SitesBLAST
Comparing WP_014026192.1 NCBI__GCF_000223395.1:WP_014026192.1 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)
3nemB Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
45% identity, 94% coverage: 28:476/476 of query aligns to 3:438/438 of 3nemB
- active site: R214 (= R236), E216 (= E238), R222 (= R244), H223 (= H245), E361 (= E399), S364 (≠ T402), R412 (= R450)
- binding adenosine-5'-triphosphate: R214 (= R236), E216 (= E238), H223 (= H245), L224 (= L246), E361 (= E399), I362 (≠ V400), S363 (≠ A401), S364 (≠ T402), G407 (= G445), G409 (= G447), R412 (= R450)
- binding magnesium ion: E361 (= E399), S364 (≠ T402)
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
45% identity, 94% coverage: 28:476/476 of query aligns to 3:438/438 of 3nemA
- active site: R214 (= R236), E216 (= E238), R222 (= R244), H223 (= H245), E361 (= E399), S364 (≠ T402), R412 (= R450)
- binding aspartyl-adenosine-5'-monophosphate: E170 (= E192), Q192 (= Q214), K195 (= K217), R214 (= R236), E216 (= E238), H223 (= H245), L224 (= L246), Y339 (= Y365), E361 (= E399), I362 (≠ V400), S363 (≠ A401), S364 (≠ T402), G365 (= G403), R368 (= R406), F406 (≠ A444), G407 (= G445), G409 (= G447), R412 (= R450)
3nelA Aspartyl-tRNA synthetase complexed with aspartic acid (see paper)
45% identity, 94% coverage: 28:476/476 of query aligns to 3:438/438 of 3nelA
- active site: R214 (= R236), E216 (= E238), R222 (= R244), H223 (= H245), E361 (= E399), S364 (≠ T402), R412 (= R450)
- binding aspartic acid: E170 (= E192), Q192 (= Q214), K195 (= K217), Y339 (= Y365), S364 (≠ T402), R368 (= R406), F406 (≠ A444), G407 (= G445)
Q52428 Aspartate--tRNA(Asp) ligase; Aspartyl-tRNA synthetase; AspRS; Discriminating aspartyl-tRNA synthetase; D-AspRS; EC 6.1.1.12 from Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) (see paper)
45% identity, 94% coverage: 28:476/476 of query aligns to 3:438/438 of Q52428
- W26 (≠ E51) mutation to H: Gains the ability to form Asp-tRNA(Asn) in vitro. Only 2-fold decrease in catalytic efficiency for Asp-tRNA(Asp) synthesis.
- K85 (≠ L109) mutation to P: Gains the ability to form Asp-tRNA(Asn) in vitro, and is impaired in its ability to synthesize Asp-tRNA(Asp) due to a 8-fold decrease in affinity for tRNA(Asp).
1b8aA Aspartyl-tRNA synthetase (see paper)
44% identity, 94% coverage: 28:476/476 of query aligns to 3:438/438 of 1b8aA
- binding adenosine-5'-triphosphate: R214 (= R236), E216 (= E238), H223 (= H245), L224 (= L246), E361 (= E399), I362 (≠ V400), S363 (≠ A401), S364 (≠ T402), G409 (= G447), R412 (= R450)
- binding manganese (ii) ion: E361 (= E399), S364 (≠ T402)
O07683 Aspartate--tRNA(Asp/Asn) ligase; Aspartyl-tRNA synthetase; AspRS; Non-discriminating aspartyl-tRNA synthetase; ND-AspRS; EC 6.1.1.23 from Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium) (see paper)
40% identity, 94% coverage: 28:476/476 of query aligns to 4:436/436 of O07683
- H26 (≠ E51) mutation H->A,Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn).
- P84 (≠ L109) mutation P->A,K: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn).
O74407 Aspartate--tRNA ligase, cytoplasmic; Aspartyl-tRNA synthetase; AspRS; EC 6.1.1.12 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
33% identity, 92% coverage: 41:476/476 of query aligns to 104:580/580 of O74407
- S282 (≠ V187) modified: Phosphoserine
- S307 (= S212) modified: Phosphoserine
P04802 Aspartate--tRNA ligase, cytoplasmic; Aspartyl-tRNA synthetase; AspRS; EC 6.1.1.12 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
34% identity, 93% coverage: 35:476/476 of query aligns to 99:557/557 of P04802
- P273 (= P184) mutation to G: Loss of activity; important for dimerization.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
1aszA The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction (see paper)
34% identity, 93% coverage: 35:476/476 of query aligns to 32:490/490 of 1aszA
- active site: R258 (= R236), E260 (= E238), R266 (= R244), H267 (= H245), E411 (= E399), S414 (≠ T402), R464 (= R450)
- binding adenosine-5'-triphosphate: R258 (= R236), M268 (≠ L246), F271 (= F249), E411 (= E399), I412 (≠ V400), L413 (≠ A401), G459 (= G445), R464 (= R450)
- binding : R52 (= R54), Q53 (≠ R55), Q54 (≠ H56), T57 (≠ V59), L58 (≠ V60), F60 (= F61), Q71 (= Q72), L73 (≠ V74), E110 (≠ A107), I112 (≠ L109), K113 (≠ G110), E135 (= E124), P138 (= P127), L140 (≠ P129), A154 (vs. gap), L156 (vs. gap), P157 (vs. gap), V158 (vs. gap), N160 (≠ S138), T163 (≠ I141), S213 (≠ T191), E214 (= E192), G215 (= G193), G216 (= G194), S217 (≠ A195), Q233 (= Q211), F237 (≠ L215), E260 (= E238), N261 (≠ K239), S262 (≠ H240), N263 (≠ H241), H267 (= H245), S356 (≠ G332), T357 (= T333), F388 (= F364), K486 (≠ E472)
1asyA Class ii aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA asp (see paper)
34% identity, 93% coverage: 35:476/476 of query aligns to 32:490/490 of 1asyA
- active site: R258 (= R236), E260 (= E238), R266 (= R244), H267 (= H245), E411 (= E399), S414 (≠ T402), R464 (= R450)
- binding : R52 (= R54), Q53 (≠ R55), Q54 (≠ H56), L58 (≠ V60), F60 (= F61), Q71 (= Q72), L73 (≠ V74), K88 (≠ E85), P111 (≠ A108), I112 (≠ L109), K113 (≠ G110), S114 (≠ G111), E135 (= E124), P138 (= P127), A154 (vs. gap), L156 (vs. gap), P157 (vs. gap), V158 (vs. gap), V159 (≠ A137), D162 (≠ A140), T163 (≠ I141), R258 (= R236), E260 (= E238), N261 (≠ K239), S262 (≠ H240), N263 (≠ H241), T264 (= T242), H267 (= H245), M268 (≠ L246), F271 (= F249), T357 (= T333), E411 (= E399), I412 (≠ V400), L413 (≠ A401), S414 (≠ T402), G459 (= G445), R464 (= R450), K486 (≠ E472)
Q9RVH4 Aspartate--tRNA(Asp/Asn) ligase; Aspartyl-tRNA synthetase 2; AspRS2; Non-discriminating aspartyl-tRNA synthetase; ND-AspRS; EC 6.1.1.23 from Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1) (see paper)
36% identity, 92% coverage: 41:476/476 of query aligns to 18:435/435 of Q9RVH4
- H28 (≠ E51) mutation to Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn).
- P77 (≠ L109) mutation P->C,I,L,F,S,V: Seems not to be able to charge tRNA(Asn) in vivo, but Asp-tRNA(Asp) formation is not affected.; mutation to K: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn) and increasing the efficiency of Asp-tRNA(Asp) synthesis in vitro. Seems not to be able to charge tRNA(Asn) in vivo.
1x55A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate analogue (see paper)
34% identity, 92% coverage: 41:476/476 of query aligns to 16:434/434 of 1x55A
- active site: R211 (= R236), E213 (= E238), R219 (= R244), H220 (= H245), E357 (= E399), G360 (≠ T402), R408 (= R450)
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E168 (= E192), S188 (= S212), Q190 (= Q214), R211 (= R236), H220 (= H245), L221 (= L246), F224 (= F249), H226 (≠ S251), E228 (≠ D253), E357 (= E399), I358 (≠ V400), I359 (≠ A401), R364 (= R406), F402 (≠ A444), G403 (= G445), G405 (= G447), R408 (= R450)
1x54A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate (see paper)
34% identity, 92% coverage: 41:476/476 of query aligns to 16:434/434 of 1x54A
- active site: R211 (= R236), E213 (= E238), R219 (= R244), H220 (= H245), E357 (= E399), G360 (≠ T402), R408 (= R450)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E168 (= E192), S188 (= S212), Q190 (= Q214), R211 (= R236), H220 (= H245), L221 (= L246), F224 (= F249), H226 (≠ S251), E228 (≠ D253), E357 (= E399), I358 (≠ V400), I359 (≠ A401), R364 (= R406), F402 (≠ A444), G403 (= G445), G405 (= G447), R408 (= R450)
3kfuC Crystal structure of the transamidosome (see paper)
36% identity, 91% coverage: 37:469/476 of query aligns to 9:377/377 of 3kfuC
- active site: E307 (= E399), S310 (≠ T402), R358 (= R450)
- binding : W24 (≠ A52), R26 (= R54), L28 (≠ H56), R30 (≠ G58), F33 (= F61), Q44 (= Q72), N68 (≠ S105), K70 (≠ A107), E76 (= E113), P93 (= P129), E95 (= E131), R102 (vs. gap), N104 (≠ S138), T107 (≠ I141)
8tc9A Human asparaginyl-tRNA synthetase bound to osm-s-106 (see paper)
28% identity, 92% coverage: 37:476/476 of query aligns to 12:434/434 of 8tc9A
- binding N~1~-[(3M)-3-(4-aminothieno[3,2-d]pyrimidin-6-yl)benzene-1-sulfonyl]-L-aspartamide: E165 (= E192), S185 (= S212), Q187 (= Q214), R208 (= R236), H217 (= H245), L218 (= L246), Y221 (≠ F249), H223 (≠ S251), E225 (≠ D253), R364 (= R411), Y402 (≠ A444), G403 (= G445), R408 (= R450)
8tc8A Human asparaginyl-tRNA synthetase bound to adenosine 5'-sulfamate (see paper)
28% identity, 92% coverage: 37:476/476 of query aligns to 12:435/435 of 8tc8A
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E166 (= E192), S186 (= S212), Q188 (= Q214), R209 (= R236), E211 (= E238), H218 (= H245), L219 (= L246), Y222 (≠ F249), H224 (≠ S251), E226 (≠ D253), E358 (≠ V400), I359 (≠ A401), V360 (≠ T402), R365 (= R411), Y403 (≠ A444), G404 (= G445), G406 (= G447)
8h53A Human asparaginyl-tRNA synthetase in complex with asparagine-amp (see paper)
28% identity, 92% coverage: 37:476/476 of query aligns to 10:427/427 of 8h53A
- binding imidodiphosphoric acid: R209 (= R244), H210 (= H245), E350 (≠ V400), R401 (= R450)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E158 (= E192), S178 (= S212), Q180 (= Q214), R201 (= R236), L211 (= L246), Y214 (≠ F249), H216 (≠ S251), E218 (≠ D253), E350 (≠ V400), I351 (≠ A401), V352 (≠ T402), R357 (= R411), Y395 (≠ A444), G396 (= G445), G398 (= G447), R401 (= R450)
2xtiA Asparaginyl-tRNA synthetase from brugia malayi complexed with atp:mg and l-asp-beta-noh adenylate:ppi:mg (see paper)
28% identity, 90% coverage: 41:469/476 of query aligns to 13:426/433 of 2xtiA
- binding 5'-O-[(R)-{[(2S)-2-amino-4-(hydroxyamino)-4-oxobutanoyl]oxy}(hydroxy)phosphoryl]adenosine: E163 (= E192), S183 (= S212), Q185 (= Q214), R206 (= R236), E208 (= E238), H215 (= H245), L216 (= L246), Y219 (≠ F249), H221 (≠ S251), E223 (≠ D253), Y333 (= Y365), E356 (= E399), I357 (≠ V400), V358 (≠ A401), G359 (≠ T402), R363 (= R406), Y401 (≠ A444), G402 (= G445), G404 (= G447), R407 (= R450)
- binding pyrophosphate 2-: R214 (= R244), H215 (= H245), E356 (= E399), R407 (= R450)
2xgtB Asparaginyl-tRNA synthetase from brugia malayi complexed with the sulphamoyl analogue of asparaginyl-adenylate (see paper)
28% identity, 90% coverage: 41:469/476 of query aligns to 11:426/433 of 2xgtB
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E163 (= E192), S183 (= S212), Q185 (= Q214), R206 (= R236), E208 (= E238), H215 (= H245), L216 (= L246), Y219 (≠ F249), H221 (≠ S251), E223 (≠ D253), E356 (= E399), I357 (≠ V400), V358 (≠ A401), G359 (≠ T402), R363 (= R406), Y401 (≠ A444), G402 (= G445), G404 (= G447)
3m4pA Entamoeba histolytica asparaginyl-tRNA synthetase (asnrs) in complex with asparaginyl-adenylate
29% identity, 92% coverage: 38:476/476 of query aligns to 12:435/435 of 3m4pA
- active site: R211 (= R236), E213 (= E238), R219 (= R244), H220 (= H245), E358 (= E399), G361 (≠ T402), R409 (= R450)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: S188 (= S212), Q190 (= Q214), R211 (= R236), H220 (= H245), L221 (= L246), Y224 (≠ F249), H226 (≠ S251), E358 (= E399), I359 (≠ V400), V360 (≠ A401), R365 (= R406), Y403 (≠ A444), G404 (= G445), G406 (= G447), R409 (= R450)
Query Sequence
>WP_014026192.1 NCBI__GCF_000223395.1:WP_014026192.1
MRGRSGAGLTRRRVVLQRWVPGLLLEARRYIADVLREGRVGEKYVIAGWVEAVRRHGGVV
FVVVRDRSGRMQVVAKKNVAREAWETARELSRESVIAVKGVLVESKAALGGKELQAEEIL
VLNEAEPLPIEPGGKTASLAIRLRYRWIDLREPRHATPIIAAAVAAEAASKFFAEQGFIE
IFTPKIVASATEGGAEVFPIIYFEKEAFLAQSPQLYKQMGVISGLERVYEIGPAFRAEKH
HTVRHLTEFTSVDFEMGFIKSYEDVMKVVEGAVTAMIEAIQSDPRTKPLLEEYYPQALEL
KPPREYPRVPIDEAYRLLREAGLEIEEDEDLGTEGEKKLGEIYEKEYGAPLVFVTMYPWS
VRPFYTMKAREEPWSCPEEPRFTNPKRTYSFDLLFKGLEVATGGQREHCPRILEEQLREK
GLNPAAFDWYLEMFRHGAPPHGGAGIGLERVVMQLLGLGNIREARFVPRDPEHLKP
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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