SitesBLAST
Comparing BWI76_RS26700 FitnessBrowser__Koxy:BWI76_RS26700 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)
5z66A Structure of periplasmic trehalase from diamondback moth gut bacteria complexed with validoxylamine (see paper)
51% identity, 88% coverage: 62:543/550 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 (= P165), F120 (= F169), Y124 (= Y173), W126 (= W175), D127 (= D176), N163 (= N212), Y169 (= Y218), Q174 (= Q223), R243 (= R292), E245 (= E294), G276 (= G324), D278 (= D326), W413 (= W460), E477 (= E525), Y478 (= Y526), F484 (= F532), W486 (= W534)
2jjbA Family 37 trehalase from escherichia coli in complex with casuarine-6- o-alpha-glucopyranose (see paper)
51% identity, 88% coverage: 62:545/550 of query aligns to 13:489/504 of 2jjbA
- binding casuarine: F113 (= F169), W119 (= W175), D120 (= D176), G270 (= G324), D272 (= D326), W407 (= W460), F476 (= F532), W478 (= W534)
- binding alpha-D-glucopyranose: R112 (= R168), Y117 (= Y173), N156 (= N212), Y162 (= Y218), R165 (= R221), R237 (= R292), E239 (= E294), D272 (= D326)
2jg0A Family 37 trehalase from escherichia coli in complex with 1- thiatrehazolin (see paper)
51% identity, 88% coverage: 62:545/550 of query aligns to 11:491/507 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 (= R168), F113 (= F169), Y117 (= Y173), W119 (= W175), D120 (= D176), N156 (= N212), Y162 (= Y218), R165 (= R221), R237 (= R292), E239 (= E294), A267 (= A321), G270 (= G324), D272 (= D326), W407 (= W460), E471 (= E525), Y472 (= Y526), F478 (= F532), W480 (= W534)
2jf4A Family 37 trehalase from escherichia coli in complex with validoxylamine (see paper)
51% identity, 88% coverage: 62:545/550 of query aligns to 11:484/500 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 (= F169), Y110 (= Y173), W112 (= W175), D113 (= D176), N149 (= N212), R158 (= R221), R230 (= R292), E232 (= E294), G263 (= G324), D265 (= D326), W400 (= W460), E464 (= E525), Y465 (= Y526), F471 (= F532), W473 (= W534)
2wynA Structure of family 37 trehalase from escherichia coli in complex with a casuarine-6-o-a-d-glucoside analogue (see paper)
51% identity, 88% coverage: 62:545/550 of query aligns to 13:491/506 of 2wynA
- binding alpha-D-glucopyranose: Y117 (= Y173), N156 (= N212), Y162 (= Y218), R165 (= R221), R237 (= R292), E239 (= E294)
- binding (1r,2r,3r,6r,7r,7ar)-3,7-bis(hydroxymethyl)hexahydro-1h-pyrrolizine-1,2,6-triol: F113 (= F169), W119 (= W175), D120 (= D176), G270 (= G324), D272 (= D326), W407 (= W460), Y472 (= Y526), F478 (= F532), W480 (= W534)
Q9W2M2 Trehalase; Alpha,alpha-trehalase; Alpha,alpha-trehalose glucohydrolase; EC 3.2.1.28 from Drosophila melanogaster (Fruit fly) (see paper)
31% identity, 91% coverage: 49:547/550 of query aligns to 46:578/596 of Q9W2M2
- N451 (≠ T428) modified: carbohydrate, N-linked (GlcNAc...) asparagine
7eawA Trehalase of arabidopsis thaliana acid mutant -d380a trehalose complex
32% identity, 82% coverage: 100:549/550 of query aligns to 62:545/560 of 7eawA
- binding alpha-D-glucopyranose: R150 (= R168), F151 (= F169), F151 (= F169), Y155 (= Y173), W157 (= W175), D158 (= D176), N194 (= N212), Y200 (= Y218), Q205 (= Q223), R270 (= R292), E272 (= E294), A301 (= A321), E506 (= E509), E521 (≠ G524), Y522 (≠ E525), Y522 (≠ E525)
5n6nC Crystal structure of the 14-3-3:neutral trehalase nth1 complex (see paper)
31% identity, 70% coverage: 154:537/550 of query aligns to 248:658/698 of 5n6nC
- binding beta-D-fructofuranose: F261 (= F169), N297 (≠ E205), H298 (≠ I206), G300 (= G208), K351 (≠ D258), D425 (= D326), Q570 (= Q459)
- binding alpha-D-glucopyranose: P257 (= P165), W267 (= W175), D268 (= D176), H298 (≠ I206), G423 (= G324), D425 (= D326), Q487 (≠ R386), A529 (= A427), T530 (= T428), K531 (≠ H429), W571 (= W460), W655 (= W534)
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)
31% identity, 70% coverage: 154:537/550 of query aligns to 290:711/751 of P32356
- WD 309:310 (= WD 175:176) binding
- N346 (= N212) binding
- RSQ 355:357 (= RSQ 221:223) binding
- E424 (vs. gap) binding
- R473 (≠ A321) binding
- S475 (= S323) 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 (= G324) binding
- D478 (= D326) mutation to A: Abolishes catalytic activity.
- E674 (= E509) mutation to A: Abolishes catalytic activity.
- R686 (vs. gap) mutation to A: Decreases catalytic activity.
- E690 (vs. gap) mutation to A: Severely decreases catalytic activity.
- Y691 (vs. gap) 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)
29% identity, 77% coverage: 114:537/550 of query aligns to 236:689/735 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
>BWI76_RS26700 FitnessBrowser__Koxy:BWI76_RS26700
MFSQKLRNVDDDELRIENDPCYEADPYELKLDEMFDAEPEPEIIEGLPASDALTPADRYL
ELFAHVQKSRIFADSKTFPDCAPKQDPLDILIHYRRVRRTPGFDLRQFVEDHFWLPDSRA
EDYVSDPNRSLKEHIDNLWPVLTREPQDHIPWSSLLALPQSYIVPGGRFSETYYWDSYFT
MLGLAESGREDLLKCMADNFAWMIEIYGHIPNGNRTYYLSRSQPPVFALMVELFEEDGVR
GAKRYLDHLQMEYSFWMDGAESLIPNQAYRHVVRMPDGSLLNRYWDDRDTPRDESWREDV
ETAKHSGRPPNEVYRDLRAGAESGWDYSSRWLRDITRLASIRTTQFIPIDLNAFLFKLEN
TIANLSGLKGDRETEAAFRQKASDRRAAVTRYLWDDESGCFRDYDWRREQLALFSAASIV
ALYVGMATHEQADRLADAVRARLLTPGGIMATEYESGEQWDKPNGWAPLQWMAVQGFKMY
GQDPLGDEIAQSWLQTVNHYYKQHYKLIEKYHIASATPHEGGGGEYPLQDGFGWTNGVVR
RLIGLYGEPL
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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