SitesBLAST
Comparing N515DRAFT_1228 FitnessBrowser__Dyella79:N515DRAFT_1228 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 20 (the maximum) hits to proteins with known functional sites (download)
Q8VZR6 Inositol transporter 1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
36% identity, 93% coverage: 21:450/463 of query aligns to 35:477/509 of Q8VZR6
Sites not aligning to the query:
- 479:509 mutation Missing: Leads to endoplasmic reticulum relocalization.
- 481:482 ER→AA: No effect on targeting.
- 500:509 mutation Missing: Leads to endoplasmic reticulum relocalization.
- 502:504 mutation LLE->AAA,SSS: Leads to plasma membrane relocalization.
A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
35% identity, 90% coverage: 34:452/463 of query aligns to 22:437/446 of A0A0H2VG78
- D22 (= D34) mutation to N: Affects symport activity. May function as an uniporter.
- R102 (= R114) mutation to A: Loss of transport activity.
- I105 (≠ L117) mutation to S: Affects symport activity. May function as an uniporter.
- E122 (= E134) mutation to A: Loss of transport activity.
- Q137 (= Q149) mutation to A: Loss of transport activity.
- Q250 (= Q264) mutation to A: Loss of transport activity.
- Q251 (= Q265) mutation to A: Loss of transport activity.
- N256 (= N270) mutation to A: Loss of transport activity.
- W357 (= W372) mutation to A: Loss of transport activity.
7aaqA Sugar/h+ symporter stp10 in outward occluded conformation (see paper)
32% identity, 95% coverage: 13:450/463 of query aligns to 1:467/487 of 7aaqA
Q9LT15 Sugar transport protein 10; AtSTP10; D-glucose-H(+) symport protein STP10; D-glucose-proton symporter STP10; Hexose transporter 10 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
32% identity, 95% coverage: 13:450/463 of query aligns to 21:487/514 of Q9LT15
- F39 (= F31) mutation to A: Reduces affinity for glucose 8-fold.
- L43 (≠ I35) mutation to A: Reduces affinity for glucose 150-fold and turns STP10 into a low affinity transporter.
- C77 (vs. gap) modified: Disulfide link with 449; mutation to A: Increases sensitivity to alkaline pH and can only function fully at acidic pH (pH < 5).
- E162 (= E134) mutation to Q: Abolishes glucose transport activity; when associated with N-344.
- Q177 (= Q149) binding ; mutation to A: Reduces affinity for glucose 37-fold.
- I184 (= I156) mutation to A: Reduces affinity for glucose 3-fold.
- Q295 (= Q264) binding
- Q296 (= Q265) binding
- N301 (= N270) binding
- N332 (= N301) binding
- D344 (= D313) mutation to N: Abolishes glucose transport activity; when associated with Q-162.
- W410 (= W372) binding
- C449 (≠ N411) modified: Disulfide link with 77; mutation to A: Increases sensitivity to alkaline pH and can only function fully at acidic pH (pH < 5).
7aarA Sugar/h+ symporter stp10 in inward open conformation (see paper)
31% identity, 95% coverage: 13:450/463 of query aligns to 6:472/485 of 7aarA
- binding Octyl Glucose Neopentyl Glycol : L28 (≠ I35), I90 (≠ L77), H94 (≠ L81), V98 (≠ R85), F101 (≠ I88), N138 (≠ T125), P142 (= P129), N158 (≠ I145), F161 (≠ Y148), Q162 (= Q149), I165 (= I152), D210 (= D195), G391 (= G368), P392 (= P369), W395 (= W372), M419 (≠ W396)
- binding beta-D-glucopyranose: Q280 (= Q264), N286 (= N270), M289 (= M273), G391 (= G368), W395 (= W372)
P0AGF4 D-xylose-proton symporter; D-xylose transporter from Escherichia coli (strain K12) (see paper)
31% identity, 95% coverage: 10:449/463 of query aligns to 3:475/491 of P0AGF4
- F24 (= F31) mutation to A: Decreases xylose transport.
- G83 (= G82) mutation to A: Abolishes xylose transport.
- R133 (= R114) mutation R->C,H,L: Abolishes xylose transport.
- E153 (= E134) mutation to A: Abolishes xylose transport.
- R160 (= R141) mutation to A: Abolishes xylose transport.
- Q168 (= Q149) binding ; mutation to A: Abolishes xylose transport.
- Q288 (= Q264) mutation to A: Abolishes xylose transport.
- QQ 288:289 (= QQ 264:265) binding
- Q289 (= Q265) mutation to A: Strongly decreases xylose transport.
- N294 (= N270) binding ; mutation to A: Abolishes xylose transport.
- Y298 (= Y274) mutation to A: Abolishes xylose transport.
- N325 (= N301) mutation to A: No effect on xylose transport.
- G340 (= G316) mutation to A: Abolishes xylose transport.
- R341 (= R317) mutation R->A,W: Abolishes xylose transport.
- W392 (= W372) binding ; mutation to A: Abolishes xylose transport.
- E397 (= E377) mutation to A: Abolishes xylose transport.
- R404 (= R384) mutation to A: Strongly decreases xylose transport.
- Q415 (≠ N395) binding
- W416 (= W396) mutation to A: Strongly decreases xylose transport.
4gc0A The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to 6-bromo-6-deoxy-d-glucose (see paper)
31% identity, 92% coverage: 22:449/463 of query aligns to 11:471/475 of 4gc0A
4gbzA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-glucose (see paper)
31% identity, 92% coverage: 22:449/463 of query aligns to 11:471/475 of 4gbzA
4gbyA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-xylose (see paper)
31% identity, 92% coverage: 22:449/463 of query aligns to 11:471/475 of 4gbyA
Q9C757 Probable inositol transporter 2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
37% identity, 67% coverage: 24:335/463 of query aligns to 35:358/580 of Q9C757
Sites not aligning to the query:
- 399 C→A: Strongly decreased nickel inhibition; when associated with A-402, A-410 and A-413.; C→S: No effect on inostol transport or nickel inhibition. No effect on inostol transport or nickel inhibition; when associated with S-410.
- 402 C→A: Strongly decreased nickel inhibition; when associated with A-399, A-410 and A-413.
- 410 C→A: Strongly decreased nickel inhibition; when associated with A-399, A-402 and A-413.; C→S: No effect on inostol transport or nickel inhibition; when associated with S-399.
- 413 C→A: Strongly decreased nickel inhibition; when associated with A-399, A-402 and A-410.
P11169 Solute carrier family 2, facilitated glucose transporter member 3; Glucose transporter type 3, brain; GLUT-3 from Homo sapiens (Human) (see paper)
29% identity, 95% coverage: 10:450/463 of query aligns to 3:463/496 of P11169
- Q159 (= Q149) binding
- QLS 277:279 (≠ QIM 261:263) Important for selectivity against fructose; mutation to HVA: Confers moderate fructose transport activity.
- QQ 280:281 (= QQ 264:265) binding
- N286 (= N270) binding
- N315 (= N301) binding
- E378 (≠ A364) binding
- W386 (= W372) binding
7sptA Crystal structure of exofacial state human glucose transporter glut3 (see paper)
29% identity, 95% coverage: 10:450/463 of query aligns to 3:463/470 of 7sptA
4zw9A Crystal structure of human glut3 bound to d-glucose in the outward- occluded conformation at 1.5 angstrom (see paper)
29% identity, 95% coverage: 10:450/463 of query aligns to 3:463/470 of 4zw9A
- binding beta-D-glucopyranose: Q159 (= Q149), I166 (= I156), Q280 (= Q264), Q281 (= Q265), N286 (= N270), F377 (= F363), W386 (= W372)
- binding alpha-D-glucopyranose: Q159 (= Q149), I162 (= I152), I166 (= I156), Q280 (= Q264), Q281 (= Q265), N286 (= N270), W386 (= W372)
O23492 Inositol transporter 4; Myo-inositol-proton symporter INT4; Protein INOSITOL TRANSPORTER 4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
36% identity, 64% coverage: 24:321/463 of query aligns to 34:346/582 of O23492
Sites not aligning to the query:
- 559:561 LLE→AAA: No effect on targeting.
- 559:582 mutation Missing: No effect on targeting.
- 564:565 FK→AA: No effect on targeting.
- 570:575 RRREKK→AAAAAA: No effect on targeting.
7crzA Crystal structure of human glucose transporter glut3 bound with c3361 (see paper)
29% identity, 95% coverage: 10:450/463 of query aligns to 1:461/469 of 7crzA
- binding (2S,3R,4S,5R,6R)-6-(hydroxymethyl)-4-undec-10-enoxy-oxane-2,3,5-triol: T26 (≠ I35), A66 (≠ M63), S69 (vs. gap), Q157 (= Q149), I164 (= I156), Q278 (= Q264), Q279 (= Q265), N284 (= N270), N313 (= N301), F375 (= F363), W384 (= W372), N411 (= N399), F412 (≠ M400), G415 (= G403)
7spsA Crystal structure of human glucose transporter glut3 bound with exofacial inhibitor sa47 (see paper)
29% identity, 95% coverage: 12:450/463 of query aligns to 2:460/468 of 7spsA
- binding methyl N-[(2-{4-[4-(5-fluoro-2-methoxyphenyl)piperazin-1-yl]-1H-pyrazolo[3,4-d]pyrimidin-1-yl}phenyl)methyl]-beta-alaninate: F21 (= F31), T25 (≠ I35), N29 (≠ S39), Q156 (= Q149), I163 (= I156), Q278 (= Q265), F286 (≠ M273), A308 (≠ V297), N312 (= N301), F374 (= F363), E375 (≠ A364), N406 (= N395), W407 (= W396), N410 (= N399)
5c65A Structure of the human glucose transporter glut3 / slc2a3
29% identity, 95% coverage: 12:450/463 of query aligns to 1:451/457 of 5c65A
- binding Octyl Glucose Neopentyl Glycol : L42 (≠ I51), L58 (≠ E57), F75 (≠ L72), S76 (≠ G73), L79 (≠ W76), R87 (≠ K84), L95 (≠ I92), L96 (= L93), L121 (≠ V115), P199 (≠ L191)
- binding cholesterol hemisuccinate: I270 (≠ A258), S396 (≠ T394), T399 (≠ I397)
P32037 Solute carrier family 2, facilitated glucose transporter member 3; Glucose transporter type 3, brain; GLUT-3 from Mus musculus (Mouse) (see paper)
29% identity, 95% coverage: 10:450/463 of query aligns to 3:463/493 of P32037
- N43 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
P17809 Solute carrier family 2, facilitated glucose transporter member 1; Glucose transporter type 1, erythrocyte/brain; GLUT-1; GT1 from Mus musculus (Mouse) (see 3 papers)
28% identity, 96% coverage: 10:455/463 of query aligns to 5:470/492 of P17809
- N45 (≠ A50) modified: carbohydrate, N-linked (GlcNAc...) asparagine
Sites not aligning to the query:
- 485 P→L: Lethality immediately after birth in knockin mice; caused by creation of a dileucine internalization motif that promotes mislocalization of the protein.
P11168 Solute carrier family 2, facilitated glucose transporter member 2; Glucose transporter type 2, liver; GLUT-2 from Homo sapiens (Human) (see 6 papers)
28% identity, 94% coverage: 12:448/463 of query aligns to 5:495/524 of P11168
- P68 (vs. gap) to L: in dbSNP:rs7637863
- T110 (≠ V69) to I: in dbSNP:rs5400
- V197 (≠ T153) to I: in NIDDM; abolishes transport activity of the transporter expressed in Xenopus oocytes; dbSNP:rs121909741
- I322 (≠ V272) mutation to V: Reduced fructose transport.
Query Sequence
>N515DRAFT_1228 FitnessBrowser__Dyella79:N515DRAFT_1228
MNSQAIATPTAHVKGTVIYTCVLAALAGLMFGLDIGVISGASQFIKAEFAISDHTIEWIV
SSMMFGAAVGALGAGWLSSHLGRKRSLILGAILFVIGSLLCGLAWSPETLIAARVILGLA
IGIATFTAPLYLAEVAPEHIRGAMISTYQLMITIGILVAFLSDTALSYHGAWRWMLGVIA
IPGALFLLGVLGLPDSPRWLMMRGRRDEAIDVLRRLRGDEVVVAREAADIEEQLKTPQRG
WDLFAENPNFRRSVFLGALLQIMQQFTGMNVVMYYAPRIFQEMGYDTAAQMWFTALVGLT
NVLATFIAIALIDRWGRKPILYTGFAVMAVGLGVVGALMNGGINGQTEQYTCVAMLLFFI
VGFAMSAGPLVWTLCSEIQPLKGRDFGIGVSTFTNWITNMVVGFTFLSLLNTIGNASTFW
LYAALNAVFIVLTFWLVPETKGVTLEQIERNLMAGKRLRDIGR
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