SitesBLAST
Comparing Ga0059261_0579 FitnessBrowser__Korea:Ga0059261_0579 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 10 hits to proteins with known functional sites (download)
2jjbA Family 37 trehalase from escherichia coli in complex with casuarine-6- o-alpha-glucopyranose (see paper)
52% identity, 99% coverage: 3:491/495 of query aligns to 2:487/504 of 2jjbA
- binding casuarine: F113 (= F118), W119 (= W124), D120 (= D125), G270 (= G274), D272 (= D276), W407 (= W410), F476 (= F480), W478 (= W482)
- binding alpha-D-glucopyranose: R112 (= R117), Y117 (= Y122), N156 (= N161), Y162 (= Y167), R165 (= R170), R237 (= R241), E239 (= E243), D272 (= D276)
2jg0A Family 37 trehalase from escherichia coli in complex with 1- thiatrehazolin (see paper)
52% identity, 99% coverage: 4:491/495 of query aligns to 1:489/507 of 2jg0A
- binding N-[(3aS,4R,5S,6S,6aS)-4,5,6-trihydroxy-4-(hydroxymethyl)-4,5,6,6a-tetrahydro-3aH-cyclopenta[d][1,3]thiazol-2-yl]-alpha- D-glucopyranosylamine: R112 (= R117), F113 (= F118), Y117 (= Y122), W119 (= W124), D120 (= D125), N156 (= N161), Y162 (= Y167), R165 (= R170), R237 (= R241), E239 (= E243), A267 (= A271), G270 (= G274), D272 (= D276), W407 (= W410), E471 (= E473), Y472 (= Y474), F478 (= F480), W480 (= W482)
2wynA Structure of family 37 trehalase from escherichia coli in complex with a casuarine-6-o-a-d-glucoside analogue (see paper)
52% identity, 99% coverage: 3:491/495 of query aligns to 2:489/506 of 2wynA
- binding alpha-D-glucopyranose: Y117 (= Y122), N156 (= N161), Y162 (= Y167), R165 (= R170), R237 (= R241), E239 (= E243)
- binding (1r,2r,3r,6r,7r,7ar)-3,7-bis(hydroxymethyl)hexahydro-1h-pyrrolizine-1,2,6-triol: F113 (= F118), W119 (= W124), D120 (= D125), G270 (= G274), D272 (= D276), W407 (= W410), Y472 (= Y474), F478 (= F480), W480 (= W482)
2jf4A Family 37 trehalase from escherichia coli in complex with validoxylamine (see paper)
51% identity, 99% coverage: 4:491/495 of query aligns to 1:482/500 of 2jf4A
- binding (1s,2s,3r,6s)-4-(hydroxymethyl)-6-{[(1s,2s,3s,4r,5r)-2,3,4-trihydroxy-5-(hydroxymethyl)cyclohexyl]amino}cyclohex-4-ene-1,2,3-triol: F106 (= F118), Y110 (= Y122), W112 (= W124), D113 (= D125), N149 (= N161), R158 (= R170), R230 (= R241), E232 (= E243), G263 (= G274), D265 (= D276), W400 (= W410), E464 (= E473), Y465 (= Y474), F471 (= F480), W473 (= W482)
5z66A Structure of periplasmic trehalase from diamondback moth gut bacteria complexed with validoxylamine (see paper)
50% identity, 98% coverage: 6:491/495 of query aligns to 6:495/512 of 5z66A
- binding (1s,2s,3r,6s)-4-(hydroxymethyl)-6-{[(1s,2s,3s,4r,5r)-2,3,4-trihydroxy-5-(hydroxymethyl)cyclohexyl]amino}cyclohex-4-ene-1,2,3-triol: P116 (= P114), F120 (= F118), Y124 (= Y122), W126 (= W124), D127 (= D125), N163 (= N161), Y169 (= Y167), Q174 (≠ H172), R243 (= R241), E245 (= E243), G276 (= G274), D278 (= D276), W413 (= W410), E477 (= E473), Y478 (= Y474), F484 (= F480), W486 (= W482)
Q9W2M2 Trehalase; Alpha,alpha-trehalase; Alpha,alpha-trehalose glucohydrolase; EC 3.2.1.28 from Drosophila melanogaster (Fruit fly) (see paper)
30% identity, 98% coverage: 11:495/495 of query aligns to 59:578/596 of Q9W2M2
- N451 (≠ S379) modified: carbohydrate, N-linked (GlcNAc...) asparagine
7eawA Trehalase of arabidopsis thaliana acid mutant -d380a trehalose complex
34% identity, 79% coverage: 103:495/495 of query aligns to 136:543/560 of 7eawA
- binding alpha-D-glucopyranose: R150 (= R117), F151 (= F118), F151 (= F118), Y155 (= Y122), W157 (= W124), D158 (= D125), N194 (= N161), Y200 (= Y167), Q205 (≠ H172), R270 (= R241), E272 (= E243), A301 (= A271), E506 (= E459), E521 (≠ Y474), Y522 (≠ G475), Y522 (≠ G475)
5n6nC Crystal structure of the 14-3-3:neutral trehalase nth1 complex (see paper)
30% identity, 78% coverage: 97:484/495 of query aligns to 241:657/698 of 5n6nC
- binding beta-D-fructofuranose: F261 (= F118), N297 (≠ D154), H298 (≠ G155), G300 (= G157), K351 (≠ R199), D425 (= D276), Q570 (= Q409)
- binding alpha-D-glucopyranose: P257 (= P114), W267 (= W124), D268 (= D125), H298 (≠ G155), G423 (= G274), D425 (= D276), Q487 (≠ R336), A529 (= A378), T530 (≠ S379), K531 (≠ A380), W571 (= W410), W655 (= W482)
Sites not aligning to the query:
P32356 Cytosolic neutral trehalase; Alpha,alpha-trehalase; Alpha,alpha-trehalose glucohydrolase; EC 3.2.1.28 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
29% identity, 78% coverage: 97:484/495 of query aligns to 283:710/751 of P32356
- WD 309:310 (= WD 124:125) binding
- N346 (= N161) binding
- RSQ 355:357 (≠ RSH 170:172) binding
- E424 (vs. gap) binding
- R473 (≠ A271) binding
- S475 (= S273) mutation to A: Abolishes activity; when associated with A-20; A-21; A-58; A-60; A-83; A-135; A-149 and A-260.
- G476 (= G274) binding
- D478 (= D276) mutation to A: Abolishes catalytic activity.
- E674 (= E459) mutation to A: Abolishes catalytic activity.
- R686 (vs. gap) mutation to A: Decreases catalytic activity.
- E690 (= E464) mutation to A: Severely decreases catalytic activity.
- Y691 (≠ Q465) mutation to A: Abolishes catalytic activity.
Sites not aligning to the query:
- 20 modified: Phosphoserine; by PKA; S→A: Abolishes activity; when associated with A-21; A-58; A-60; A-83; A-135; A-149; A-260 and A-475. Abolishes activation by BMH1 and BMH2; when associated with A-21; A-60 and A-83.
- 21 modified: Phosphoserine; by PKA; S→A: Abolishes activity; when associated with A-20; A-58; A-60; A-83; A-135; A-149; A-260 and A-475. Abolishes activation by BMH1 and BMH2; when associated with A-20; A-60 and A-83.
- 55 BMH1 binding
- 58 T→A: Abolishes activity; when associated with A-20; A-21; A-60; A-83; A-135; A-149; A-260 and A-475.
- 60 modified: Phosphoserine; by PKA; S→A: Abolishes activity; when associated with A-20; A-21; A-58; A-83; A-135; A-149; A-260 and A-475. Abolishes activation by BMH1 and BMH2; when associated with A-20; A-21 and A-83.
- 83 modified: Phosphoserine; by PKA; S→A: Abolishes activity; when associated with A-20; A-21; A-58; A-60; A-135; A-149; A-260 and A-475. Abolishes activation by BMH1 and BMH2; when associated with A-20; A-21 and A-60.
- 114 binding
- 116 binding
- 118 binding
- 120 binding ; Q→A: Decreases catalytic activity.
- 125 binding
- 135 T→A: Abolishes activity; when associated with A-20; A-21; A-58; A-60; A-83; A-149; A-260 and A-475.
- 149 T→A: Abolishes activity; when associated with A-20; A-21; A-58; A-60; A-83; A-135; A-260 and A-475.
- 260 T→A: Abolishes activity; when associated with A-20; A-21; A-58; A-60; A-83; A-135; A-149 and A-475.
O42893 Cytosolic neutral trehalase; Alpha,alpha-trehalase; Alpha,alpha-trehalose glucohydrolase; Neutral trehalase; EC 3.2.1.28 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 3 papers)
30% identity, 76% coverage: 112:485/495 of query aligns to 278:689/735 of O42893
Sites not aligning to the query:
- 6 S→A: Abolishes activation during osmotic stress and thermal stress. Increases cellular trehalose level during osmotic stress but not thermal stress. Does not affect binding to tps1.
- 41 S→A: Decreases activation during osmotic stress and thermal stress. Increases cellular trehalose level during osmotic stress but not thermal stress. Does not affect binding to tps1.
- 47 modified: Phosphothreonine
- 49 modified: Phosphoserine
- 50 modified: Phosphothreonine
- 51 modified: Phosphoserine; S→A: Abolishes activation during osmotic stress and thermal stress. Increases cellular trehalose level during osmotic stress but not thermal stress. Does not affect binding to tps1.
- 71 mutation S->A,D: Abolishes activation and increases cellular trehalose level during osmotic stress and thermal stress. Does not affect binding to tps1.
- 97 D→L: Abolishes calcium binding. Abolishes activation and increases cellular trehalose level during osmotic stress and thermal stress.
- 100 R→L: Decreases calcium binding. Decreases activation and increases cellular trehalose level during osmotic stress and thermal stress. Does not affect binding to tps1.
- 108 D→L: Abolishes calcium binding. Abolishes activation and increases cellular trehalose level during osmotic stress and thermal stress. Does not affect binding to tps1.
Query Sequence
>Ga0059261_0579 FitnessBrowser__Korea:Ga0059261_0579
MSVPQPSDLFGDLFTTVQECALFPDSKTFADAVPRRGPEAIMQDWKAQPPSGDAGLRAFV
DANFVLPTEADCDAPDGRPLREHITQLWPVLTREPETPAPGSSLLALPRRHVVPGGRFRE
LYYWDSYFTMLGLVRSDRQDLVEDMIAVFGSLLDGYGHIPNGTRSYYLSRSHPPVFYLMA
ALSQDRSANARAQRLSWMRAEHEFWMAGEKDLAPGGEHRRVVRLADGALLNRYWDDRAAP
RDESWREDIELAQRAPDRDAPELWRDIRAAAESGWDFSSRWLGDGQSLETIRTTRLLPID
LNALLFGLEQAIAEEAKALGDDTAATEFARRADARREAIDLHLWHPDAAFYADYDLDLGR
ASGRLTAALGFALFTGVASAQRAPDAANAIAGLLRAGGLLTTECVTGQQWDAPNGWAPLH
WVVIEGLRAYGQNALADTIAQRWLAMVASHYDATGQLLEKYDIEQCRAGGGGEYGTEIGF
GWTNGVTLALMQDLG
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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