SitesBLAST
Comparing 6936893 FitnessBrowser__SB2B:6936893 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)
Q55415 Bicarbonate transporter BicA from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
28% identity, 94% coverage: 29:568/572 of query aligns to 11:543/564 of Q55415
- T69 (= T87) binding ; mutation to A: Alters bicarbonate transport.
- D258 (≠ E296) binding ; mutation D->A,E: Alters bicarbonate transport.
- T262 (≠ C300) binding ; mutation to A: Alters bicarbonate transport.
- G300 (≠ A338) binding
- A301 (= A339) binding
- T302 (≠ I340) binding ; mutation to A: Alters bicarbonate transport.
- A471 (≠ P495) mutation to N: Alters bicarbonate transport.
- L476 (≠ W501) mutation to S: Alters bicarbonate transport.
- A486 (≠ G511) mutation to E: Alters bicarbonate transport.
- L490 (= L515) mutation to Q: Alters bicarbonate transport.
5da0A Structure of the the slc26 transporter slc26dg in complex with a nanobody (see paper)
27% identity, 89% coverage: 23:531/572 of query aligns to 1:453/467 of 5da0A
- binding decyl-beta-d-maltopyranoside: R2 (= R24), W4 (≠ S26), R57 (≠ S79), V114 (= V136), M115 (≠ T137), F118 (= F140), V119 (≠ T141), L223 (≠ M291), V224 (≠ L292), L227 (≠ I295), E228 (= E296), L231 (= L299), D241 (≠ G309), T242 (≠ N310), T243 (≠ R311), I272 (= I340), V322 (= V390), S325 (≠ H393), T326 (≠ M394), V359 (≠ I431)
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
28% identity, 94% coverage: 24:559/572 of query aligns to 16:570/597 of 7v74A
- binding cholesterol: L206 (≠ V198), K209 (≠ P201), V379 (= V389), K382 (vs. gap), A391 (= A397), P392 (≠ K398), W395 (≠ L401), F402 (≠ H408)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: I152 (= I146), V176 (≠ F168), M386 (≠ W392), F388 (≠ M394), F388 (≠ M394), K389 (≠ S395), V413 (≠ L419), F414 (≠ M420)
- binding sulfate ion: F80 (≠ T87), V286 (≠ E296), V290 (≠ C300), S329 (≠ A339), F330 (≠ I340), L384 (≠ V390)
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
28% identity, 94% coverage: 24:559/572 of query aligns to 16:578/605 of 7v75A
- binding cholesterol: F202 (≠ L194), L206 (≠ V198), K209 (≠ P201), V379 (= V389), K382 (vs. gap), A391 (= A397), P392 (≠ K398), W395 (≠ L401), F402 (≠ H408)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L129 (≠ M123), L131 (= L125), I152 (= I146), M386 (≠ W392), F388 (≠ M394), F388 (≠ M394), K389 (≠ S395), F414 (≠ M420)
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
25% identity, 98% coverage: 7:565/572 of query aligns to 7:571/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L125 (= L122), L126 (≠ M123), R127 (= R124), L128 (= L125), W130 (≠ R127)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (= L125), W130 (≠ R127), L131 (= L128), I135 (= I132), P266 (= P284), L270 (≠ A288), L277 (≠ I295), E409 (≠ V428), V412 (vs. gap), L413 (vs. gap), G417 (= G434), A421 (= A438), F422 (≠ S439), H425 (vs. gap)
- binding sulfate ion: Y47 (≠ L51), V83 (≠ T87), A84 (= A88), S321 (≠ A339), F322 (≠ I340), S323 (≠ A341)
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
28% identity, 71% coverage: 29:432/572 of query aligns to 10:392/392 of 6ki1B
7lguA Structure of human prestin in the presence of nacl (see paper)
21% identity, 97% coverage: 7:560/572 of query aligns to 55:625/680 of 7lguA
Q9EPH0 Prestin; Solute carrier family 26 member 5 from Rattus norvegicus (Rat) (see paper)
22% identity, 85% coverage: 7:493/572 of query aligns to 67:561/744 of Q9EPH0
- D154 (≠ G104) mutation to N: Shifts the voltage-sensitivity to more negative values.
- D155 (≠ G105) mutation to N: Shifts the voltage-sensitivity to more negative values.
- E169 (vs. gap) mutation to Q: No effect.
- K177 (vs. gap) mutation to Q: No effect.
- R197 (= R124) mutation to Q: Shifts the voltage-sensitivity to more negative values.
- K233 (≠ P160) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (≠ E162) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
- R236 (≠ A163) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-235.
- E277 (≠ K202) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values.
- R281 (≠ K206) mutation to Q: No effect; when associated with Q-283 and Q-285.
- K283 (≠ P208) mutation to Q: No effect; when associated with Q-218 and Q-285.
- K285 (≠ H210) mutation to Q: No effect; when associated with Q-281 and Q-283.
- D332 (≠ N275) mutation to Q: No effect.
- D342 (≠ S285) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K409 (= K352) mutation to Q: No effect.
- K557 (≠ H489) mutation to Q: No effect; when associated with Q-558 and Q-559.
- R558 (= R490) mutation to Q: No effect; when associated with Q-557 and Q-559.
- K559 (≠ Q491) mutation to Q: No effect; when associated with Q-557 and Q-558.
Sites not aligning to the query:
- 571 R→Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-572 and Q-577.
- 572 R→Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-571 and Q-577.
- 577 K→Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-571 and Q-572.
7xulA Human slc26a3 in complex with tenidap
24% identity, 91% coverage: 7:526/572 of query aligns to 46:554/690 of 7xulA