SitesBLAST
Comparing HSERO_RS21060 FitnessBrowser__HerbieS:HSERO_RS21060 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 13 hits to proteins with known functional sites (download)
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
32% identity, 59% coverage: 27:371/581 of query aligns to 27:341/497 of 1ct9A
- active site: L50 (= L50), N74 (= N75), G75 (= G76), T305 (≠ S340), R308 (vs. gap), E332 (≠ D362)
- binding adenosine monophosphate: L232 (≠ F261), L233 (= L262), S234 (= S263), S239 (= S268), A255 (≠ S286), V256 (≠ I287), D263 (≠ E296), M316 (≠ V347), S330 (= S360), G331 (= G361), E332 (≠ D362)
- binding glutamine: R49 (= R49), L50 (= L50), I52 (= I52), V53 (≠ R53), 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)
31% identity, 64% coverage: 1:371/581 of query aligns to 1:358/554 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 (≠ F29) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D33) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ W81) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ Q106) mutation to H: Little effect on the kinetic properties.
- E349 (≠ D362) 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.
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, 64% coverage: 1:371/581 of query aligns to 1:365/557 of P78753
Sites not aligning to the query:
- 391 modified: Phosphoserine
- 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)
28% identity, 64% coverage: 1:371/581 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 (≠ G6) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
- V210 (≠ K229) to E: in dbSNP:rs1049674
- F362 (≠ L359) 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, 64% coverage: 2:371/581 of query aligns to 1:361/509 of 6gq3A
- active site: W4 (≠ A5), L49 (= L50), N74 (= N75), G75 (= G76), T324 (≠ P335), R327 (≠ D338)
- binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R49), V51 (≠ I52), V52 (≠ R53), Y73 (≠ F74), N74 (= N75), G75 (= G76), E76 (= E77), V95 (≠ S99), D96 (= D100)
1q19A Carbapenam synthetase (see paper)
27% identity, 47% coverage: 99:370/581 of query aligns to 79:352/500 of 1q19A
- active site: L318 (≠ A339), E321 (≠ L342), Y344 (≠ D362)
- binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ F261), L244 (= L262), S245 (= S263), D249 (= D267), S250 (= S268), S268 (= S286), I269 (= I287), T342 (≠ S360), G343 (= G361), D347 (= D365)
- binding (2s,5s)-5-carboxymethylproline: Y344 (≠ D362), G345 (= G363), L348 (≠ E366)
Sites not aligning to the query:
Q9XB61 Carbapenam-3-carboxylate synthase; Carbapenam-3-carboxylate ligase; EC 6.3.3.6 from Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. carotovora) (see 3 papers)
27% identity, 47% coverage: 99:370/581 of query aligns to 80:353/503 of Q9XB61
- 244:251 (vs. 261:268, 75% identical) binding
- I270 (= I287) binding
- GYGSD 344:348 (≠ GDGGD 361:365) binding
- Y345 (≠ D362) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
- G346 (= G363) binding
Sites not aligning to the query:
- 371 binding
- 374 binding
- 380 E→A: Loss of activity.; E→D: Reduces catalytic efficiency.; E→Q: Reduces catalytic efficiency.
- 421 binding
- 443 mutation K->A,M: Loss of activity.
- 444:446 binding
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
27% identity, 52% coverage: 71:373/581 of query aligns to 65:348/496 of 1mbzA
- active site: A69 (≠ N75), G70 (= G76), D311 (≠ F336), Y337 (≠ D362)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ F261), L237 (= L262), S238 (= S263), S243 (= S268), S261 (= S286), M262 (≠ I287), Y315 (≠ S340), L319 (≠ T344), G336 (= G361), Y337 (≠ D362), G338 (= G363), D340 (= D365), I341 (≠ E366)
- binding magnesium ion: D242 (= D267), D340 (= D365)
- binding pyrophosphate 2-: S238 (= S263), G240 (= G265), D242 (= D267), S243 (= S268), D340 (= D365)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
27% identity, 52% coverage: 71:373/581 of query aligns to 61:343/491 of 1mc1A
- active site: A65 (≠ N75), G66 (= G76), D306 (≠ F336), Y332 (≠ D362)
- binding adenosine monophosphate: V231 (≠ F261), S233 (= S263), S238 (= S268), S256 (= S286), M257 (≠ I287), G331 (= G361)
- binding magnesium ion: D237 (= D267), D335 (= D365)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ S340), Y332 (≠ D362), G333 (= G363), I336 (≠ E366)
- binding pyrophosphate 2-: S233 (= S263), G235 (= G265), D237 (= D267), S238 (= S268), D335 (= D365)
Sites not aligning to the query:
1jgtB Crystal structure of beta-lactam synthetase (see paper)
27% identity, 52% coverage: 71:373/581 of query aligns to 69:356/500 of 1jgtB
- active site: A73 (≠ N75), G74 (= G76), D319 (≠ F336), Y345 (≠ D362)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ F261), L245 (= L262), S246 (= S263), G248 (= G265), I249 (≠ V266), D250 (= D267), S251 (= S268), S269 (= S286), M270 (≠ I287), L327 (≠ T344), G344 (= G361), Y345 (≠ D362), D348 (= D365)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ S340), Y345 (≠ D362), G346 (= G363), D348 (= D365), I349 (≠ E366), M354 (≠ Y371)
- binding magnesium ion: D250 (= D267), D348 (= D365)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
26% identity, 52% coverage: 71:373/581 of query aligns to 66:347/485 of 1mb9A
- active site: A70 (≠ N75), G71 (= G76), D310 (≠ F336), Y336 (≠ D362)
- binding adenosine monophosphate: V235 (≠ F261), L236 (= L262), S242 (= S268), S260 (= S286), M261 (≠ I287), Y314 (≠ S340), L318 (≠ T344), G335 (= G361), Y336 (≠ D362)
- binding adenosine-5'-triphosphate: V235 (≠ F261), L236 (= L262), S237 (= S263), G239 (= G265), D241 (= D267), S242 (= S268), S260 (= S286), M261 (≠ I287), L318 (≠ T344), G335 (= G361), D339 (= D365)
- binding magnesium ion: D241 (= D267), D339 (= D365)
- binding pyrophosphate 2-: S237 (= S263), G239 (= G265), D241 (= D267), S242 (= S268), D339 (= D365)
Sites not aligning to the query:
6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
25% identity, 36% coverage: 68:275/581 of query aligns to 95:291/460 of 6lbpA
Sites not aligning to the query:
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)
25% identity, 36% coverage: 68:275/581 of query aligns to 181:377/561 of Q9STG9
- H187 (≠ F74) 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.
- G371 (≠ S269) mutation to S: Low resistance to the bleaching herbicides DAS073 and DAS734.
Sites not aligning to the query:
- 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
>HSERO_RS21060 FitnessBrowser__HerbieS:HSERO_RS21060
MCGIAGILMNQAALPDVSVLRAMAASMAFRGPDDEGIHVAPSIGLVHRRLSIRDLSSAGH
CPMSTADGRYTLVFNGEIYNWRELRAELESMGQVFHSQSDTEVVLQAYNAWGTDVIARLE
GMFALAVWDDQAGSLFLARDRMGEKPLYYARTDQGLAFSSSPSAVLHATGPLPLDPMGIA
CHLSHTFIPATHTGWAGLRVLAPATWLLAHADGRIEERRYWDFPRTSPKPIAWADALSEV
ESILDDSVQRTLDADVEVGVFLSGGVDSSLIAALAARHNKRVKAFSIGFAEVQYNELPYS
EAVAKHLGIEQHVHIVTCDDIIDALPHLVRQYGQPFGDASALPTYLVSRLARQHAKVCLS
GDGGDELFGGYWRLQAGVYAARYGALVPTWLRRHAVPAVASRLGRLGRRLDAMNTLSLAE
AGSGYTNSESWFNHLQQVAGPNLLPALDMEKLVAARVGKATNRPEASIVQRLLYDDIQIQ
FPDALLAKVDVASMAASLEVREPFLTPRLLEFAWGLPDHTKLKWGNRKALLKEIAARHVP
RDVVYRPKMGFASPLDKWFKGELGEYGASLFEHSVAVASGY
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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