (= G484), R479 (= R487), I521 (≠ M529), A522 (= A530), G524 (= G532)
6hhwA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)uridine (see paper)
39% identity, 97% coverage: 15:581/583 of query aligns to 11:573/574 of 6hhwA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)uridine: Q202 (= Q199), K205 (= K202), R224 (= R221), F236 (= F234), Q238 (= Q236), H438 (= H446), E472 (= E480), V473 (≠ L481), G474 (≠ S482), G475 (≠ S483), G476 (= G484), R479 (= R487), I521 (≠ M529), A522 (= A530), G524 (= G532)
6hhvA Structure of t. Thermophilus asprs in complex with 5'-o-(n-(l- aspartyl)-sulfamoyl)n3-methyluridine (see paper)
39% identity, 97% coverage: 15:581/583 of query aligns to 11:573/574 of 6hhvA
- binding 5'-O-(N-(L-aspartyl)-sulfamoyl)N3-methyluridine: Q202 (= Q199), R224 (= R221), F236 (= F234), Q238 (= Q236), H438 (= H446), E472 (= E480), V473 (≠ L481), G474 (≠ S482), G475 (≠ S483), G476 (= G484), R479 (= R487), I521 (≠ M529), A522 (= A530), G524 (= G532), R527 (= R535)
7ap4A Thermus thermophilus aspartyl-tRNA synthetase in complex with compound asps7hmdda (see paper)
38% identity, 97% coverage: 15:581/583 of query aligns to 11:572/573 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 (≠ S230), F234 (= F234), Q236 (= Q236), E471 (= E480), G473 (≠ S482), G474 (≠ S483), G475 (= G484), R478 (= R487), I520 (≠ M529), A521 (= A530), G523 (= G532)
4o2dB Crystal structure of aspartyl-tRNA synthetase from mycobacterium smegmatis with bound aspartic acid (see paper)
37% identity, 98% coverage: 6:579/583 of query aligns to 1:514/515 of 4o2dB
- active site: R216 (= R221), E218 (= E223), R222 (= R229), Q223 (≠ S230), E415 (= E480), G418 (≠ S483), R470 (= R535)
- binding aspartic acid: E170 (= E175), S192 (≠ A197), Q194 (= Q199), Q228 (= Q236), H382 (≠ N447), G418 (≠ S483), R422 (= R487), I464 (≠ M529), A465 (= A530)
Q6PI48 Aspartate--tRNA ligase, mitochondrial; Aspartyl-tRNA synthetase; AspRS; EC 6.1.1.12 from Homo sapiens (Human) (see 2 papers)
32% identity, 99% coverage: 6:583/583 of query aligns to 48:635/645 of Q6PI48
- R58 (≠ S16) mutation to G: No effect on its mitochondria localization.
- T136 (= T90) mutation to S: No effect on its mitochondria localization.
- Q184 (≠ K139) to K: in LBSL; Significant impairment of its mitochondrial matrix localization; dbSNP:rs1469160736
- R263 (≠ P218) to Q: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918207
- G338 (≠ P298) mutation to E: No effect on its mitochondria localization.
- L613 (≠ V561) to F: in LBSL; no effect on its mitochondrial localization; dbSNP:rs121918212
- L626 (= L574) 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)
29% identity, 48% coverage: 6:285/583 of query aligns to 1:289/438 of 3nemB
Sites not aligning to the query:
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
29% identity, 48% coverage: 6:285/583 of query aligns to 1:289/438 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_005346630.1 NCBI__GCF_000173975.1:WP_005346630.1
MNIANIYRDRTLDMLSEENVGETVRVAGWVENIRDHGGVSFIDLRDMYGVLQVVMRDTTL
LEGINKEDCISLEGVIEHRDEETYNPKIPTGTIELEAHKVDMLGKVYKQLPFEVMTSKEN
HENVRLKYRYLDLRNKKVKDNMIFRSKVISFLRQKMTDMGFLEIQTPILCASSPEGARDY
IVPSRKYKGKFYALPQAPQQYKQLLMVSGFDKYFQIAPCFRDEDARADRSPGEFYQLDFE
MSFATQEDVFRVGEEVLTATFEKFAPEGSVVTAAPYPVISYKQAMLEFGSDKPDLRNPLR
IVDVTDFFQRCTFKPFHGQTVRAIKVSNKMSKGFHEKLLKFATSIGMGGLGYLEVKEDLS
YKGPIDKFIPDDMKAEIREIASLKAGDTIFFIADKEKQAALYAGQLRNELGQRLDLLEKN
AYRFCFINDFPMYEYDEEQKKIIFTHNPFSMPQGGLEALTTKDPLELLAYQYDIVCNGVE
LSSGAVRNHNLDIMVKAFEIAGYTEEDLKEKFGALYNAFQYGAPPHAGMAPGVDRMIMLL
RNEENIREVIPFPMNGNAQDVMCGAPNEVSEMQLREVHIKVRK
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