SitesBLAST
Comparing Ga0059261_4199 FitnessBrowser__Korea:Ga0059261_4199 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)
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)
30% identity, 62% coverage: 1:389/630 of query aligns to 1:388/557 of P78753
Sites not aligning to the query:
- 391 modified: Phosphoserine
- 489 modified: Phosphoserine
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
31% identity, 58% coverage: 28:390/630 of query aligns to 27:362/497 of 1ct9A
- active site: L50 (= L51), N74 (= N75), G75 (= G76), T305 (≠ A342), R308 (≠ L345), E332 (≠ D365)
- binding adenosine monophosphate: L232 (≠ F264), L233 (= L265), S234 (= S266), S239 (= S271), A255 (≠ T290), V256 (≠ I291), D263 (≠ E300), M316 (≠ L353), S330 (= S363), G331 (= G364), E332 (≠ D365)
- binding glutamine: R49 (= R50), L50 (= L51), I52 (= I53), V53 (≠ I54), N74 (= N75), G75 (= G76), E76 (= E77), D98 (= D100)
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)
29% identity, 62% coverage: 1:390/630 of query aligns to 1:379/554 of P22106
- M1 (= M1) modified: Initiator methionine, Removed
- C2 (= C2) mutation C->A,S: Loss of glutamine-dependent activity but no effect on ammonia-dependent asparagine synthetase activity.
- H30 (= H30) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D34) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ F81) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ H106) mutation to H: Little effect on the kinetic properties.
- E349 (≠ D365) 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.
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)
28% identity, 61% coverage: 1:382/630 of query aligns to 1:380/561 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 (≠ G6) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
- V210 (= V217) to E: in dbSNP:rs1049674
- F362 (≠ L362) 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
6gq3A Human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1.85 a resolution (see paper)
28% identity, 60% coverage: 2:382/630 of query aligns to 1:367/509 of 6gq3A
- active site: W4 (≠ A5), L49 (= L51), N74 (= N75), G75 (= G76), T324 (≠ P338), R327 (≠ D341)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R50), V51 (≠ I53), V52 (≠ I54), Y73 (= Y74), N74 (= N75), G75 (= G76), E76 (= E77), V95 (≠ S99), D96 (= D100)
6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
30% identity, 26% coverage: 2:166/630 of query aligns to 1:199/460 of 6lbpA
Sites not aligning to the query:
- active site: 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)
30% identity, 26% coverage: 2:166/630 of query aligns to 87:285/561 of Q9STG9
- H187 (≠ Y74) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
- R264 (≠ K145) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
- P265 (= P146) 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.
1jgtB Crystal structure of beta-lactam synthetase (see paper)
29% identity, 40% coverage: 76:325/630 of query aligns to 74:302/500 of 1jgtB
Sites not aligning to the query:
- active site: 73, 319, 345, 379, 440
- binding diphosphomethylphosphonic acid adenosyl ester: 327, 344, 345, 348, 420, 440
- binding n2-(carboxyethyl)-l-arginine: 323, 345, 346, 348, 349, 354, 370, 379
- binding magnesium ion: 348
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
28% identity, 40% coverage: 76:325/630 of query aligns to 70:294/496 of 1mbzA
Sites not aligning to the query:
- active site: 69, 311, 337, 371, 432
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: 315, 319, 336, 337, 338, 340, 341, 362, 371, 432, 434, 435
- binding magnesium ion: 340
- binding pyrophosphate 2-: 340, 412, 432, 433
1mb9A Beta-lactam synthetase complexed with atp (see paper)
28% identity, 40% coverage: 76:325/630 of query aligns to 71:293/485 of 1mb9A
- active site: G71 (= G76)
- binding adenosine monophosphate: V235 (≠ F264), L236 (= L265), S242 (= S271), S260 (≠ G292), M261 (≠ F293)
- binding adenosine-5'-triphosphate: V235 (≠ F264), L236 (= L265), S237 (= S266), G239 (= G268), D241 (= D270), S242 (= S271), S260 (≠ G292), M261 (≠ F293)
- binding magnesium ion: D241 (= D270)
- binding pyrophosphate 2-: S237 (= S266), G239 (= G268), D241 (= D270), S242 (= S271)
Sites not aligning to the query:
- active site: 70, 310, 336, 370, 431
- binding adenosine monophosphate: 314, 318, 335, 336
- binding adenosine-5'-triphosphate: 318, 335, 339, 411, 431
- binding magnesium ion: 339
- binding pyrophosphate 2-: 339, 411, 431
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
28% identity, 40% coverage: 76:325/630 of query aligns to 66:289/491 of 1mc1A
Sites not aligning to the query:
- active site: 65, 306, 332, 366, 427
- binding adenosine monophosphate: 331, 427, 430
- binding magnesium ion: 335
- binding deoxyguanidinoproclavaminic acid: 310, 332, 333, 336, 357, 366, 427
- binding pyrophosphate 2-: 335, 407, 427, 428
Query Sequence
>Ga0059261_4199 FitnessBrowser__Korea:Ga0059261_4199
MCGIAGLYYPGVPKPVEPQRIKAMADALAHRGPDGSGAWTAPGIGLGHRRLSIIDLAGGA
QPMATPEGDVVVSYNGEIYNFLEVRRELEAKGAQFLSNSDTEVLLHGWRAWGSAMLGKLN
GMFAIALYDARSKSLMLARDRLGVKPLHYVELSDGAVAFASEIKGLLAHPLFRRQPDFNA
IEDFLGLGYVPDDASVLAGVKKLPAGHYLLLERGKPVPAPTEWWDVDFSKRTKGSARDLE
AELIEHMRAAIQSRMIADVPLGAFLSGGVDSSAVVALMAEASRNAVKACTIGFDETDHDE
RVYARAVAERFCTEHRTRTVAADDFALIDALVHHFDEPFADASALATYRVCELARETVTV
ALSGDGADEALAGYRRYRFHAAEERVRGLFPATARQGVFGTLGRLYPKADWAPRPLRAKT
TLLALAEDGGAAYAKAVGVTALTVRMGLYTDAARALLGGHRAETRYVETMRNAPARDGLD
RAQYADFKHWLPGDILTKMDRTSMAVSLEAREPLLDYRFVEFAATLPASMRIRGGQGKWL
MKKALEPWLPKDILYRPKMGFVTPVSAWFRTALADDAAALSRSAVLAGSGWFEPKAIARL
AEEHRSGRAEHGRTLWQLMMLERSLGRLFA
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