SitesBLAST
Comparing N515DRAFT_1910 FitnessBrowser__Dyella79:N515DRAFT_1910 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 17 hits to proteins with known functional sites (download)
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, 93% coverage: 16:536/560 of query aligns to 170:714/751 of P32356
- T260 (≠ Q95) 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 130:131) binding
- N346 (= N167) binding
- RSQ 355:357 (= RSQ 176:178) binding
- E424 (= E245) binding
- R473 (= R321) 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 (= E504) mutation to A: Abolishes catalytic activity.
- R686 (= R516) mutation to A: Decreases catalytic activity.
- E690 (≠ G520) mutation to A: Severely decreases catalytic activity.
- Y691 (= Y521) 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.
5n6nC Crystal structure of the 14-3-3:neutral trehalase nth1 complex (see paper)
31% identity, 93% coverage: 16:536/560 of query aligns to 128:661/698 of 5n6nC
- binding beta-D-fructofuranose: K216 (≠ A93), I217 (= I94), F261 (= F124), N297 (≠ E160), H298 (= H161), G300 (= G163), K351 (≠ R215), D425 (= D326), Q570 (= Q454)
- binding alpha-D-glucopyranose: D188 (vs. gap), P257 (= P120), W267 (= W130), D268 (= D131), H298 (= H161), G423 (= G324), D425 (= D326), Q487 (≠ K381), A529 (= A423), T530 (≠ S424), K531 (≠ P425), W571 (= W455), W655 (= W530)
Sites not aligning to the query:
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)
34% identity, 84% coverage: 63:535/560 of query aligns to 234:691/735 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.
2jf4A Family 37 trehalase from escherichia coli in complex with validoxylamine (see paper)
32% identity, 80% coverage: 109:558/560 of query aligns to 91:498/500 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 (= F124), Y110 (= Y128), W112 (= W130), D113 (= D131), N149 (= N167), R158 (= R176), R230 (= R285), E232 (≠ A287), G263 (= G324), D265 (= D326), W400 (= W455), E464 (≠ A519), Y465 (≠ G520), F471 (= F528), W473 (= W530)
2jjbA Family 37 trehalase from escherichia coli in complex with casuarine-6- o-alpha-glucopyranose (see paper)
32% identity, 80% coverage: 109:558/560 of query aligns to 98:503/504 of 2jjbA
- binding casuarine: F113 (= F124), W119 (= W130), D120 (= D131), G270 (= G324), D272 (= D326), W407 (= W455), F476 (= F528), W478 (= W530)
- binding alpha-D-glucopyranose: R112 (≠ F123), Y117 (= Y128), N156 (= N167), Y162 (= Y173), R165 (= R176), R237 (= R285), E239 (≠ A287), D272 (= D326)
2jg0A Family 37 trehalase from escherichia coli in complex with 1- thiatrehazolin (see paper)
32% identity, 78% coverage: 109:542/560 of query aligns to 98:492/507 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 (≠ F123), F113 (= F124), Y117 (= Y128), W119 (= W130), D120 (= D131), N156 (= N167), Y162 (= Y173), R165 (= R176), R237 (= R285), E239 (≠ A287), A267 (≠ R321), G270 (= G324), D272 (= D326), W407 (= W455), E471 (≠ A519), Y472 (≠ G520), F478 (= F528), W480 (= W530)
2wynA Structure of family 37 trehalase from escherichia coli in complex with a casuarine-6-o-a-d-glucoside analogue (see paper)
32% identity, 78% coverage: 109:542/560 of query aligns to 98:492/506 of 2wynA
- binding alpha-D-glucopyranose: Y117 (= Y128), N156 (= N167), Y162 (= Y173), R165 (= R176), R237 (= R285), E239 (≠ A287)
- binding (1r,2r,3r,6r,7r,7ar)-3,7-bis(hydroxymethyl)hexahydro-1h-pyrrolizine-1,2,6-triol: F113 (= F124), W119 (= W130), D120 (= D131), G270 (= G324), D272 (= D326), W407 (= W455), Y472 (≠ G520), F478 (= F528), W480 (= W530)
5z66A Structure of periplasmic trehalase from diamondback moth gut bacteria complexed with validoxylamine (see paper)
31% identity, 80% coverage: 109:558/560 of query aligns to 105:511/512 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 (= P120), F120 (= F124), Y124 (= Y128), W126 (= W130), D127 (= D131), N163 (= N167), Y169 (= Y173), Q174 (= Q178), R243 (≠ K255), E245 (≠ I257), G276 (= G324), D278 (= D326), W413 (= W455), E477 (≠ A519), Y478 (≠ G520), F484 (= F528), W486 (= W530)
Q9W2M2 Trehalase; Alpha,alpha-trehalase; Alpha,alpha-trehalose glucohydrolase; EC 3.2.1.28 from Drosophila melanogaster (Fruit fly) (see paper)
27% identity, 82% coverage: 81:537/560 of query aligns to 150:572/596 of Q9W2M2
- N451 (≠ S424) modified: carbohydrate, N-linked (GlcNAc...) asparagine
7eawA Trehalase of arabidopsis thaliana acid mutant -d380a trehalose complex
26% identity, 77% coverage: 110:540/560 of query aligns to 137:540/560 of 7eawA
- binding alpha-D-glucopyranose: R150 (≠ F123), F151 (= F124), F151 (= F124), Y155 (= Y128), W157 (= W130), D158 (= D131), N194 (= N167), Y200 (= Y173), Q205 (= Q178), R270 (≠ V243), E272 (= E245), A301 (= A287), E506 (= E504), E521 (≠ A519), Y522 (≠ G520), Y522 (≠ G520)
3w7uA Escherichia coli k12 ygjk complexed with galactose (see paper)
26% identity, 55% coverage: 203:511/560 of query aligns to 409:734/760 of 3w7uA
Sites not aligning to the query:
3w7tA Escherichia coli k12 ygjk complexed with mannose (see paper)
26% identity, 55% coverage: 203:511/560 of query aligns to 409:734/760 of 3w7tA
Sites not aligning to the query:
- binding beta-D-mannopyranose: 77, 134, 215, 308, 315, 321, 321, 323, 324, 368, 391, 391, 744
3w7sA Escherichia coli k12 ygjk complexed with glucose (see paper)
26% identity, 55% coverage: 203:511/560 of query aligns to 409:734/760 of 3w7sA
Sites not aligning to the query:
- binding alpha-D-glucopyranose: 3, 90, 97, 99, 321, 338, 341, 349, 350, 351, 352, 353, 356, 368, 378, 384, 386, 391
6xuxA Crystal structure of megabody mb-nb207-cygjk_no (see paper)
31% identity, 30% coverage: 343:511/560 of query aligns to 98:282/879 of 6xuxA
Sites not aligning to the query:
5gw7B Crystal structure of the glycosynthase mutant e727a of escherichia coli gh63 glycosidase in complex with glucose and lactose (see paper)
26% identity, 55% coverage: 203:511/560 of query aligns to 409:734/760 of 5gw7B
Sites not aligning to the query:
4wvbA Crystal structure of gh63 mannosylglycerate hydrolase from thermus thermophilus hb8 in complex with glucose (see paper)
29% identity, 35% coverage: 337:532/560 of query aligns to 202:394/394 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)
29% identity, 35% coverage: 337:532/560 of query aligns to 221:413/413 of 4wvcA
Sites not aligning to the query:
Query Sequence
>N515DRAFT_1910 FitnessBrowser__Dyella79:N515DRAFT_1910
MTRSPHLLRAVLFAAIFTAAATQAATPDPAKTRAYIDQAWTTLTRSQDQCNALTDPKIAG
HPVLYVPAEMKVPSTLADIGKRCGVDIRPLPRAIQRLGDIDATKLPAQGLLYLPHPYVVP
GGFFNEMYGWDSYFIVLGLAADQRGKLARDMVDNALFEVEHYGAVLNANRTYYLSRSQPP
FLTAMMATVLGDPDAFASDAERKAWLAGAYPLAVRNHDVWTREEHRAGDTGLARYYDLGD
GPVLEAQNSDDFYVKVIKWLRAHPKDDPGYLLKGAQQPDDAEAARLAKDSCDVRASKVCL
GNWHDGYRLTADYYRGDRAMRESGYDTNFHFGPFGGSTHHYASVDLNSLLYRYELDLADF
ATKLGKSDEAKRWTDAAAARKQAMDKYLWRAGDGMYRDYDFVAGKPSPTPYINTFYPLWA
GAASPQQAAAVRGKLAVFERRGGLSMDNQPSGVQWNDPFGWAPTNWLAIKGLEDYGFHDD
ARRLAGNFTATVDRGLADDGTIREKYNMAKGNADVRVSAGYSENVIGFGWTNGVYLKLQE
ILQRNKAEPAPTPRVPETAK
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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