SitesBLAST
Comparing RR42_RS28230 FitnessBrowser__Cup4G11:RR42_RS28230 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)
54% identity, 90% coverage: 33:516/536 of query aligns to 13:487/504 of 2jjbA
- binding casuarine: F113 (= F140), W119 (= W146), D120 (= D147), G270 (= G295), D272 (= D297), W407 (= W431), F476 (= F505), W478 (= W507)
- binding alpha-D-glucopyranose: R112 (= R139), Y117 (= Y144), N156 (= N183), Y162 (= Y189), R165 (= R192), R237 (= R263), E239 (= E265), D272 (= D297)
2jg0A Family 37 trehalase from escherichia coli in complex with 1- thiatrehazolin (see paper)
54% identity, 90% coverage: 33:516/536 of query aligns to 11:489/507 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 (= R139), F113 (= F140), Y117 (= Y144), W119 (= W146), D120 (= D147), N156 (= N183), Y162 (= Y189), R165 (= R192), R237 (= R263), E239 (= E265), A267 (= A292), G270 (= G295), D272 (= D297), W407 (= W431), E471 (= E498), Y472 (= Y499), F478 (= F505), W480 (= W507)
2jf4A Family 37 trehalase from escherichia coli in complex with validoxylamine (see paper)
54% identity, 90% coverage: 33:516/536 of query aligns to 11:482/500 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 (= F140), Y110 (= Y144), W112 (= W146), D113 (= D147), N149 (= N183), R158 (= R192), R230 (= R263), E232 (= E265), G263 (= G295), D265 (= D297), W400 (= W431), E464 (= E498), Y465 (= Y499), F471 (= F505), W473 (= W507)
5z66A Structure of periplasmic trehalase from diamondback moth gut bacteria complexed with validoxylamine (see paper)
53% identity, 90% coverage: 33:516/536 of query aligns to 13:495/512 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 (= P136), F120 (= F140), Y124 (= Y144), W126 (= W146), D127 (= D147), N163 (= N183), Y169 (= Y189), Q174 (= Q194), R243 (= R263), E245 (= E265), G276 (= G295), D278 (= D297), W413 (= W431), E477 (= E498), Y478 (= Y499), F484 (= F505), W486 (= W507)
2wynA Structure of family 37 trehalase from escherichia coli in complex with a casuarine-6-o-a-d-glucoside analogue (see paper)
54% identity, 90% coverage: 33:516/536 of query aligns to 13:489/506 of 2wynA
- binding alpha-D-glucopyranose: Y117 (= Y144), N156 (= N183), Y162 (= Y189), R165 (= R192), R237 (= R263), E239 (= E265)
- binding (1r,2r,3r,6r,7r,7ar)-3,7-bis(hydroxymethyl)hexahydro-1h-pyrrolizine-1,2,6-triol: F113 (= F140), W119 (= W146), D120 (= D147), G270 (= G295), D272 (= D297), W407 (= W431), Y472 (= Y499), F478 (= F505), W480 (= W507)
Q9W2M2 Trehalase; Alpha,alpha-trehalase; Alpha,alpha-trehalose glucohydrolase; EC 3.2.1.28 from Drosophila melanogaster (Fruit fly) (see paper)
31% identity, 95% coverage: 22:532/536 of query aligns to 48:594/596 of Q9W2M2
- N451 (≠ T399) modified: carbohydrate, N-linked (GlcNAc...) asparagine
7eawA Trehalase of arabidopsis thaliana acid mutant -d380a trehalose complex
33% identity, 81% coverage: 92:527/536 of query aligns to 99:552/560 of 7eawA
- binding alpha-D-glucopyranose: R150 (= R139), F151 (= F140), F151 (= F140), Y155 (= Y144), W157 (= W146), D158 (= D147), N194 (= N183), Y200 (= Y189), Q205 (= Q194), R270 (= R263), E272 (= E265), A301 (= A292), E506 (= E480), E521 (≠ G497), Y522 (≠ E498), Y522 (≠ E498)
5n6nC Crystal structure of the 14-3-3:neutral trehalase nth1 complex (see paper)
31% identity, 71% coverage: 131:509/536 of query aligns to 252:657/698 of 5n6nC
- binding beta-D-fructofuranose: F261 (= F140), N297 (≠ D176), H298 (≠ T177), G300 (= G179), K351 (= K222), D425 (= D297), Q570 (= Q430)
- binding alpha-D-glucopyranose: P257 (= P136), W267 (= W146), D268 (= D147), H298 (≠ T177), G423 (= G295), D425 (= D297), Q487 (≠ R356), A529 (= A398), T530 (= T399), K531 (≠ P400), W571 (= W431), W655 (= W507)
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)
30% identity, 71% coverage: 131:509/536 of query aligns to 294:710/751 of P32356
- WD 309:310 (= WD 146:147) binding
- N346 (= N183) binding
- RSQ 355:357 (= RSQ 192:194) binding
- E424 (vs. gap) binding
- R473 (≠ A292) binding
- S475 (= S294) 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 (= G295) binding
- D478 (= D297) mutation to A: Abolishes catalytic activity.
- E674 (= E480) mutation to A: Abolishes catalytic activity.
- R686 (vs. gap) mutation to A: Decreases catalytic activity.
- E690 (≠ A491) mutation to A: Severely decreases catalytic activity.
- Y691 (≠ V492) 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)
31% identity, 71% coverage: 132:510/536 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
>RR42_RS28230 FitnessBrowser__Cup4G11:RR42_RS28230
MGDPTGGQTLAPHRLAGCAHADPLTPADRYQELFVAVQMGRIFPDSKTFTDAMPRQDPAT
ILAAYRARAGAAGFDLAAFVHAHFALPEVPRSCYESDPNQPLADHIDGLWAVLTRHPAQH
PPQCSLLPLPHPYVVPGGRFSELYYWDSYFTMLGLAASGQGGLLRGMAENFSYLLDTYGV
IPNGTRSYYLSRSQPPVFALMVELFEDQGVQPELGFLPQLRKEYAFWMRGADCLAPGQAC
RRVVRLADGSLLNRYWDERDTPREEAFIEDTGTAALAARPAAEVFRDLRAAAESGWDFSS
RWQEPGGGLETVRTTAILPVDLNCLLFKLEHKLAELAQAAGDADAPVFAQRAQARREAID
RLMWREAEGAYFDFDWQRHHARANLTAATVVPLYVGAATPAQAARVAQTVAARLLQPGGI
ATTERVSGQQWDLPNGWAPLQWLAIGGFACCGQAALAHEIAHRWLVTVASLYQREYKLVE
KYALQPGEDGAVGGGGGEYPLQDGFGWTNGVVRRLLQDHPAHVACRCRAGVKSVHP
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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