SitesBLAST
Comparing BPHYT_RS26585 FitnessBrowser__BFirm:BPHYT_RS26585 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)
55% identity, 90% coverage: 59:557/557 of query aligns to 3:494/504 of 2jjbA
- binding casuarine: F113 (= F174), W119 (= W180), D120 (= D181), G270 (= G331), D272 (= D333), W407 (= W467), F476 (= F539), W478 (= W541)
- binding alpha-D-glucopyranose: R112 (= R173), Y117 (= Y178), N156 (= N217), Y162 (= Y223), R165 (= R226), R237 (= R298), E239 (= E300), D272 (= D333)
2jg0A Family 37 trehalase from escherichia coli in complex with 1- thiatrehazolin (see paper)
55% identity, 90% coverage: 59:557/557 of query aligns to 1:496/507 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 (= R173), F113 (= F174), Y117 (= Y178), W119 (= W180), D120 (= D181), N156 (= N217), Y162 (= Y223), R165 (= R226), R237 (= R298), E239 (= E300), A267 (= A328), G270 (= G331), D272 (= D333), W407 (= W467), E471 (= E532), Y472 (= Y533), F478 (= F539), W480 (= W541)
5z66A Structure of periplasmic trehalase from diamondback moth gut bacteria complexed with validoxylamine (see paper)
55% identity, 89% coverage: 61:555/557 of query aligns to 5:500/512 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 (= P170), F120 (= F174), Y124 (= Y178), W126 (= W180), D127 (= D181), N163 (= N217), Y169 (= Y223), Q174 (= Q228), R243 (= R298), E245 (= E300), G276 (= G331), D278 (= D333), W413 (= W467), E477 (= E532), Y478 (= Y533), F484 (= F539), W486 (= W541)
2wynA Structure of family 37 trehalase from escherichia coli in complex with a casuarine-6-o-a-d-glucoside analogue (see paper)
55% identity, 90% coverage: 59:557/557 of query aligns to 3:496/506 of 2wynA
- binding alpha-D-glucopyranose: Y117 (= Y178), N156 (= N217), Y162 (= Y223), R165 (= R226), R237 (= R298), E239 (= E300)
- binding (1r,2r,3r,6r,7r,7ar)-3,7-bis(hydroxymethyl)hexahydro-1h-pyrrolizine-1,2,6-triol: F113 (= F174), W119 (= W180), D120 (= D181), G270 (= G331), D272 (= D333), W407 (= W467), Y472 (= Y533), F478 (= F539), W480 (= W541)
2jf4A Family 37 trehalase from escherichia coli in complex with validoxylamine (see paper)
55% identity, 90% coverage: 59:557/557 of query aligns to 1:489/500 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 (= F174), Y110 (= Y178), W112 (= W180), D113 (= D181), N149 (= N217), R158 (= R226), R230 (= R298), E232 (= E300), G263 (= G331), D265 (= D333), W400 (= W467), E464 (= E532), Y465 (= Y533), F471 (= F539), W473 (= W541)
Q9W2M2 Trehalase; Alpha,alpha-trehalase; Alpha,alpha-trehalose glucohydrolase; EC 3.2.1.28 from Drosophila melanogaster (Fruit fly) (see paper)
32% identity, 88% coverage: 59:550/557 of query aligns to 49:574/596 of Q9W2M2
- N451 (≠ W435) modified: carbohydrate, N-linked (GlcNAc...) asparagine
7eawA Trehalase of arabidopsis thaliana acid mutant -d380a trehalose complex
32% identity, 80% coverage: 108:553/557 of query aligns to 63:542/560 of 7eawA
- binding alpha-D-glucopyranose: R150 (= R173), F151 (= F174), F151 (= F174), Y155 (= Y178), W157 (= W180), D158 (= D181), N194 (= N217), Y200 (= Y223), Q205 (= Q228), R270 (= R298), E272 (= E300), A301 (= A328), E506 (= E516), E521 (≠ G531), Y522 (≠ E532), Y522 (≠ E532)
5n6nC Crystal structure of the 14-3-3:neutral trehalase nth1 complex (see paper)
28% identity, 68% coverage: 166:544/557 of query aligns to 253:658/698 of 5n6nC
- binding beta-D-fructofuranose: F261 (= F174), N297 (≠ D210), H298 (≠ T211), G300 (= G213), K351 (≠ Q264), D425 (= D333), Q570 (= Q466)
- binding alpha-D-glucopyranose: P257 (= P170), W267 (= W180), D268 (= D181), H298 (≠ T211), G423 (= G331), D425 (= D333), Q487 (≠ A393), A529 (= A434), T530 (≠ W435), K531 (≠ P436), W571 (= W467), W655 (= W541)
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)
28% identity, 68% coverage: 166:544/557 of query aligns to 295:711/751 of P32356
- WD 309:310 (= WD 180:181) binding
- N346 (= N217) binding
- RSQ 355:357 (= RSQ 226:228) binding
- E424 (≠ R284) binding
- R473 (≠ A328) binding
- S475 (= S330) 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 (= G331) binding
- D478 (= D333) mutation to A: Abolishes catalytic activity.
- E674 (= E516) mutation to A: Abolishes catalytic activity.
- R686 (vs. gap) mutation to A: Decreases catalytic activity.
- E690 (≠ T525) mutation to A: Severely decreases catalytic activity.
- Y691 (≠ G526) 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, 68% coverage: 166:544/557 of query aligns to 276:689/735 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
>BPHYT_RS26585 FitnessBrowser__BFirm:BPHYT_RS26585
MIESSQPRNFGRAGIASRTAFRSVESTRLHRIAAASSFVFLINLAGVCHADTQVGGPLPP
APDKLYGDLFVAVQTAQIYPDQKTFVDATPNADPAAIVQLYEQQKHNPGFSLAKFVNKYF
TPPSEPVITPPANQTLREHINWLWPALTRTTTSAPPNSSLIPLPKPYVVPGGRFREGYYW
DTYFTMLGLQESGNENLVDDMLDNFAYEIDTFGHIPNGNRTYYLDRSQPPFFSHMVELAA
KMEGHGVYQKYLPALRKEYAYWMQGESTTRPGSATRNVVVMPDRTVLNRYWDELDTPRDE
SYLEDIQTAQQASGRNPNDVYRELRATAESGWDFSSRWFGDNMTLATVRTTSIIPVDLNS
LMFHLEITIAKGCGETRDFRCVGEFAQRAAKRALGINRYLWNPNGYYGDYDWQLARPRDN
KTAAMVFPLFVGAAWPDRALKTAKQVQSTLLQPGGLVTTTYNTTQQWDAPNGWAPLHWAA
IQGLKRYGQDALAQQIGTRFLSDVKGVYASDQKLVEKYVVEGSGTGGGGGGEYPLQDGFG
WTNGVTLKLLDLYSPGD
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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