SitesBLAST
Comparing GFF357 FitnessBrowser__psRCH2:GFF357 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 12 hits to proteins with known functional sites (download)
5z66A Structure of periplasmic trehalase from diamondback moth gut bacteria complexed with validoxylamine (see paper)
53% identity, 92% coverage: 22:514/534 of query aligns to 3:495/512 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 (= P135), F120 (= F139), Y124 (= Y143), W126 (= W145), D127 (= D146), N163 (= N182), Y169 (= Y188), Q174 (= Q193), R243 (= R262), E245 (= E264), G276 (= G294), D278 (= D296), W413 (= W432), E477 (= E496), Y478 (= Y497), F484 (= F503), W486 (= W505)
2jjbA Family 37 trehalase from escherichia coli in complex with casuarine-6- o-alpha-glucopyranose (see paper)
54% identity, 90% coverage: 32:514/534 of query aligns to 13:487/504 of 2jjbA
- binding casuarine: F113 (= F139), W119 (= W145), D120 (= D146), G270 (= G294), D272 (= D296), W407 (= W432), F476 (= F503), W478 (= W505)
- binding alpha-D-glucopyranose: R112 (= R138), Y117 (= Y143), N156 (= N182), Y162 (= Y188), R165 (= R191), R237 (= R262), E239 (= E264), D272 (= D296)
2jg0A Family 37 trehalase from escherichia coli in complex with 1- thiatrehazolin (see paper)
54% identity, 90% coverage: 32:514/534 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 (= R138), F113 (= F139), Y117 (= Y143), W119 (= W145), D120 (= D146), N156 (= N182), Y162 (= Y188), R165 (= R191), R237 (= R262), E239 (= E264), A267 (= A291), G270 (= G294), D272 (= D296), W407 (= W432), E471 (= E496), Y472 (= Y497), F478 (= F503), W480 (= W505)
2jf4A Family 37 trehalase from escherichia coli in complex with validoxylamine (see paper)
54% identity, 90% coverage: 32:514/534 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 (= F139), Y110 (= Y143), W112 (= W145), D113 (= D146), N149 (= N182), R158 (= R191), R230 (= R262), E232 (= E264), G263 (= G294), D265 (= D296), W400 (= W432), E464 (= E496), Y465 (= Y497), F471 (= F503), W473 (= W505)
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: 32:514/534 of query aligns to 13:489/506 of 2wynA
- binding alpha-D-glucopyranose: Y117 (= Y143), N156 (= N182), Y162 (= Y188), R165 (= R191), R237 (= R262), E239 (= E264)
- binding (1r,2r,3r,6r,7r,7ar)-3,7-bis(hydroxymethyl)hexahydro-1h-pyrrolizine-1,2,6-triol: F113 (= F139), W119 (= W145), D120 (= D146), G270 (= G294), D272 (= D296), W407 (= W432), Y472 (= Y497), F478 (= F503), W480 (= W505)
Q9W2M2 Trehalase; Alpha,alpha-trehalase; Alpha,alpha-trehalose glucohydrolase; EC 3.2.1.28 from Drosophila melanogaster (Fruit fly) (see paper)
34% identity, 88% coverage: 41:509/534 of query aligns to 72:569/596 of Q9W2M2
- N451 (≠ S399) modified: carbohydrate, N-linked (GlcNAc...) asparagine
7eawA Trehalase of arabidopsis thaliana acid mutant -d380a trehalose complex
32% identity, 89% coverage: 43:516/534 of query aligns to 32:541/560 of 7eawA
- binding alpha-D-glucopyranose: R150 (= R138), F151 (= F139), F151 (= F139), Y155 (= Y143), W157 (= W145), D158 (= D146), N194 (= N182), Y200 (= Y188), Q205 (= Q193), R270 (= R262), E272 (= E264), A301 (= A291), E506 (= E481), E521 (= E496), Y522 (= Y497), Y522 (= Y497)
5n6nC Crystal structure of the 14-3-3:neutral trehalase nth1 complex (see paper)
30% identity, 73% coverage: 119:507/534 of query aligns to 241:657/698 of 5n6nC
- binding beta-D-fructofuranose: F261 (= F139), N297 (≠ D175), H298 (≠ T176), G300 (= G178), K351 (= K221), D425 (= D296), Q570 (= Q431)
- binding alpha-D-glucopyranose: P257 (= P135), W267 (= W145), D268 (= D146), H298 (≠ T176), G423 (= G294), D425 (= D296), Q487 (≠ L356), A529 (= A398), T530 (≠ S399), K531 (≠ A400), W571 (= W432), W655 (= W505)
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, 70% coverage: 132:507/534 of query aligns to 296:710/751 of P32356
- WD 309:310 (= WD 145:146) binding
- N346 (= N182) binding
- RSQ 355:357 (= RSQ 191:193) binding
- E424 (vs. gap) binding
- R473 (≠ A291) binding
- S475 (= S293) 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 (= G294) binding
- D478 (= D296) mutation to A: Abolishes catalytic activity.
- E674 (= E481) mutation to A: Abolishes catalytic activity.
- R686 (≠ A492) mutation to A: Decreases catalytic activity.
- E690 (= E496) mutation to A: Severely decreases catalytic activity.
- Y691 (= Y497) 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)
32% identity, 73% coverage: 117:508/534 of query aligns to 264:689/735 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.
4wvcA Crystal structure of gh63 mannosylglycerate hydrolase from thermus thermophilus hb8 in complex with tris and d-glycerate (see paper)
28% identity, 37% coverage: 315:510/534 of query aligns to 224:408/413 of 4wvcA
Sites not aligning to the query:
4wvbA Crystal structure of gh63 mannosylglycerate hydrolase from thermus thermophilus hb8 in complex with glucose (see paper)
28% identity, 37% coverage: 315:510/534 of query aligns to 205:389/394 of 4wvbA
Sites not aligning to the query:
Query Sequence
>GFF357 FitnessBrowser__psRCH2:GFF357
MTDIAPCQPFTYDVSAISLADTLTPAERYQELFVAVQMQCIFPDSKTFVDCAPLQHPEAI
LADYRGRCDEPGFDLAAFVREHFSLYEMPVKEFVANPDDSLAEHIDRLWPILTRHPQDHP
EHSSLLPLPHDYVVPGGRFTELYYWDSYFTMLGLDESGHCDLLRAMADNFAYLIDTYGHV
PNGNRTYYLGRSQPPVFALMTELFEETGVYRASDYLPQLHKEYAFWMDGADALRPGEAHR
RCVCLADGVVLNRYWDERDTPREESYREDVETARSSCRPRHEVYRDLRAGAESGWDFSSR
WLDDAHRLATIRTTSILPVDLNALLYKLERQIAELSAVKNQHACAEDFARRAAARLSAID
NYLWNPNAAAYFDYDWQRGRQRDNLTAATLAPLFVGMASAEQAAAVALTVQARLLVPGGL
ATTEIGGSGEQWDRPNGWAPLQWIGIRGLQRYGHDALALEIEERWLTIVSHLFERENKLV
EKYVLRPCTEHAGGGEYPLQDGFGWTNGVTRKLMQEDPGHEANRCRAGHCRTAS
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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