SitesBLAST
Comparing BWI76_RS24055 FitnessBrowser__Koxy:BWI76_RS24055 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)
A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
38% identity, 91% coverage: 32:451/464 of query aligns to 22:437/446 of A0A0H2VG78
- D22 (= D32) mutation to N: Affects symport activity. May function as an uniporter.
- R102 (= R112) mutation to A: Loss of transport activity.
- I105 (≠ L115) mutation to S: Affects symport activity. May function as an uniporter.
- E122 (= E132) mutation to A: Loss of transport activity.
- Q137 (= Q147) mutation to A: Loss of transport activity.
- Q250 (= Q262) mutation to A: Loss of transport activity.
- Q251 (= Q263) mutation to A: Loss of transport activity.
- N256 (= N268) mutation to A: Loss of transport activity.
- W357 (= W371) mutation to A: Loss of transport activity.
Q8VZR6 Inositol transporter 1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
37% identity, 92% coverage: 22:449/464 of query aligns to 38:477/509 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.
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)
33% identity, 93% coverage: 19:449/464 of query aligns to 29:487/514 of Q9LT15
- F39 (= F29) mutation to A: Reduces affinity for glucose 8-fold.
- L43 (≠ I33) mutation to A: Reduces affinity for glucose 150-fold and turns STP10 into a low affinity transporter.
- C77 (≠ V57) modified: Disulfide link with 449; mutation to A: Increases sensitivity to alkaline pH and can only function fully at acidic pH (pH < 5).
- E162 (= E132) mutation to Q: Abolishes glucose transport activity; when associated with N-344.
- Q177 (= Q147) binding beta-D-glucose; mutation to A: Reduces affinity for glucose 37-fold.
- I184 (= I154) mutation to A: Reduces affinity for glucose 3-fold.
- Q295 (= Q262) binding beta-D-glucose
- Q296 (= Q263) binding beta-D-glucose
- N301 (= N268) binding beta-D-glucose
- N332 (= N300) binding beta-D-glucose
- D344 (= D312) mutation to N: Abolishes glucose transport activity; when associated with Q-162.
- W410 (= W371) binding beta-D-glucose
- C449 (≠ N410) 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)
33% identity, 93% coverage: 19:449/464 of query aligns to 9:467/487 of 7aaqA
P0AGF4 D-xylose-proton symporter; D-xylose transporter from Escherichia coli (strain K12) (see paper)
32% identity, 95% coverage: 9:448/464 of query aligns to 4:475/491 of P0AGF4
- F24 (= F29) mutation to A: Decreases xylose transport.
- G83 (= G80) mutation to A: Abolishes xylose transport.
- R133 (= R112) mutation R->C,H,L: Abolishes xylose transport.
- E153 (= E132) mutation to A: Abolishes xylose transport.
- R160 (= R139) mutation to A: Abolishes xylose transport.
- Q168 (= Q147) binding beta-D-xylose; mutation to A: Abolishes xylose transport.
- Q288 (= Q262) mutation to A: Abolishes xylose transport.
- QQ 288:289 (= QQ 262:263) binding beta-D-xylose
- Q289 (= Q263) mutation to A: Strongly decreases xylose transport.
- N294 (= N268) binding beta-D-xylose; mutation to A: Abolishes xylose transport.
- Y298 (= Y272) mutation to A: Abolishes xylose transport.
- N325 (= N300) mutation to A: No effect on xylose transport.
- G340 (= G315) mutation to A: Abolishes xylose transport.
- R341 (= R316) mutation R->A,W: Abolishes xylose transport.
- W392 (= W371) binding beta-D-xylose; mutation to A: Abolishes xylose transport.
- E397 (= E376) mutation to A: Abolishes xylose transport.
- R404 (= R383) mutation to A: Strongly decreases xylose transport.
- Q415 (≠ N394) binding beta-D-xylose
- W416 (= W395) 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)
32% identity, 94% coverage: 11:448/464 of query aligns to 2:471/475 of 4gc0A
4gbzA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-glucose (see paper)
32% identity, 94% coverage: 11:448/464 of query aligns to 2:471/475 of 4gbzA
4gbyA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-xylose (see paper)
32% identity, 94% coverage: 11:448/464 of query aligns to 2:471/475 of 4gbyA
7aarA Sugar/h+ symporter stp10 in inward open conformation (see paper)
33% identity, 93% coverage: 19:449/464 of query aligns to 14:472/485 of 7aarA
- binding Octyl Glucose Neopentyl Glycol : L28 (≠ I33), I90 (≠ L75), H94 (≠ L79), V98 (≠ K83), F101 (≠ M86), N138 (≠ S123), P142 (= P127), N158 (≠ I143), F161 (≠ Y146), Q162 (= Q147), I165 (= I150), D210 (= D193), G391 (= G367), P392 (= P368), W395 (= W371), M419 (≠ W395)
- binding beta-D-glucopyranose: Q280 (= Q262), N286 (= N268), M289 (= M271), G391 (= G367), W395 (= W371)
Q9C757 Probable inositol transporter 2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
40% identity, 71% coverage: 20:347/464 of query aligns to 33:371/580 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.
9g11A Sugar/h+ symporter stp6 in inward occluded conformation with glucose bound
32% identity, 95% coverage: 13:453/464 of query aligns to 2:468/476 of 9g11A