SitesBLAST
Comparing 16922 FitnessBrowser__Keio:16922 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)
37% identity, 93% coverage: 19:459/472 of query aligns to 21:477/509 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)
33% identity, 90% coverage: 39:461/472 of query aligns to 22:437/446 of A0A0H2VG78
- D22 (= D39) mutation to N: Affects symport activity. May function as an uniporter.
- R102 (= R119) mutation to A: Loss of transport activity.
- I105 (≠ L122) mutation to S: Affects symport activity. May function as an uniporter.
- E122 (= E139) mutation to A: Loss of transport activity.
- Q137 (= Q154) mutation to A: Loss of transport activity.
- Q250 (= Q269) mutation to A: Loss of transport activity.
- Q251 (= Q270) mutation to A: Loss of transport activity.
- N256 (= N275) mutation to A: Loss of transport activity.
- W357 (= W381) mutation to A: Loss of transport activity.
P0AGF4 D-xylose-proton symporter; D-xylose transporter from Escherichia coli (strain K12) (see paper)
31% identity, 92% coverage: 25:458/472 of query aligns to 13:475/491 of P0AGF4
- F24 (= F36) mutation to A: Decreases xylose transport.
- G83 (= G87) mutation to A: Abolishes xylose transport.
- R133 (= R119) mutation R->C,H,L: Abolishes xylose transport.
- E153 (= E139) mutation to A: Abolishes xylose transport.
- R160 (= R146) mutation to A: Abolishes xylose transport.
- Q168 (= Q154) binding beta-D-xylose; mutation to A: Abolishes xylose transport.
- Q288 (= Q269) mutation to A: Abolishes xylose transport.
- QQ 288:289 (= QQ 269:270) binding beta-D-xylose
- Q289 (= Q270) mutation to A: Strongly decreases xylose transport.
- N294 (= N275) binding beta-D-xylose; mutation to A: Abolishes xylose transport.
- Y298 (= Y279) mutation to A: Abolishes xylose transport.
- N325 (≠ F307) mutation to A: No effect on xylose transport.
- G340 (= G322) mutation to A: Abolishes xylose transport.
- R341 (= R323) mutation R->A,W: Abolishes xylose transport.
- W392 (= W381) binding beta-D-xylose; mutation to A: Abolishes xylose transport.
- E397 (= E386) mutation to A: Abolishes xylose transport.
- R404 (= R393) mutation to A: Strongly decreases xylose transport.
- Q415 (≠ N404) binding beta-D-xylose
- W416 (= W405) 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: 25:458/472 of query aligns to 9:471/475 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: 25:458/472 of query aligns to 9:471/475 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: 25:458/472 of query aligns to 9:471/475 of 4gbyA
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)
30% identity, 92% coverage: 27:459/472 of query aligns to 30:487/514 of Q9LT15
- F39 (= F36) mutation to A: Reduces affinity for glucose 8-fold.
- L43 (≠ I40) 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 (= E139) mutation to Q: Abolishes glucose transport activity; when associated with N-344.
- Q177 (= Q154) binding beta-D-glucose; mutation to A: Reduces affinity for glucose 37-fold.
- I184 (= I161) mutation to A: Reduces affinity for glucose 3-fold.
- Q295 (= Q269) binding beta-D-glucose
- Q296 (= Q270) binding beta-D-glucose
- N301 (= N275) binding beta-D-glucose
- N332 (≠ F307) binding beta-D-glucose
- D344 (= D319) mutation to N: Abolishes glucose transport activity; when associated with Q-162.
- W410 (= W381) binding beta-D-glucose
- C449 (≠ D420) modified: Disulfide link with 77; mutation to A: Increases sensitivity to alkaline pH and can only function fully at acidic pH (pH < 5).
7aaqA Sugar/h+ symporter stp10 in outward occluded conformation (see paper)
30% identity, 92% coverage: 27:459/472 of query aligns to 10:467/487 of 7aaqA
Q9C757 Probable inositol transporter 2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
38% identity, 67% coverage: 25:339/472 of query aligns to 31:358/580 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.
7aarA Sugar/h+ symporter stp10 in inward open conformation (see paper)
29% identity, 92% coverage: 27:459/472 of query aligns to 15:472/485 of 7aarA
- binding Octyl Glucose Neopentyl Glycol : L28 (≠ I40), I90 (≠ L82), H94 (≠ L86), V98 (≠ Y90), F101 (≠ M93), N138 (≠ S130), P142 (= P134), N158 (≠ I150), F161 (≠ Y153), Q162 (= Q154), I165 (≠ V157), D210 (≠ N200), G391 (≠ A377), P392 (= P378), W395 (= W381), M419 (≠ W405)
- binding beta-D-glucopyranose: Q280 (= Q269), N286 (= N275), M289 (= M278), G391 (≠ A377), W395 (= W381)
A1Z8N1 Trehalose transporter 1; Facilitated trehalose transporter Tret1-1; DmTret1-1 from Drosophila melanogaster (Fruit fly) (see paper)
33% identity, 80% coverage: 86:463/472 of query aligns to 464:839/857 of A1Z8N1
Sites not aligning to the query:
- 248 modified: Phosphoserine
- 249 modified: Phosphoserine
- 250 modified: Phosphoserine
- 320 modified: Phosphoserine
- 322 modified: Phosphoserine
- 845 modified: Phosphoserine
- 846 modified: Phosphoserine
Q9JIF3 Solute carrier family 2, facilitated glucose transporter member 8; Glucose transporter type 8; GLUT-8; Glucose transporter type X1 from Mus musculus (Mouse) (see paper)
32% identity, 96% coverage: 5:457/472 of query aligns to 8:470/477 of Q9JIF3
- LL 12:13 (≠ AL 9:10) Dileucine internalization motif; mutation to AA: Abolishes interaction with AP2B1.
Q9JJZ1 Solute carrier family 2, facilitated glucose transporter member 8; Glucose transporter type 8; GLUT-8; Glucose transporter type X1 from Rattus norvegicus (Rat) (see paper)
32% identity, 95% coverage: 11:457/472 of query aligns to 15:471/478 of Q9JJZ1
Sites not aligning to the query:
- 12:13 Dileucine internalization motif; LL→AA: Changes subcellular location mainly to the plasma membrane, thereby increasing transport activity.
9g11A Sugar/h+ symporter stp6 in inward occluded conformation with glucose bound
29% identity, 92% coverage: 29:461/472 of query aligns to 12:466/476 of 9g11A
- binding beta-D-glucopyranose: Q275 (= Q270), I279 (≠ M274), N280 (= N275), W387 (= W381)
- binding cholesterol hemisuccinate: L313 (≠ F309), A314 (= A310), R324 (≠ K320), F329 (≠ P325), Q333 (≠ I329), Q333 (≠ I329), H337 (≠ V333), H337 (≠ V333)
O23492 Inositol transporter 4; Myo-inositol-proton symporter INT4; Protein INOSITOL TRANSPORTER 4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
34% identity, 64% coverage: 23:324/472 of query aligns to 28:343/582 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.
W7MAT5 Myo-inositol transporter FST1 from Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot fungus) (Fusarium verticillioides) (see paper)
30% identity, 91% coverage: 29:458/472 of query aligns to 83:523/574 of W7MAT5
- IRG 276:278 (≠ LRD 221:223) mutation Missing: Abolishes transporter activity. Abolishes synthesis of the polyketide mycotoxin fumonisin B1 (FB1), severely decreases macroconidia production.
- R277 (= R222) mutation R->G,K: Abolishes production of the polyketide mycotoxin fumonisin B1 (FB1), severely decreases macroconidia production.
- VVS 295:297 (vs. gap) mutation Missing: Abolishes transporter activity. Abolishes synthesis of the polyketide mycotoxin fumonisin B1 (FB1), severely decreases macroconidia production, results in hydrogen peroxide sensitivity, and decreases virulence in maize kernels.
- EEI 520:522 (≠ EHI 455:457) mutation Missing: Abolishes transporter activity. Abolishes synthesis of the polyketide mycotoxin fumonisin B1 (FB1), severely decreases macroconidia production.
Sites not aligning to the query:
- 546:548 mutation Missing: Abolishes transporter activity. Strongly decreases synthesis of the polyketide mycotoxin fumonisin B1 (FB1), severely decreases macroconidia production, results in hydrogen peroxide sensitivity, and decreases virulence in maize kernels.
- 547 L→D: Decreases transporter activity. Moderately decreases synthesis of the polyketide mycotoxin fumonisin B1 (FB1).
P11169 Solute carrier family 2, facilitated glucose transporter member 3; Glucose transporter type 3, brain; GLUT-3 from Homo sapiens (Human) (see paper)
28% identity, 93% coverage: 23:459/472 of query aligns to 11:463/496 of P11169
- Q159 (= Q154) binding D-glucose
- QLS 277:279 (≠ QAM 266:268) Important for selectivity against fructose; mutation to HVA: Confers moderate fructose transport activity.
- QQ 280:281 (= QQ 269:270) binding D-glucose
- N286 (= N275) binding D-glucose
- N315 (≠ F307) binding D-glucose
- E378 (≠ A373) binding D-glucose
- W386 (= W381) binding D-glucose
7crzA Crystal structure of human glucose transporter glut3 bound with c3361 (see paper)
28% identity, 93% coverage: 23:459/472 of query aligns to 9:461/469 of 7crzA
- binding (2S,3R,4S,5R,6R)-6-(hydroxymethyl)-4-undec-10-enoxy-oxane-2,3,5-triol: T26 (≠ I40), A66 (≠ S66), S69 (≠ M69), Q157 (= Q154), I164 (= I161), Q278 (= Q269), Q279 (= Q270), N284 (= N275), N313 (≠ F307), F375 (≠ Y372), W384 (= W381), N411 (= N408), F412 (≠ M409), G415 (= G412)
4zw9A Crystal structure of human glut3 bound to d-glucose in the outward- occluded conformation at 1.5 angstrom (see paper)
28% identity, 93% coverage: 23:459/472 of query aligns to 11:463/470 of 4zw9A
- binding beta-D-glucopyranose: Q159 (= Q154), I166 (= I161), Q280 (= Q269), Q281 (= Q270), N286 (= N275), F377 (≠ Y372), W386 (= W381)
- binding alpha-D-glucopyranose: Q159 (= Q154), I162 (≠ V157), I166 (= I161), Q280 (= Q269), Q281 (= Q270), N286 (= N275), W386 (= W381)
7spsA Crystal structure of human glucose transporter glut3 bound with exofacial inhibitor sa47 (see paper)
28% identity, 93% coverage: 23:459/472 of query aligns to 8:460/468 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 (= F36), T25 (≠ I40), N29 (≠ A44), Q156 (= Q154), I163 (= I161), Q278 (= Q270), F286 (≠ M278), A308 (≠ V303), N312 (≠ F307), F374 (≠ Y372), E375 (≠ A373), N406 (= N404), W407 (= W405), N410 (= N408)
Query Sequence
>16922 FitnessBrowser__Keio:16922
MVTINTESALTPRSLRDTRRMNMFVSVAAAVAGLLFGLDIGVIAGALPFITDHFVLTSRL
QEWVVSSMMLGAAIGALFNGWLSFRLGRKYSLMAGAILFVLGSIGSAFATSVEMLIAARV
VLGIAVGIASYTAPLYLSEMASENVRGKMISMYQLMVTLGIVLAFLSDTAFSYSGNWRAM
LGVLALPAVLLIILVVFLPNSPRWLAEKGRHIEAEEVLRMLRDTSEKAREELNEIRESLK
LKQGGWALFKINRNVRRAVFLGMLLQAMQQFTGMNIIMYYAPRIFKMAGFTTTEQQMIAT
LVVGLTFMFATFIAVFTVDKAGRKPALKIGFSVMALGTLVLGYCLMQFDNGTASSGLSWL
SVGMTMMCIAGYAMSAAPVVWILCSEIQPLKCRDFGITCSTTTNWVSNMIIGATFLTLLD
SIGAAGTFWLYTALNIAFVGITFWLIPETKNVTLEHIERKLMAGEKLRNIGV
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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