SitesBLAST
Comparing BWI76_RS03110 FitnessBrowser__Koxy:BWI76_RS03110 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)
37% identity, 89% coverage: 40:481/499 of query aligns to 20:446/446 of A0A0H2VG78
- D22 (= D42) mutation to N: Affects symport activity. May function as an uniporter.
- R102 (= R122) mutation to A: Loss of transport activity.
- I105 (≠ L125) mutation to S: Affects symport activity. May function as an uniporter.
- E122 (= E142) mutation to A: Loss of transport activity.
- Q137 (≠ E157) mutation to A: Loss of transport activity.
- Q250 (= Q278) mutation to A: Loss of transport activity.
- Q251 (= Q279) mutation to A: Loss of transport activity.
- N256 (= N284) mutation to A: Loss of transport activity.
- W357 (= W392) mutation to A: Loss of transport activity.
Q8VZR6 Inositol transporter 1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
38% identity, 89% coverage: 32:475/499 of query aligns to 38:482/509 of Q8VZR6
- ER 481:482 (≠ DK 474:475) mutation to AA: No effect on targeting.
Sites not aligning to the query:
- 479:509 mutation Missing: Leads to endoplasmic reticulum relocalization.
- 500:509 mutation Missing: Leads to endoplasmic reticulum relocalization.
- 502:504 mutation LLE->AAA,SSS: Leads to plasma membrane relocalization.
P0AGF4 D-xylose-proton symporter; D-xylose transporter from Escherichia coli (strain K12) (see paper)
31% identity, 92% coverage: 21:481/499 of query aligns to 6:487/491 of P0AGF4
- F24 (= F39) mutation to A: Decreases xylose transport.
- G83 (= G90) mutation to A: Abolishes xylose transport.
- R133 (= R122) mutation R->C,H,L: Abolishes xylose transport.
- E153 (= E142) mutation to A: Abolishes xylose transport.
- R160 (= R149) mutation to A: Abolishes xylose transport.
- Q168 (≠ E157) binding beta-D-xylose; mutation to A: Abolishes xylose transport.
- Q288 (= Q278) mutation to A: Abolishes xylose transport.
- QQ 288:289 (= QQ 278:279) binding beta-D-xylose
- Q289 (= Q279) mutation to A: Strongly decreases xylose transport.
- N294 (= N284) binding beta-D-xylose; mutation to A: Abolishes xylose transport.
- Y298 (= Y288) mutation to A: Abolishes xylose transport.
- N325 (≠ S315) mutation to A: No effect on xylose transport.
- G340 (= G330) mutation to A: Abolishes xylose transport.
- R341 (= R331) mutation R->A,W: Abolishes xylose transport.
- W392 (= W392) binding beta-D-xylose; mutation to A: Abolishes xylose transport.
- E397 (= E397) mutation to A: Abolishes xylose transport.
- R404 (= R404) mutation to A: Strongly decreases xylose transport.
- Q415 (≠ M415) binding beta-D-xylose
- W416 (= W416) 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, 90% coverage: 21:469/499 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, 90% coverage: 21:469/499 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, 90% coverage: 21:469/499 of query aligns to 2:471/475 of 4gbyA
Q9C757 Probable inositol transporter 2 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
36% identity, 68% coverage: 17:354/499 of query aligns to 20:363/580 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.
O23492 Inositol transporter 4; Myo-inositol-proton symporter INT4; Protein INOSITOL TRANSPORTER 4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
37% identity, 66% coverage: 22:352/499 of query aligns to 24:363/582 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.
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)
29% identity, 90% coverage: 22:468/499 of query aligns to 22:485/514 of Q9LT15
- F39 (= F39) mutation to A: Reduces affinity for glucose 8-fold.
- L43 (≠ T43) mutation to A: Reduces affinity for glucose 150-fold and turns STP10 into a low affinity transporter.
- C77 (≠ T63) modified: Disulfide link with 449; mutation to A: Increases sensitivity to alkaline pH and can only function fully at acidic pH (pH < 5).
- E162 (= E142) mutation to Q: Abolishes glucose transport activity; when associated with N-344.
- Q177 (≠ E157) binding beta-D-glucose; mutation to A: Reduces affinity for glucose 37-fold.
- I184 (≠ Q164) mutation to A: Reduces affinity for glucose 3-fold.
- Q295 (= Q278) binding beta-D-glucose
- Q296 (= Q279) binding beta-D-glucose
- N301 (= N284) binding beta-D-glucose
- N332 (≠ S315) binding beta-D-glucose
- D344 (≠ G327) mutation to N: Abolishes glucose transport activity; when associated with Q-162.
- W410 (= W392) binding beta-D-glucose
- C449 (≠ A431) 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)
29% identity, 90% coverage: 22:468/499 of query aligns to 2:465/487 of 7aaqA
7aarA Sugar/h+ symporter stp10 in inward open conformation (see paper)
29% identity, 90% coverage: 18:468/499 of query aligns to 3:470/485 of 7aarA