SitesBLAST
Comparing AO356_24205 FitnessBrowser__pseudo5_N2C3_1:AO356_24205 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 12 hits to proteins with known functional sites (download)
5z66A Structure of periplasmic trehalase from diamondback moth gut bacteria complexed with validoxylamine (see paper)
56% identity, 91% coverage: 40:531/541 of query aligns to 6:497/512 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 (= P149), F120 (= F153), Y124 (= Y157), W126 (= W159), D127 (= D160), N163 (= N196), Y169 (= Y202), Q174 (= Q207), R243 (= R277), E245 (= E279), G276 (= G310), D278 (= D312), W413 (= W447), E477 (= E511), Y478 (= Y512), F484 (= F518), W486 (= W520)
2jjbA Family 37 trehalase from escherichia coli in complex with casuarine-6- o-alpha-glucopyranose (see paper)
55% identity, 91% coverage: 39:529/541 of query aligns to 5:487/504 of 2jjbA
- binding casuarine: F113 (= F153), W119 (= W159), D120 (= D160), G270 (= G310), D272 (= D312), W407 (= W447), F476 (= F518), W478 (= W520)
- binding alpha-D-glucopyranose: R112 (= R152), Y117 (= Y157), N156 (= N196), Y162 (= Y202), R165 (= R205), R237 (= R277), E239 (= E279), D272 (= D312)
2jg0A Family 37 trehalase from escherichia coli in complex with 1- thiatrehazolin (see paper)
56% identity, 91% coverage: 39:529/541 of query aligns to 3:489/507 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 (= R152), F113 (= F153), Y117 (= Y157), W119 (= W159), D120 (= D160), N156 (= N196), Y162 (= Y202), R165 (= R205), R237 (= R277), E239 (= E279), A267 (= A307), G270 (= G310), D272 (= D312), W407 (= W447), E471 (= E511), Y472 (= Y512), F478 (= F518), W480 (= W520)
2jf4A Family 37 trehalase from escherichia coli in complex with validoxylamine (see paper)
56% identity, 91% coverage: 39:529/541 of query aligns to 3:482/500 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 (= F153), Y110 (= Y157), W112 (= W159), D113 (= D160), N149 (= N196), R158 (= R205), R230 (= R277), E232 (= E279), G263 (= G310), D265 (= D312), W400 (= W447), E464 (= E511), Y465 (= Y512), F471 (= F518), W473 (= W520)
2wynA Structure of family 37 trehalase from escherichia coli in complex with a casuarine-6-o-a-d-glucoside analogue (see paper)
56% identity, 91% coverage: 39:529/541 of query aligns to 5:489/506 of 2wynA
- binding alpha-D-glucopyranose: Y117 (= Y157), N156 (= N196), Y162 (= Y202), R165 (= R205), R237 (= R277), E239 (= E279)
- binding (1r,2r,3r,6r,7r,7ar)-3,7-bis(hydroxymethyl)hexahydro-1h-pyrrolizine-1,2,6-triol: F113 (= F153), W119 (= W159), D120 (= D160), G270 (= G310), D272 (= D312), W407 (= W447), Y472 (= Y512), F478 (= F518), W480 (= W520)
Q9W2M2 Trehalase; Alpha,alpha-trehalase; Alpha,alpha-trehalose glucohydrolase; EC 3.2.1.28 from Drosophila melanogaster (Fruit fly) (see paper)
34% identity, 91% coverage: 47:537/541 of query aligns to 61:582/596 of Q9W2M2
- N451 (≠ S415) modified: carbohydrate, N-linked (GlcNAc...) asparagine
7eawA Trehalase of arabidopsis thaliana acid mutant -d380a trehalose complex
34% identity, 73% coverage: 138:533/541 of query aligns to 136:543/560 of 7eawA
- binding alpha-D-glucopyranose: R150 (= R152), F151 (= F153), F151 (= F153), Y155 (= Y157), W157 (= W159), D158 (= D160), N194 (= N196), Y200 (= Y202), Q205 (= Q207), R270 (= R277), E272 (= E279), A301 (= A307), E506 (= E496), E521 (= E511), Y522 (= Y512), Y522 (= Y512)
5n6nC Crystal structure of the 14-3-3:neutral trehalase nth1 complex (see paper)
30% identity, 70% coverage: 145:523/541 of query aligns to 253:658/698 of 5n6nC
- binding beta-D-fructofuranose: F261 (= F153), N297 (≠ D189), H298 (≠ T190), G300 (= G192), K351 (= K236), D425 (= D312), Q570 (= Q446)
- binding alpha-D-glucopyranose: P257 (= P149), W267 (= W159), D268 (= D160), H298 (≠ T190), G423 (= G310), D425 (= D312), Q487 (= Q372), A529 (= A414), T530 (≠ S415), K531 (≠ A416), W571 (= W447), W655 (= W520)
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: 145:523/541 of query aligns to 295:711/751 of P32356
- WD 309:310 (= WD 159:160) binding
- N346 (= N196) binding
- RSQ 355:357 (= RSQ 205:207) binding
- E424 (≠ S264) binding
- R473 (≠ A307) binding
- S475 (= S309) 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 (= G310) binding
- D478 (= D312) mutation to A: Abolishes catalytic activity.
- E674 (= E496) 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)
30% identity, 70% coverage: 145:523/541 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.
4wvbA Crystal structure of gh63 mannosylglycerate hydrolase from thermus thermophilus hb8 in complex with glucose (see paper)
25% identity, 36% coverage: 332:526/541 of query aligns to 206:390/394 of 4wvbA
Sites not aligning to the query:
4wvcA Crystal structure of gh63 mannosylglycerate hydrolase from thermus thermophilus hb8 in complex with tris and d-glycerate (see paper)
25% identity, 36% coverage: 332:526/541 of query aligns to 225:409/413 of 4wvcA
Sites not aligning to the query:
Query Sequence
>AO356_24205 FitnessBrowser__pseudo5_N2C3_1:AO356_24205
MRPIELTSLSFATLLCVACSSQPPATWSYVDAQGRANLPPDQAYPELFEAVQRGQVFTDQ
KHFVDALPNRDPAQIRADYLARRDHDGFDIKAFVKDNFIESGQAESPAPKPGAPIQEHID
SLWPILSRSYSQVPAYSSLLPLPQPYVVPGGRFREMYYWDSYFTMLGLEQSGDKARVRQM
TDNFAYMIDTYGHIPNGNRTYYLSRSQPPFFAYMVALQARIEGDQAYGRYLPQLQKEYAY
WMAGAQALKPGAADRHVVKLADGSVLNRYWDASPTPRQESWLQDVRTAEQAPDRPKEEVW
RDLRAGAESGWDFSSRWLDDGQNLASIRTTAIVPVDLNSLIYHLEQTIAKACETVQNAPC
VQAYGRRAELRQRAIEQHLWNADKGFYVDYDWQRQQQRQQLTAATLFPLYTGLASAEHAH
RTADAVRDGLLRVAGIATTQVNTGQQWDEPNGWAPLQWVAVEGLDRYGHTALAQQVGSRF
LQQVENLYRKENKLVEKYDLSGRGDGGGGGEYELQDGFGWTNGVTLKLLGKYGKTSSTLG
E
Or try a new SitesBLAST search
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