SitesBLAST
Comparing Echvi_1262 FitnessBrowser__Cola:Echvi_1262 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 11 hits to proteins with known functional sites (download)
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
28% identity, 70% coverage: 27:444/598 of query aligns to 29:425/497 of 1ct9A
- active site: L50 (= L49), N74 (= N74), G75 (= G75), T305 (≠ V336), R308 (≠ S339), E332 (≠ A362), M366 (≠ K384)
- binding adenosine monophosphate: L232 (= L257), L233 (= L258), S234 (= S259), S239 (= S264), A255 (≠ T283), V256 (≠ A284), D263 (= D296), M316 (≠ I347), S330 (= S360), G331 (= G361), E332 (≠ A362)
- binding glutamine: R49 (= R48), L50 (= L49), I52 (≠ T51), V53 (= V52), N74 (= N74), G75 (= G75), E76 (≠ A76), D98 (= D99)
Sites not aligning to the query:
P22106 Asparagine synthetase B [glutamine-hydrolyzing]; AS-B; EC 6.3.5.4 from Escherichia coli (strain K12) (see 2 papers)
28% identity, 70% coverage: 27:444/598 of query aligns to 30:445/554 of P22106
- H30 (= H27) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D31) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ A80) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ R105) mutation to H: Little effect on the kinetic properties.
- E349 (≠ A362) mutation E->A,Q: Loss of glutamine- and ammonia-dependent synthetase activity, but still exhibits glutaminase activity.; mutation to D: 5-fold increase in affinity for aspartate when assaying both the glutamine- and ammonia-dependent synthetase reactions, and 2-fold decrease in kcat for these reactions. Modifies the product glutamate/asparagine stoichiometry.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 mutation C->A,S: Loss of glutamine-dependent activity but no effect on ammonia-dependent asparagine synthetase activity.
6gq3A Human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1.85 a resolution (see paper)
27% identity, 62% coverage: 2:371/598 of query aligns to 1:361/509 of 6gq3A
- active site: W4 (≠ M8), L49 (= L49), N74 (= N74), G75 (= G75), T324 (≠ V336), R327 (≠ S339)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R48), V51 (≠ T51), V52 (= V52), Y73 (≠ W73), N74 (= N74), G75 (= G75), E76 (≠ A76), V95 (≠ S98), D96 (= D99)
P78753 Probable asparagine synthetase [glutamine-hydrolyzing]; Glutamine-dependent asparagine synthetase; EC 6.3.5.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
28% identity, 75% coverage: 1:447/598 of query aligns to 1:455/557 of P78753
- S391 (≠ A385) modified: Phosphoserine
Sites not aligning to the query:
- 489 modified: Phosphoserine
P08243 Asparagine synthetase [glutamine-hydrolyzing]; Cell cycle control protein TS11; Glutamine-dependent asparagine synthetase; EC 6.3.5.4 from Homo sapiens (Human) (see 7 papers)
27% identity, 62% coverage: 1:371/598 of query aligns to 1:374/561 of P08243
- C2 (= C2) active site, For GATase activity; mutation to A: Loss of the glutamine-dependent asparagine synthetase activity, while the ammonia-dependent activity remained unaffected.
- A6 (≠ N9) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
- V210 (≠ I223) to E: in dbSNP:rs1049674
- F362 (≠ I359) to V: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122973
Sites not aligning to the query:
- 550 R → C: in ASNSD; increases level of protein abundance; dbSNP:rs398122974
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
24% identity, 64% coverage: 26:406/598 of query aligns to 22:385/496 of 1mbzA
- active site: A69 (≠ N74), G70 (= G75), D311 (= D338), Y337 (≠ A362), E371 (≠ V393)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ L257), L237 (= L258), S238 (= S259), S243 (= S264), S261 (≠ R285), M262 (≠ F286), Y315 (≠ F342), L319 (≠ M346), G336 (= G361), Y337 (≠ A362), G338 (= G363), D340 (= D365), I341 (≠ E366), D362 (≠ K384), E371 (≠ V393)
- binding magnesium ion: D242 (= D263), D340 (= D365)
- binding pyrophosphate 2-: S238 (= S259), G240 (= G261), D242 (= D263), S243 (= S264), D340 (= D365)
Sites not aligning to the query:
P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
30% identity, 23% coverage: 25:160/598 of query aligns to 53:205/476 of P00497
Sites not aligning to the query:
- 1:11 modified: propeptide
- 12 active site, Nucleophile; C→F: Loss of enzyme activity and N-terminal processing.
- 247 binding
- 294 binding
- 356 binding
- 357 binding
- 393 binding
- 394 F→V: Partial loss of activity.
- 442 D→S: Partial loss of activity.
- 448 binding ; C→S: Loss of activity.
- 451 binding ; C→S: Loss of activity.
- 452 F→C: Lethal.
1gph1 Structure of the allosteric regulatory enzyme of purine biosynthesis (see paper)
30% identity, 23% coverage: 25:160/598 of query aligns to 42:194/465 of 1gph1
Sites not aligning to the query:
- active site: 300, 305, 315, 423
- binding adenosine monophosphate: 242, 242, 244, 245, 246, 282, 283, 283, 304, 305, 307, 345, 346, 347, 349, 350, 353, 388
- binding iron/sulfur cluster: 236, 237, 382, 384, 388, 437, 440
1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
30% identity, 23% coverage: 25:161/598 of query aligns to 42:191/455 of 1ao0A
Sites not aligning to the query:
- active site: 1, 27, 238, 296, 301, 311, 419
- binding guanosine-5'-monophosphate: 234, 238, 279, 341, 342, 343, 345, 346, 347, 348, 349
- binding adenosine-5'-diphosphate: 25, 238, 240, 241, 242, 277, 278, 279, 300, 301, 301, 303
- binding magnesium ion: 279, 341, 342
- binding iron/sulfur cluster: 232, 233, 234, 378, 380, 433, 436
6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
35% identity, 16% coverage: 67:161/598 of query aligns to 95:196/460 of 6lbpA
Sites not aligning to the query:
- active site: 1, 27, 243, 301, 306, 316, 424
- binding iron/sulfur cluster: 237, 239, 383, 385, 434, 436, 437
Q9STG9 Amidophosphoribosyltransferase 2, chloroplastic; AtATase2; AtPURF2; PRPP2; Glutamine phosphoribosylpyrophosphate amidotransferase 2; AtGPRAT2; Protein CHLOROPLAST IMPORT APPARATUS 1; Protein DIFFERENTIAL DEVELOPMENT OF VASCULAR ASSOCIATED CELLS; EC 2.4.2.14 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
35% identity, 16% coverage: 67:161/598 of query aligns to 181:282/561 of Q9STG9
- H187 (≠ W73) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ K144) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P145) mutation to S: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with F-494.
Sites not aligning to the query:
- 371 G→S: Low resistance to the bleaching herbicides DAS073 and DAS734.
- 476 P→S: Resistance to the bleaching herbicides DAS073 and DAS734.
- 494 Y→F: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with S-265.
Query Sequence
>Echvi_1262 FitnessBrowser__Cola:Echvi_1262
MCGINLAMNLPGSGEDAIQQMMAATAHRGPDHSDWCKITGQLFLAGNRLKTVDLSDWSNQ
PLQINQGAHTLVWNGALYNADELRNELLEDGESFESRSDSEVLLRWLKRHGISGINRLQG
MYALVFVEREEKSIIIARDPHGKKPLYYFHQNHLWLFSSEARGIIAAGQIKRQLDKTQLT
PYLYTRHSFPDKSFFQQVQQIVPGKALQLDFGGNIRAEHRTVIPQATLELPRKEHFRSLL
TDATLKHFRADIPVGVLLSGGADSSLLLDTWMRETDLPLHTFTARFEQKYLKKYQDPIHA
RQVAEKYRCVHHEVLITPALLRAQLPEYIASLDQPVGDSASFLSWMIAREAKEHVKILIS
GAGADELFGGYNRHEAFKQYLQHKAIALKASKVMGKLSFLGRHFQKIAKGIRKDEATTFL
NFSALRNIPADQREAFLAYYPKGVPPYKAALEWDRSYYLVNDILKIHDNALMAHGVEGRA
PYLDKNLVSLSMSLTEEQHLSLKPKQWIRELLRETGLEKVAVRKKFGFGLPLKEWLEEDQ
ALRSLVVETISGFVQQHHHSIPEEFHILAKEPDKKIKLHFLEIWNLYILAAWCTYHQL
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