SitesBLAST
Comparing WP_011869534.1 NCBI__GCF_000016125.1:WP_011869534.1 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)
51% identity, 98% coverage: 9:438/438 of query aligns to 3:438/438 of 3nemB
- active site: R214 (= R220), E216 (= E222), R222 (= R228), H223 (= H229), E361 (= E361), S364 (= S364), R412 (= R412)
- binding adenosine-5'-triphosphate: R214 (= R220), E216 (= E222), H223 (= H229), L224 (= L230), E361 (= E361), I362 (= I362), S363 (= S363), S364 (= S364), G407 (= G407), G409 (= G409), R412 (= R412)
- binding magnesium ion: E361 (= E361), S364 (= S364)
3nemA Aspartyl-tRNA synthetase complexed with aspartyl adenylate (see paper)
51% identity, 98% coverage: 9:438/438 of query aligns to 3:438/438 of 3nemA
- active site: R214 (= R220), E216 (= E222), R222 (= R228), H223 (= H229), E361 (= E361), S364 (= S364), R412 (= R412)
- binding aspartyl-adenosine-5'-monophosphate: E170 (= E176), Q192 (= Q198), K195 (= K201), R214 (= R220), E216 (= E222), H223 (= H229), L224 (= L230), Y339 (= Y339), E361 (= E361), I362 (= I362), S363 (= S363), S364 (= S364), G365 (= G365), R368 (= R368), F406 (≠ W406), G407 (= G407), G409 (= G409), R412 (= R412)
3nelA Aspartyl-tRNA synthetase complexed with aspartic acid (see paper)
51% identity, 98% coverage: 9:438/438 of query aligns to 3:438/438 of 3nelA
- active site: R214 (= R220), E216 (= E222), R222 (= R228), H223 (= H229), E361 (= E361), S364 (= S364), R412 (= R412)
- binding aspartic acid: E170 (= E176), Q192 (= Q198), K195 (= K201), Y339 (= Y339), S364 (= S364), R368 (= R368), F406 (≠ W406), G407 (= G407)
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)
51% identity, 98% coverage: 9:438/438 of query aligns to 3:438/438 of Q52428
- W26 (≠ H32) 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 (≠ P91) 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)
50% identity, 98% coverage: 9:438/438 of query aligns to 3:438/438 of 1b8aA
- binding adenosine-5'-triphosphate: R214 (= R220), E216 (= E222), H223 (= H229), L224 (= L230), E361 (= E361), I362 (= I362), S363 (= S363), S364 (= S364), G409 (= G409), R412 (= R412)
- binding manganese (ii) ion: E361 (= E361), S364 (= S364)
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)
38% identity, 97% coverage: 12:438/438 of query aligns to 6:436/436 of O07683
- H26 (= H32) mutation H->A,Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn).
- P84 (= P91) mutation P->A,K: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn), by decreasing the ability to form Asp-tRNA(Asn).
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)
38% identity, 96% coverage: 17:438/438 of query aligns to 13:435/435 of Q9RVH4
- H28 (= H32) mutation to Q: Enhances enzyme specificity for tRNA(Asp) over tRNA(Asn).
- P77 (= P91) 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)
38% identity, 97% coverage: 12:438/438 of query aligns to 6:434/434 of 1x55A
- active site: R211 (= R220), E213 (= E222), R219 (= R228), H220 (= H229), E357 (= E361), G360 (≠ S364), R408 (= R412)
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E168 (= E176), S188 (= S196), Q190 (= Q198), R211 (= R220), H220 (= H229), L221 (= L230), F224 (≠ A233), H226 (≠ S235), E228 (≠ D237), E357 (= E361), I358 (= I362), I359 (≠ S363), R364 (= R368), F402 (≠ W406), G403 (= G407), G405 (= G409), R408 (= R412)
1x54A Crystal structure of asparaginyl-tRNA synthetase from pyrococcus horikoshii complexed with asparaginyl-adenylate (see paper)
38% identity, 97% coverage: 12:438/438 of query aligns to 6:434/434 of 1x54A
- active site: R211 (= R220), E213 (= E222), R219 (= R228), H220 (= H229), E357 (= E361), G360 (≠ S364), R408 (= R412)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E168 (= E176), S188 (= S196), Q190 (= Q198), R211 (= R220), H220 (= H229), L221 (= L230), F224 (≠ A233), H226 (≠ S235), E228 (≠ D237), E357 (= E361), I358 (= I362), I359 (≠ S363), R364 (= R368), F402 (≠ W406), G403 (= G407), G405 (= G409), R408 (= R412)
1aszA The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction (see paper)
33% identity, 95% coverage: 23:438/438 of query aligns to 40:490/490 of 1aszA
- active site: R258 (= R220), E260 (= E222), R266 (= R228), H267 (= H229), E411 (= E361), S414 (= S364), R464 (= R412)
- binding adenosine-5'-triphosphate: R258 (= R220), M268 (≠ L230), F271 (≠ A233), E411 (= E361), I412 (= I362), L413 (≠ S363), G459 (= G407), R464 (= R412)
- binding : R52 (= R35), Q53 (≠ A36), Q54 (≠ L37), T57 (≠ K39), L58 (= L40), F60 (= F42), Q71 (= Q53), L73 (≠ V55), E110 (≠ K89), I112 (≠ P91), K113 (= K92), E135 (≠ A109), P138 (= P112), L140 (vs. gap), A154 (vs. gap), L156 (vs. gap), P157 (vs. gap), V158 (vs. gap), N160 (vs. gap), T163 (= T125), S213 (≠ T175), E214 (= E176), G215 (= G177), G216 (= G178), S217 (≠ T179), Q233 (= Q195), F237 (≠ L199), E260 (= E222), N261 (≠ E223), S262 (≠ H224), N263 (= N225), H267 (= H229), S356 (= S311), T357 (≠ R312), F388 (= F338), K486 (≠ Q434)
1asyA Class ii aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA asp (see paper)
33% identity, 95% coverage: 23:438/438 of query aligns to 40:490/490 of 1asyA
- active site: R258 (= R220), E260 (= E222), R266 (= R228), H267 (= H229), E411 (= E361), S414 (= S364), R464 (= R412)
- binding : R52 (= R35), Q53 (≠ A36), Q54 (≠ L37), L58 (= L40), F60 (= F42), Q71 (= Q53), L73 (≠ V55), K88 (≠ A67), P111 (≠ A90), I112 (≠ P91), K113 (= K92), S114 (≠ G93), E135 (≠ A109), P138 (= P112), A154 (vs. gap), L156 (vs. gap), P157 (vs. gap), V158 (vs. gap), V159 (vs. gap), D162 (= D124), T163 (= T125), R258 (= R220), E260 (= E222), N261 (≠ E223), S262 (≠ H224), N263 (= N225), T264 (= T226), H267 (= H229), M268 (≠ L230), F271 (≠ A233), T357 (≠ R312), E411 (= E361), I412 (= I362), L413 (≠ S363), S414 (= S364), G459 (= G407), R464 (= R412), K486 (≠ Q434)
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)
33% identity, 95% coverage: 23:438/438 of query aligns to 107:557/557 of P04802
- P273 (= P168) mutation to G: Loss of activity; important for dimerization.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
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, 95% coverage: 21:438/438 of query aligns to 103:580/580 of O74407
- S282 (≠ V171) modified: Phosphoserine
- S307 (= S196) modified: Phosphoserine
3kfuC Crystal structure of the transamidosome (see paper)
35% identity, 94% coverage: 22:431/438 of query aligns to 13:377/377 of 3kfuC
- active site: E307 (= E361), S310 (= S364), R358 (= R412)
- binding : W24 (≠ S33), R26 (= R35), L28 (= L37), R30 (≠ K39), F33 (= F42), Q44 (= Q53), N68 (= N87), K70 (= K89), E76 (= E95), P93 (= P112), E95 (≠ D114), R102 (≠ A120), N104 (≠ E122), T107 (= T125)
8tc9A Human asparaginyl-tRNA synthetase bound to osm-s-106 (see paper)
31% identity, 95% coverage: 22:438/438 of query aligns to 16:434/434 of 8tc9A
- binding N~1~-[(3M)-3-(4-aminothieno[3,2-d]pyrimidin-6-yl)benzene-1-sulfonyl]-L-aspartamide: E165 (= E176), S185 (= S196), Q187 (= Q198), R208 (= R220), H217 (= H229), L218 (= L230), Y221 (≠ A233), H223 (≠ S235), E225 (≠ D237), R364 (= R368), Y402 (≠ W406), G403 (= G407), R408 (= R412)
8h53A Human asparaginyl-tRNA synthetase in complex with asparagine-amp (see paper)
31% identity, 95% coverage: 22:438/438 of query aligns to 14:427/427 of 8h53A
- binding imidodiphosphoric acid: R209 (= R228), H210 (= H229), E350 (= E361), R401 (= R412)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: E158 (= E176), S178 (= S196), Q180 (= Q198), R201 (= R220), L211 (= L230), Y214 (≠ A233), H216 (≠ S235), E218 (≠ D237), E350 (= E361), I351 (= I362), V352 (≠ S363), R357 (= R368), Y395 (≠ W406), G396 (= G407), G398 (= G409), R401 (= R412)
8tc8A Human asparaginyl-tRNA synthetase bound to adenosine 5'-sulfamate (see paper)
31% identity, 95% coverage: 22:438/438 of query aligns to 16:435/435 of 8tc8A
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E166 (= E176), S186 (= S196), Q188 (= Q198), R209 (= R220), E211 (= E222), H218 (= H229), L219 (= L230), Y222 (≠ A233), H224 (≠ S235), E226 (≠ D237), E358 (= E361), I359 (= I362), V360 (≠ S363), R365 (= R368), Y403 (≠ W406), G404 (= G407), G406 (= G409)
2xgtB Asparaginyl-tRNA synthetase from brugia malayi complexed with the sulphamoyl analogue of asparaginyl-adenylate (see paper)
33% identity, 95% coverage: 23:438/438 of query aligns to 12:433/433 of 2xgtB
- binding 5'-o-[n-(l-asparaginyl)sulfamoyl]adenosine: E163 (= E176), S183 (= S196), Q185 (= Q198), R206 (= R220), E208 (= E222), H215 (= H229), L216 (= L230), Y219 (≠ A233), H221 (≠ S235), E223 (≠ D237), E356 (= E361), I357 (= I362), V358 (≠ S363), G359 (≠ S364), R363 (= R368), Y401 (≠ W406), G402 (= G407), G404 (= G409)
2xtiA Asparaginyl-tRNA synthetase from brugia malayi complexed with atp:mg and l-asp-beta-noh adenylate:ppi:mg (see paper)
33% identity, 95% coverage: 23:438/438 of query aligns to 14:433/433 of 2xtiA
- binding 5'-O-[(R)-{[(2S)-2-amino-4-(hydroxyamino)-4-oxobutanoyl]oxy}(hydroxy)phosphoryl]adenosine: E163 (= E176), S183 (= S196), Q185 (= Q198), R206 (= R220), E208 (= E222), H215 (= H229), L216 (= L230), Y219 (≠ A233), H221 (≠ S235), E223 (≠ D237), Y333 (= Y339), E356 (= E361), I357 (= I362), V358 (≠ S363), G359 (≠ S364), R363 (= R368), Y401 (≠ W406), G402 (= G407), G404 (= G409), R407 (= R412)
- binding pyrophosphate 2-: R214 (= R228), H215 (= H229), E356 (= E361), R407 (= R412)
3m4pA Entamoeba histolytica asparaginyl-tRNA synthetase (asnrs) in complex with asparaginyl-adenylate
30% identity, 96% coverage: 20:438/438 of query aligns to 13:435/435 of 3m4pA
- active site: R211 (= R220), E213 (= E222), R219 (= R228), H220 (= H229), E358 (= E361), G361 (≠ S364), R409 (= R412)
- binding 4-amino-1,4-dioxobutan-2-aminium adenosine-5'-monophosphate: S188 (= S196), Q190 (= Q198), R211 (= R220), H220 (= H229), L221 (= L230), Y224 (≠ A233), H226 (≠ S235), E358 (= E361), I359 (= I362), V360 (≠ S363), R365 (= R368), Y403 (≠ W406), G404 (= G407), G406 (= G409), R409 (= R412)
Query Sequence
>WP_011869534.1 NCBI__GCF_000016125.1:WP_011869534.1
MYLIADWRRTHYSEEVIPEMDGQEVILMGWVHSIRALGKLAFVILRDREGTIQAVVPKQK
VDEETFAIAKKLGKEDIIAIRGKVVANEKAPKGFEVIPIEIRVLNKADAPLPLDPSEKVA
AEIDTRLDKRFLDIRRPKIQAIFKIRSEMLRSIRKTFADGGFVEVNTPKLVASATEGGTE
LFPISYFEKEAFLGQSPQLYKQMMMAGGFDKVFEIAQIFRAEEHNTRRHLNEAISIDTEM
SFVNEKDAMAMLEKVVYNCYADIEYNRPQEIELLELNWEIPEKTFDKITYTEAIDIANAK
GVEIEWGEDLSRAAERAVGDEMGGLYFITEWPTQTRPFYTLPHKHDNKVCKAFDLMYKEL
EISSGAQRVHKYDLLVENISNMGMNPDSFETYLEAFKFGMPPHAGWGLGADRFAMVLTAQ
DNIRECVLFPRDRQRLTP
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