SitesBLAST
Comparing WP_010875691.1 NCBI__GCF_000008645.1:WP_010875691.1 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)
3aiiA Archaeal non-discriminating glutamyl-tRNA synthetase from methanothermobacter thermautotrophicus (see paper)
97% identity, 84% coverage: 87:553/553 of query aligns to 1:455/455 of 3aiiA
4h3sA The structure of glutaminyl-tRNA synthetase from saccharomyces cerevisiae (see paper)
31% identity, 74% coverage: 95:502/553 of query aligns to 36:472/585 of 4h3sA
Q8CGC7 Bifunctional glutamate/proline--tRNA ligase; Bifunctional aminoacyl-tRNA synthetase; EC 6.1.1.17; EC 6.1.1.15 from Mus musculus (Mouse) (see 2 papers)
34% identity, 66% coverage: 89:452/553 of query aligns to 189:556/1512 of Q8CGC7
Sites not aligning to the query:
- 999 modified: Phosphoserine; by RPS6KB1; S→A: Loss of function in translation inhibition. Loss of interaction with SLC27A1. Mutant mice have no apparent developmental defect but display reduced adiposity associated with decreased insulin levels and adipocytes size. They also display increased lipolysis and fatty acid beta-oxidation and an extended lifespan. Adipocytes display decreased insulin-stimulated long-chain fatty acid uptake.; S→D: Constitutively active in translation inhibition (phosphomimetic). Mutant mice have no apparent developmental defect and do not display overt phenotype related to adiposity or lifespan.
P07814 Bifunctional glutamate/proline--tRNA ligase; Bifunctional aminoacyl-tRNA synthetase; Cell proliferation-inducing gene 32 protein; Glutamatyl-prolyl-tRNA synthetase; EC 6.1.1.17; EC 6.1.1.15 from Homo sapiens (Human) (see 13 papers)
34% identity, 68% coverage: 78:452/553 of query aligns to 179:556/1512 of P07814
- K300 (≠ R199) modified: N6-malonyllysine; alternate
- D308 (≠ E206) to E: in dbSNP:rs2230301
- Q334 (≠ G231) to H: in dbSNP:rs1063236
Sites not aligning to the query:
- 886 modified: Phosphoserine; by CDK5; S→A: Abolishes release from the aminoacyl-tRNA synthetase multienzyme complex and association with the GAIT complex upon interferon-gamma treatment. Abolishes interaction with SYNCRIP.; S→D: Not active in translation inhibition (phosphomimetic) and abolishes GAIT complex association with eiF4G. No effect on interaction with SYNCRIP.
- 999 modified: Phosphoserine; by RPS6KB1; S→A: Not active in translation inhibition, abolishes release from the aminoacyl-tRNA synthetase multienzyme complex and association with the GAIT complex upon interferon-gamma treatment.; S→D: Active in translation inhibition (phosphomimetic). No effect on GAIT complex association with eiF4G.
- 1043 I → V: in dbSNP:rs5030752
- 1097 F→A: Almost complete loss of prolyl-tRNA ligase activity.; F→W: No effect on prolyl-tRNA ligase activity. Decreases inhibition by halofuginone.
- 1115 P → R: in HLD15; slightly decreased protein level; does not affect multisynthetase complex assembly; dbSNP:rs1288116010
- 1121:1123 binding L-proline
- 1126 M → T: in HLD15; uncertain significance; small decrease in aminoacylation activity; dbSNP:rs1474000585
- 1152 binding ATP; binding L-proline; R→K: No effect on prolyl-tRNA ligase activity. Decreases inhibition by halofuginone.; R→L: Almost complete loss of prolyl-tRNA ligase activity.
- 1154 binding ATP
- 1160 P → S: in HLD15; uncertain significance; dbSNP:rs898824971
- 1163 binding ATP
- 1164 binding ATP
- 1237 binding ATP; binding Mg(2+)
- 1240 binding ATP
- 1242 binding L-proline
- 1276 binding ATP
- 1278 binding ATP
- 1448 binding Zn(2+)
- 1453 binding Zn(2+)
- 1495 binding Zn(2+)
- 1497 binding Zn(2+)
P28668 Bifunctional glutamate/proline--tRNA ligase; Bifunctional aminoacyl-tRNA synthetase; EC 6.1.1.17; EC 6.1.1.15 from Drosophila melanogaster (Fruit fly) (see 2 papers)
33% identity, 75% coverage: 32:448/553 of query aligns to 149:558/1714 of P28668
Sites not aligning to the query:
- 170:754 Glutamate--tRNA ligase
- 1110 modified: Phosphoserine
- 1207:1714 Proline--tRNA ligase
O13775 Probable glutamate--tRNA ligase, cytoplasmic; Glutamyl-tRNA synthetase; GluRS; EC 6.1.1.17 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
33% identity, 69% coverage: 69:452/553 of query aligns to 175:567/716 of O13775
- S190 (≠ R84) modified: Phosphoserine
2re8A Glutaminyl-tRNA synthetase mutant c229r with bound analog 5'-o-[n-(l- glutamyl)-sulfamoyl]adenosine (see paper)
31% identity, 82% coverage: 91:541/553 of query aligns to 14:510/529 of 2re8A
- binding o5'-(l-glutamyl-sulfamoyl)-adenosine: P25 (≠ A102), P26 (= P103), E27 (≠ N104), G35 (= G112), H36 (= H113), D59 (≠ E136), Y204 (≠ M274), H208 (≠ V278), R222 (= R292), T223 (≠ G293), R253 (= R322), L254 (= L323), K263 (≠ T332)
- binding : E27 (≠ N104), T61 (= T138), N62 (≠ D139), L117 (≠ C193), P119 (= P195), R123 (= R199), R126 (vs. gap), T128 (vs. gap), L129 (= L201), G161 (= G231), P174 (= P244), F175 (≠ N245), I176 (≠ P246), V182 (= V252), R185 (= R255), M203 (= M273), Y204 (≠ M274), F226 (≠ H296), D228 (≠ A298), I306 (= I375), T309 (≠ K378), K310 (≠ I379), Q311 (≠ A380), N313 (≠ S382), T314 (= T383), E316 (≠ S385), S319 (≠ K388), S322 (≠ G391), N329 (≠ E398), R334 (= R403), P362 (= P430), N363 (≠ D431), Q392 (vs. gap), K394 (vs. gap), R395 (vs. gap), R403 (= R459), R405 (≠ I461), N406 (≠ D462), L435 (= L486), Q499 (= Q530), E501 (= E532), R502 (= R533)
Sites not aligning to the query:
1o0cA Crystal structure of l-glutamate and ampcpp bound to glutamine aminoacyl tRNA synthetase (see paper)
31% identity, 82% coverage: 91:541/553 of query aligns to 14:510/529 of 1o0cA
- binding adenosine monophosphate: F24 (= F101), P26 (= P103), H33 (= H110), G35 (= G112), H36 (= H113), S39 (≠ A116), T223 (≠ G293), R253 (= R322), L254 (= L323), K263 (≠ T332)
- binding glutamic acid: R23 (= R100), Y204 (≠ M274), H208 (≠ V278), C222 (≠ R292)
- binding : E27 (≠ N104), T61 (= T138), N62 (≠ D139), P119 (= P195), R123 (= R199), R126 (vs. gap), T128 (vs. gap), L129 (= L201), T130 (≠ K202), G161 (= G231), P174 (= P244), F175 (≠ N245), I176 (≠ P246), R185 (= R255), K187 (≠ V257), M203 (= M273), Y204 (≠ M274), F226 (≠ H296), Q227 (≠ L297), D228 (≠ A298), R231 (≠ E301), I306 (= I375), T309 (≠ K378), K310 (≠ I379), Q311 (≠ A380), N313 (≠ S382), T314 (= T383), E316 (≠ S385), A318 (≠ K387), S319 (≠ K388), S322 (≠ G391), N329 (≠ E398), R334 (= R403), P362 (= P430), Q392 (vs. gap), K394 (vs. gap), R395 (vs. gap), R403 (= R459), R405 (≠ I461), N406 (≠ D462), L435 (= L486), Q499 (= Q530), E501 (= E532), R502 (= R533)
Sites not aligning to the query:
1o0bA Crystal structure of l-glutamine and ampcpp bound to glutamine aminoacyl tRNA synthetase (see paper)
31% identity, 82% coverage: 91:541/553 of query aligns to 14:510/529 of 1o0bA
- binding adenosine monophosphate: F24 (= F101), P26 (= P103), H33 (= H110), G35 (= G112), H36 (= H113), S39 (≠ A116), R253 (= R322), L254 (= L323)
- binding glutamine: P25 (≠ A102), D59 (≠ E136), Y204 (≠ M274), H208 (≠ V278), C222 (≠ R292), F226 (≠ H296)
- binding : E27 (≠ N104), D59 (≠ E136), T61 (= T138), N62 (≠ D139), P119 (= P195), R123 (= R199), R126 (vs. gap), T128 (vs. gap), L129 (= L201), T130 (≠ K202), G161 (= G231), P174 (= P244), F175 (≠ N245), I176 (≠ P246), V182 (= V252), R185 (= R255), K187 (≠ V257), M203 (= M273), Y204 (≠ M274), F226 (≠ H296), Q227 (≠ L297), D228 (≠ A298), R231 (≠ E301), I306 (= I375), T309 (≠ K378), K310 (≠ I379), Q311 (≠ A380), D312 (= D381), N313 (≠ S382), T314 (= T383), E316 (≠ S385), A318 (≠ K387), S322 (≠ G391), N329 (≠ E398), R334 (= R403), P362 (= P430), N363 (≠ D431), Q392 (vs. gap), K394 (vs. gap), R395 (vs. gap), R403 (= R459), R405 (≠ I461), N406 (≠ D462), L435 (= L486), V437 (≠ M490), Q499 (= Q530), E501 (= E532), R502 (= R533)
Sites not aligning to the query:
1gtsA Structural basis for transfer RNA aminoaceylation by escherichia coli glutaminyl-tRNA synthetase (see paper)
31% identity, 82% coverage: 91:541/553 of query aligns to 14:510/529 of 1gtsA
- binding adenosine monophosphate: E27 (≠ N104), G35 (= G112), H36 (= H113), S39 (≠ A116), T223 (≠ G293), R253 (= R322), L254 (= L323), K263 (≠ T332)
- binding : E27 (≠ N104), D59 (≠ E136), T61 (= T138), N62 (≠ D139), P119 (= P195), R126 (vs. gap), L129 (= L201), G161 (= G231), P174 (= P244), F175 (≠ N245), I176 (≠ P246), V182 (= V252), R185 (= R255), K187 (≠ V257), M203 (= M273), Y204 (≠ M274), F226 (≠ H296), Q227 (≠ L297), D228 (≠ A298), I306 (= I375), T309 (≠ K378), K310 (≠ I379), Q311 (≠ A380), N313 (≠ S382), T314 (= T383), E316 (≠ S385), A318 (≠ K387), S322 (≠ G391), N329 (≠ E398), R334 (= R403), Q392 (vs. gap), Y393 (vs. gap), K394 (vs. gap), R395 (vs. gap), R403 (= R459), R405 (≠ I461), N406 (≠ D462), V437 (≠ M490), E501 (= E532), R502 (= R533)
Sites not aligning to the query:
1exdA Crystal structure of a tight-binding glutamine tRNA bound to glutamine aminoacyl tRNA synthetase (see paper)
31% identity, 82% coverage: 91:541/553 of query aligns to 14:510/529 of 1exdA
- active site: E27 (≠ N104), R253 (= R322), K263 (≠ T332)
- binding adenosine-5'-monophosphate: F24 (= F101), P26 (= P103), E27 (≠ N104), G35 (= G112), H36 (= H113), S39 (≠ A116), R253 (= R322), L254 (= L323), K263 (≠ T332)
- binding sulfate ion: V260 (≠ A329), M261 (≠ L330), S262 (= S331), K265 (≠ G334)
- binding : E27 (≠ N104), D59 (≠ E136), T61 (= T138), N62 (≠ D139), P119 (= P195), R123 (= R199), R126 (vs. gap), L129 (= L201), T130 (≠ K202), G161 (= G231), P174 (= P244), F175 (≠ N245), I176 (≠ P246), V182 (= V252), R185 (= R255), K187 (≠ V257), M203 (= M273), Y204 (≠ M274), F226 (≠ H296), Q227 (≠ L297), D228 (≠ A298), I306 (= I375), T309 (≠ K378), K310 (≠ I379), Q311 (≠ A380), D312 (= D381), N313 (≠ S382), T314 (= T383), E316 (≠ S385), A318 (≠ K387), S319 (≠ K388), S322 (≠ G391), N329 (≠ E398), R334 (= R403), P362 (= P430), Q392 (vs. gap), K394 (vs. gap), R395 (vs. gap), R403 (= R459), R405 (≠ I461), N406 (≠ D462), V437 (≠ M490), Q499 (= Q530), E501 (= E532), R502 (= R533)
Sites not aligning to the query:
1euqA Crystal structure of glutaminyl-tRNA synthetase complexed with a tRNA- gln mutant and an active-site inhibitor (see paper)
31% identity, 82% coverage: 91:541/553 of query aligns to 14:510/529 of 1euqA
- active site: E27 (≠ N104), R253 (= R322), K263 (≠ T332)
- binding 5'-o-[n-(l-glutaminyl)-sulfamoyl]adenosine: P26 (= P103), H33 (= H110), G35 (= G112), H36 (= H113), S39 (≠ A116), Y204 (≠ M274), H208 (≠ V278), C222 (≠ R292), F226 (≠ H296), R253 (= R322), K263 (≠ T332)
- binding : E27 (≠ N104), D59 (≠ E136), T61 (= T138), N62 (≠ D139), P119 (= P195), R123 (= R199), R126 (vs. gap), L129 (= L201), G161 (= G231), C164 (≠ V234), P174 (= P244), F175 (≠ N245), I176 (≠ P246), V182 (= V252), R185 (= R255), K187 (≠ V257), M203 (= M273), Y204 (≠ M274), F226 (≠ H296), I306 (= I375), T309 (≠ K378), K310 (≠ I379), Q311 (≠ A380), N313 (≠ S382), T314 (= T383), E316 (≠ S385), A318 (≠ K387), S322 (≠ G391), N329 (≠ E398), R334 (= R403), N363 (≠ D431), Q392 (vs. gap), K394 (vs. gap), R403 (= R459), R405 (≠ I461), N406 (≠ D462), V437 (≠ M490), Q499 (= Q530), E501 (= E532), R502 (= R533)
Sites not aligning to the query:
P00962 Glutamine--tRNA ligase; Glutaminyl-tRNA synthetase; GlnRS; EC 6.1.1.18 from Escherichia coli (strain K12) (see 7 papers)
30% identity, 82% coverage: 91:541/553 of query aligns to 22:529/554 of P00962
- R31 (= R100) mutation R->A,K: Decreased affinity for glutamine and catalytic activity.
- EPN 35:37 (≠ NPS 104:106) binding ATP
- 41:47 (vs. 110:116, 71% identical) binding ATP
- D67 (≠ E136) binding L-glutamine
- Y212 (≠ M274) binding L-glutamine
- C230 (≠ R292) mutation to R: Decreases catalytic activity 1000-fold, but has no effect on affinity for glutamine. Loss of catalytic activity; when associated with I-256.
- T231 (≠ G293) binding ATP
- Q256 (≠ F317) mutation to I: Loss of catalytic activity; when associated with R-230.
- RL 261:262 (= RL 322:323) binding ATP
- MSK 269:271 (≠ LST 330:332) binding ATP
- 317:324 (vs. 378:385, 25% identical) Interaction with tRNA
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P46655 Glutamate--tRNA ligase, cytoplasmic; Glutamyl-tRNA synthetase; (c)ERS; GluRS; P85; EC 6.1.1.17 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
28% identity, 82% coverage: 95:549/553 of query aligns to 200:693/708 of P46655
Sites not aligning to the query:
- 148 R→A: Abolishes interaction with ARC1.
4jyzA Crystal structure of e. Coli glutaminyl-tRNA synthetase bound to atp and native tRNA(gln) containing the cmnm5s2u34 anticodon wobble base (see paper)
30% identity, 82% coverage: 91:541/553 of query aligns to 15:522/542 of 4jyzA
- active site: E28 (≠ N104), R254 (= R322), K264 (≠ T332)
- binding adenosine-5'-triphosphate: H34 (= H110), G36 (= G112), H37 (= H113), S40 (≠ A116), T224 (≠ G293), R254 (= R322), L255 (= L323), M262 (≠ L330), K264 (≠ T332)
- binding : E28 (≠ N104), T62 (= T138), N63 (≠ D139), P120 (= P195), R124 (= R199), R127 (vs. gap), T129 (vs. gap), L130 (= L201), G162 (= G231), C165 (≠ V234), P175 (= P244), F176 (≠ N245), I177 (≠ P246), V183 (= V252), R186 (= R255), K188 (≠ V257), M204 (= M273), Y205 (≠ M274), F227 (≠ H296), Q228 (≠ L297), D229 (≠ A298), R232 (≠ E301), I307 (= I375), T310 (≠ K378), K311 (≠ I379), Q312 (≠ A380), D313 (= D381), N314 (≠ S382), T315 (= T383), E317 (≠ S385), A319 (≠ K387), S320 (≠ K388), S323 (≠ G391), N330 (≠ E398), R335 (= R403), N364 (≠ D431), Q393 (vs. gap), K395 (vs. gap), R396 (vs. gap), R404 (= R459), R406 (≠ I461), S437 (= S477), K438 (≠ E478), V449 (≠ M490), Q511 (= Q530), E513 (= E532), R514 (= R533)
Sites not aligning to the query:
8uk6A Candida albicans glutaminyl tRNA synthetase (gln4) in complex with n- pyrimidinyl-beta-thiophenylacrylamide (see paper)
31% identity, 66% coverage: 93:457/553 of query aligns to 35:407/573 of 8uk6A
5zdkA Crystal structure analysis of ttqrs in complex with atp (see paper)
32% identity, 80% coverage: 92:536/553 of query aligns to 20:521/543 of 5zdkA
- binding adenosine-5'-triphosphate: F29 (= F101), P31 (= P103), E32 (≠ N104), G40 (= G112), H41 (= H113), T223 (≠ G293), R259 (= R322), L260 (= L323)
- binding cesium ion: W366 (≠ H429), P367 (= P430), I370 (≠ H432), E373 (≠ I435)
7waoA Glutamyl-tRNA synthetase from plasmodium falciparum (pfers) in complex with mn (see paper)
31% identity, 62% coverage: 92:436/553 of query aligns to 5:355/502 of 7waoA
Sites not aligning to the query:
P47897 Glutamine--tRNA ligase; Glutaminyl-tRNA synthetase; GlnRS; EC 6.1.1.18 from Homo sapiens (Human) (see 2 papers)
29% identity, 70% coverage: 73:457/553 of query aligns to 242:623/775 of P47897
- R403 (= R236) to W: in MSCCA; results in loss of glutaminyl-tRNA aminoacylation activity; impairs protein folding; does not interact with RARS1; results in reduced protein solubility; dbSNP:rs587777332
- R515 (= R351) to W: in MSCCA; results in loss of glutaminyl-tRNA aminoacylation activity; impairs protein folding; results in reduced protein solubility; dbSNP:rs587777334
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 45 G → V: in MSCCA; results in reduced glutaminyl-tRNA aminoacylation activity; does not affect interaction with RARS1; dbSNP:rs587777331
- 57 Y → H: in MSCCA; results in reduced glutaminyl-tRNA aminoacylation activity; does not affect interaction with RARS1; dbSNP:rs587777333
- 175 H→A: Decreases catalytic efficiency about 60-fold.
7wajA Glutamyl-tRNA synthetase from plasmodium falciparum (pfers) complexed with atp and co (see paper)
27% identity, 82% coverage: 92:544/553 of query aligns to 5:480/492 of 7wajA
Sites not aligning to the query:
Query Sequence
>WP_010875691.1 NCBI__GCF_000008645.1:WP_010875691.1
MVPVEDLVYRYALLNAVKHRGRANPGAVMGAVMSNEPELRKMAPQVKEAVEAAVERVNSL
SPEEQQQEMERLGLEITERKQKKRKGLRELAGVKGEVVLRFAPNPSGPLHIGHARAAILN
HEYARKYDGRLILRIEDTDPRRVDPEAYDMIPADLEWLGVEWDETVIQSDRMETYYEYTE
KLIERGGAYVCTCRPEEFRELKNRGEACHCRSLGFRENLQRWREMFEMKEGSAVVRVKTD
LNHPNPAIRDWVSMRIVEAEHPRTGTRYRVYPMMNFSVAVDDHLLGVTHVLRGKDHLANR
EKQEYLYRHLGWEPPEFIHYGRLKMDDVALSTSGAREGILRGEYSGWDDPRLGTLRAIAR
RGIRPEAIRKLMVEIGVKIADSTMSWKKIYGLNRSILEEEARRYFFAADPVKLEVVGLPG
PVRVERPLHPDHPEIGNRVLELRGEVYLPGDDLGEGPLRLIDAVNVIYSGGELRYHSEGI
EEARELGASMIHWVPAESALEAEVIMPDASRVRGVIEADASELEVDDVVQLERFGFARLD
SAGPGMVFYYAHK
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