SitesBLAST
Comparing H281DRAFT_02882 FitnessBrowser__Burk376:H281DRAFT_02882 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
51% identity, 80% coverage: 83:583/627 of query aligns to 1:489/504 of 2jjbA
- binding casuarine: F113 (= F203), W119 (= W209), D120 (= D210), G270 (= G360), D272 (= D362), W407 (= W497), F476 (= F570), W478 (= W572)
- binding alpha-D-glucopyranose: R112 (= R202), Y117 (= Y207), N156 (= N246), Y162 (= Y252), R165 (= R255), R237 (= R327), E239 (= E329), D272 (= D362)
2jg0A Family 37 trehalase from escherichia coli in complex with 1- thiatrehazolin (see paper)
51% identity, 80% coverage: 85:583/627 of query aligns to 1:491/507 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 (= R202), F113 (= F203), Y117 (= Y207), W119 (= W209), D120 (= D210), N156 (= N246), Y162 (= Y252), R165 (= R255), R237 (= R327), E239 (= E329), A267 (≠ G357), G270 (= G360), D272 (= D362), W407 (= W497), E471 (= E563), Y472 (= Y564), F478 (= F570), W480 (= W572)
2jf4A Family 37 trehalase from escherichia coli in complex with validoxylamine (see paper)
50% identity, 80% coverage: 85:583/627 of query aligns to 1:484/500 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 (= F203), Y110 (= Y207), W112 (= W209), D113 (= D210), N149 (= N246), R158 (= R255), R230 (= R327), E232 (= E329), G263 (= G360), D265 (= D362), W400 (= W497), E464 (= E563), Y465 (= Y564), F471 (= F570), W473 (= W572)
2wynA Structure of family 37 trehalase from escherichia coli in complex with a casuarine-6-o-a-d-glucoside analogue (see paper)
51% identity, 80% coverage: 83:583/627 of query aligns to 1:491/506 of 2wynA
- binding alpha-D-glucopyranose: Y117 (= Y207), N156 (= N246), Y162 (= Y252), R165 (= R255), R237 (= R327), E239 (= E329)
- binding (1r,2r,3r,6r,7r,7ar)-3,7-bis(hydroxymethyl)hexahydro-1h-pyrrolizine-1,2,6-triol: F113 (= F203), W119 (= W209), D120 (= D210), G270 (= G360), D272 (= D362), W407 (= W497), Y472 (= Y564), F478 (= F570), W480 (= W572)
5z66A Structure of periplasmic trehalase from diamondback moth gut bacteria complexed with validoxylamine (see paper)
49% identity, 80% coverage: 95:595/627 of query aligns to 13:506/512 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 (= P199), F120 (= F203), Y124 (= Y207), W126 (= W209), D127 (= D210), N163 (= N246), Y169 (= Y252), Q174 (= Q257), R243 (= R327), E245 (= E329), G276 (= G360), D278 (= D362), W413 (= W497), E477 (= E563), Y478 (= Y564), F484 (= F570), W486 (= W572)
Q9W2M2 Trehalase; Alpha,alpha-trehalase; Alpha,alpha-trehalose glucohydrolase; EC 3.2.1.28 from Drosophila melanogaster (Fruit fly) (see paper)
33% identity, 78% coverage: 94:582/627 of query aligns to 60:575/596 of Q9W2M2
- N451 (≠ S465) modified: carbohydrate, N-linked (GlcNAc...) asparagine
7eawA Trehalase of arabidopsis thaliana acid mutant -d380a trehalose complex
31% identity, 76% coverage: 106:584/627 of query aligns to 32:542/560 of 7eawA
- binding alpha-D-glucopyranose: R150 (= R202), F151 (= F203), F151 (= F203), Y155 (= Y207), W157 (= W209), D158 (= D210), N194 (= N246), Y200 (= Y252), Q205 (= Q257), R270 (= R327), E272 (= E329), A301 (≠ G357), E506 (= E546), E521 (≠ G562), Y522 (≠ E563), Y522 (≠ E563)
5n6nC Crystal structure of the 14-3-3:neutral trehalase nth1 complex (see paper)
27% identity, 75% coverage: 106:574/627 of query aligns to 176:657/698 of 5n6nC
- binding beta-D-fructofuranose: K216 (≠ R151), I217 (≠ M152), F261 (= F203), N297 (= N239), H298 (≠ R240), G300 (= G242), K351 (≠ Q285), D425 (= D362), Q570 (= Q496)
- binding alpha-D-glucopyranose: D188 (≠ A118), P257 (= P199), W267 (= W209), D268 (= D210), H298 (≠ R240), G423 (= G360), D425 (= D362), Q487 (≠ A422), A529 (= A464), T530 (≠ S465), K531 (≠ R466), W571 (= W497), W655 (= W572)
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)
27% identity, 75% coverage: 106:574/627 of query aligns to 218:710/751 of P32356
- T260 (≠ S153) mutation to A: Abolishes activity; when associated with A-20; A-21; A-58; A-60; A-83; A-135; A-149 and A-475.
- WD 309:310 (= WD 209:210) binding
- N346 (= N246) binding
- RSQ 355:357 (= RSQ 255:257) binding
- E424 (≠ A311) binding
- R473 (≠ G357) binding
- S475 (≠ T359) 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 (= G360) binding
- D478 (= D362) mutation to A: Abolishes catalytic activity.
- E674 (= E546) mutation to A: Abolishes catalytic activity.
- R686 (vs. gap) mutation to A: Decreases catalytic activity.
- E690 (≠ S554) mutation to A: Severely decreases catalytic activity.
- Y691 (≠ P555) 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.
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, 60% coverage: 196:574/627 of query aligns to 277:688/735 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
>H281DRAFT_02882 FitnessBrowser__Burk376:H281DRAFT_02882
MTVHAFAAVARLHLRRALTLHVARPGAWLGTTPVAAHVAALAAALMLHASIAAAAPAADA
APQASGITRVALHVEPPVQASPVVPVPPSEQYPDLYRDVQLAHLYPDSKTFADMVPLAPP
AQIAAAYETARQQPGFNLGDFVKRNFTLPVRMSKSYVSDPNEDVVSHIDTLWNVLRREPD
AAASPWSSLLPLPDAYIVPGDRFDEIYYWDSYFIMLGLEASGHHAWVVDELKNFATLINR
YGHIPNGNRTYYLSRSQPPFFAQMVRLVAEKDGDAVYAQYLPELQREYAYWMDGSEGLPA
GHANRHVVRLADGSLLNRYWDERAAPRDESYREDIATSQQTPQRNADDLWRNLRAGGETG
WDFSSRWFADGKTLATVDVTSLAPIDLNCLIVDLERALAKAYRVRGDVTHAENMSQRAAT
RADTIRRVLWDPQLQAFGDYDFVHRTLTHRLTAATVYPLYTGVASRQQAKAVAATLQREL
LRPGGLATTRVATGQQWDAPNGWAPLQYLAVIGLRRYSEPALAQTIATRWIKTNVSYYQH
TGKLVEKYDVDAASPGVSAGGGEYPLQDGFGWTNGVLRTLLALYPQAAGTSRPSDIPAGP
AGVSAAAASAAAASKNTHRLQGTRVNP
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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