SitesBLAST
Comparing GFF2874 FitnessBrowser__psRCH2:GFF2874 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 9 hits to proteins with known functional sites (download)
1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
27% identity, 80% coverage: 57:558/627 of query aligns to 23:433/497 of 1ct9A
- active site: L50 (= L87), N74 (= N112), G75 (= G113), T305 (≠ S385), R308 (≠ H386), E332 (≠ Q409), M366 (≠ G472)
- binding adenosine monophosphate: L232 (= L303), L233 (= L304), S234 (= S305), S239 (= S310), A255 (≠ S330), V256 (≠ I331), D263 (≠ E343), M316 (≠ L394), S330 (= S407), G331 (= G408), E332 (≠ Q409)
- binding glutamine: R49 (= R86), L50 (= L87), I52 (= I89), V53 (≠ M90), N74 (= N112), G75 (= G113), E76 (≠ A114), D98 (= D137)
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)
27% identity, 83% coverage: 38:558/627 of query aligns to 1:453/554 of P22106
- M1 (= M38) modified: Initiator methionine, Removed
- C2 (= C39) mutation C->A,S: Loss of glutamine-dependent activity but no effect on ammonia-dependent asparagine synthetase activity.
- H30 (= H63) mutation to A: 4,5-fold decrease in glutamine affinity.
- D34 (= D70) mutation D->N,E: Little effect on the kinetic properties.
- H81 (≠ Y118) mutation to A: 5-fold decrease in glutamine affinity.
- A105 (≠ K143) mutation to H: Little effect on the kinetic properties.
- E349 (≠ Q409) 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)
27% identity, 80% coverage: 38:541/627 of query aligns to 1:443/557 of P78753
- S391 (≠ V490) 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)
25% identity, 83% coverage: 38:558/627 of query aligns to 1:470/561 of P08243
- C2 (= C39) active site, For GATase activity; mutation to A: Loss of the glutamine-dependent asparagine synthetase activity, while the ammonia-dependent activity remained unaffected.
- A6 (≠ G43) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
- V210 (= V248) to E: in dbSNP:rs1049674
- F362 (≠ Q406) 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)
25% identity, 78% coverage: 64:554/627 of query aligns to 23:453/509 of 6gq3A
- active site: L49 (= L87), N74 (= N112), G75 (= G113), T324 (≠ S385), R327 (≠ H386)
- binding 5-oxo-l-norleucine: R48 (= R86), V51 (≠ I89), V52 (≠ M90), Y73 (≠ F111), N74 (= N112), G75 (= G113), E76 (≠ A114), V95 (≠ G136), D96 (= D137)
Sites not aligning to the query:
1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
27% identity, 57% coverage: 65:419/627 of query aligns to 11:342/491 of 1mc1A
- active site: A65 (≠ N112), G66 (= G113), D306 (= D387), Y332 (≠ Q409)
- binding adenosine monophosphate: V231 (≠ L303), S233 (= S305), S238 (= S310), S256 (= S330), M257 (≠ I331), G331 (= G408)
- binding magnesium ion: D237 (= D309), D335 (= D412)
- binding deoxyguanidinoproclavaminic acid: Y310 (≠ F391), Y332 (≠ Q409), G333 (= G410), I336 (≠ E413)
- binding pyrophosphate 2-: S233 (= S305), G235 (= G307), D237 (= D309), S238 (= S310), D335 (= D412)
Sites not aligning to the query:
1jgtB Crystal structure of beta-lactam synthetase (see paper)
27% identity, 50% coverage: 108:419/627 of query aligns to 69:355/500 of 1jgtB
- active site: A73 (≠ N112), G74 (= G113), D319 (= D387), Y345 (≠ Q409)
- binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ L303), L245 (= L304), S246 (= S305), G248 (= G307), I249 (≠ V308), D250 (= D309), S251 (= S310), S269 (= S330), M270 (≠ I331), L327 (vs. gap), G344 (= G408), Y345 (≠ Q409), D348 (= D412)
- binding n2-(carboxyethyl)-l-arginine: Y323 (≠ F391), Y345 (≠ Q409), G346 (= G410), D348 (= D412), I349 (≠ E413), M354 (≠ Y418)
- binding magnesium ion: D250 (= D309), D348 (= D412)
Sites not aligning to the query:
1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
26% identity, 50% coverage: 108:419/627 of query aligns to 65:347/496 of 1mbzA
- active site: A69 (≠ N112), G70 (= G113), D311 (= D387), Y337 (≠ Q409)
- binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ L303), L237 (= L304), S238 (= S305), S243 (= S310), S261 (= S330), M262 (≠ I331), Y315 (≠ F391), L319 (vs. gap), G336 (= G408), Y337 (≠ Q409), G338 (= G410), D340 (= D412), I341 (≠ E413)
- binding magnesium ion: D242 (= D309), D340 (= D412)
- binding pyrophosphate 2-: S238 (= S305), G240 (= G307), D242 (= D309), S243 (= S310), D340 (= D412)
Sites not aligning to the query:
1mb9A Beta-lactam synthetase complexed with atp (see paper)
26% identity, 50% coverage: 108:419/627 of query aligns to 66:346/485 of 1mb9A
- active site: A70 (≠ N112), G71 (= G113), D310 (= D387), Y336 (≠ Q409)
- binding adenosine monophosphate: V235 (≠ L303), L236 (= L304), S242 (= S310), S260 (= S330), M261 (≠ I331), Y314 (≠ F391), L318 (vs. gap), G335 (= G408), Y336 (≠ Q409)
- binding adenosine-5'-triphosphate: V235 (≠ L303), L236 (= L304), S237 (= S305), G239 (= G307), D241 (= D309), S242 (= S310), S260 (= S330), M261 (≠ I331), L318 (vs. gap), G335 (= G408), D339 (= D412)
- binding magnesium ion: D241 (= D309), D339 (= D412)
- binding pyrophosphate 2-: S237 (= S305), G239 (= G307), D241 (= D309), S242 (= S310), D339 (= D412)
Sites not aligning to the query:
Query Sequence
>GFF2874 FitnessBrowser__psRCH2:GFF2874
MTEPSQAGSTPLRWSEKLNFARDGSVTLPNGKTGKDLMCGIAGELRFDNRPADLAAVERI
TQHLTARGPDACGFHSQGPLALGHRRLKIMDLCEASGQPMIDSALGLSMVFNGAIYNYPE
LRAELEGLGYRFFSEGDTEVLLKGFHAWGEALLPRLNGMFAFAIWQRDTQQLFIARDRLG
VKPLYLSRTDQRLRFASSLPALLKGGDIAGVLNPVALNHYMSFHAVVPAPDTLIAGIEKL
PPASWMRVDANGATTTQRWWELQFGAREEERNYSFEDWKQRTLDTMREAVAIRQRAAVDV
GVLLSGGVDSSLLVGLLREAGVADNLLTFSIGFEDAGGERGDEFKYSDLIAKHYKTRHHQ
LRIQEKEILEQLPAAFQAMSEPMVSHDCIAFYLLSREVAKHCKVVQSGQGADELFAGYHW
YPLVDGAEDPVAAYLAAFRDRSYEEYAETVQQQWVQGDFSGDFVRQHFAQPGADAAVDKA
LRIDSTVMLVDDPVKRVDNMTMAWGLEARTPFLDYRVAELSARIPAKFKLPEGGKYVLKE
AARQVIPAEVIDRPKGYFPVPGLKHLQGATLNWVREMLLDPSQERGLYNPQALEKLLADP
DGQLTPLRGSKLWQLAAVNLWLSEQGL
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