SitesBLAST
Comparing WP_068115291.1 NCBI__GCF_001653335.1:WP_068115291.1 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)
32% identity, 90% coverage: 30:531/560 of query aligns to 10:522/564 of Q55415
- T69 (= T89) binding hydrogencarbonate; mutation to A: Alters bicarbonate transport.
- D258 (≠ E270) binding Na(+); mutation D->A,E: Alters bicarbonate transport.
- T262 (≠ C274) binding Na(+); mutation to A: Alters bicarbonate transport.
- G300 (≠ A313) binding Na(+)
- A301 (= A314) binding hydrogencarbonate
- T302 (≠ I315) binding Na(+); mutation to A: Alters bicarbonate transport.
- A471 (≠ V480) mutation to N: Alters bicarbonate transport.
- L476 (≠ M485) mutation to S: Alters bicarbonate transport.
- A486 (≠ G495) mutation to E: Alters bicarbonate transport.
- L490 (= L499) mutation to Q: Alters bicarbonate transport.
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
35% identity, 67% coverage: 30:406/560 of query aligns to 9:392/392 of 6ki1B
5da0A Structure of the the slc26 transporter slc26dg in complex with a nanobody (see paper)
29% identity, 87% coverage: 31:518/560 of query aligns to 7:456/467 of 5da0A
Sites not aligning to the query:
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
27% identity, 87% coverage: 30:517/560 of query aligns to 24:539/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (≠ S125), R127 (≠ G126), W130 (≠ R129)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (= L127), L131 (≠ F130), E409 (≠ D400), L413 (≠ A404), G417 (= G408), A421 (= A412)
- binding sulfate ion: A84 (≠ V95), S321 (≠ A314), F322 (≠ I315)
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
27% identity, 86% coverage: 35:513/560 of query aligns to 26:547/597 of 7v74A
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
27% identity, 86% coverage: 35:513/560 of query aligns to 26:555/605 of 7v75A
Q9EPH0 Prestin; Solute carrier family 26 member 5 from Rattus norvegicus (Rat) (see 3 papers)
24% identity, 77% coverage: 35:465/560 of query aligns to 83:549/744 of Q9EPH0
- L104 (≠ A56) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- V149 (= V94) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D154 (vs. gap) mutation to N: Shifts the voltage-sensitivity to more negative values.
- D155 (vs. gap) mutation to N: Shifts the voltage-sensitivity to more negative values.
- E169 (≠ S106) mutation to Q: No effect.
- K177 (vs. gap) mutation to Q: No effect.
- R197 (≠ G126) mutation to Q: Shifts the voltage-sensitivity to more negative values.
- A202 (≠ V131) mutation to C: Is only accessible to the intracellular side application of thiol-reactive reagents. Is not affected by thiol-reactive reagents extracellular side application.
- K233 (≠ A162) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (≠ A164) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
- R236 (≠ T165) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.; mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-235.
- K276 (≠ G203) mutation to C: Is only accessible to the intracellular side application of thiol-reactive reagents. Is not affected by thiol-reactive reagents extracellular side application.
- E277 (≠ R204) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values.
- R281 (= R208) mutation to Q: No effect; when associated with Q-283 and Q-285.
- K283 (vs. gap) mutation to Q: No effect; when associated with Q-218 and Q-285.
- K285 (vs. gap) mutation to Q: No effect; when associated with Q-281 and Q-283.
- P331 (= P241) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D332 (≠ A242) mutation to Q: No effect.
- D342 (= D254) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K359 (≠ M281) mutation to C: Is only accessible to the intracellular side application of thiol-reactive reagents. Is not affected by thiol-reactive reagents extracellular side application.
- Q389 (≠ G307) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S398 (≠ A316) Controls the electromotile activity; mutation to C: Does not affect anion-dependent electromotility-related charge movement. Strongly attenuates inhibition by oxalate of electromotility-related charge movement. Is sensible to intracellular thiol-reactive reagents. Is completely insensitive to both reagents applied to the extracellular face of the membrane. Strongly affects the interaction with oxalate.
- R399 (= R317) Contributes to anion binding; mutation to C: Largely abolishes anion-dependent electromotility-related charge movement.; mutation to E: Fully abolishes anion-dependent electromotility-related charge movement.; mutation to K: Does not affect anion-dependent electromotility-related charge movement.; mutation to Q: Fully abolishes anion-dependent electromotility-related charge movement.; mutation to S: Does not affect anion-dependent electromotility-related charge movement. Abrogates salicylate inhibition of electromotility-related charge movement.
- G408 (≠ A326) mutation to C: Is only accessible to the intracellular side application of thiol-reactive reagents. Is not affected by thiol-reactive reagents extracellular side application.
- K409 (≠ G327) mutation to Q: No effect.
- L431 (= L349) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S465 (≠ T382) mutation to C: Is only accessible to the intracellular side application of thiol-reactive reagents. Is not affected by thiol-reactive reagents extracellular side application.
- D485 (≠ G406) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
Sites not aligning to the query:
- 505:718 Extended region for STAS domain
- 557 K→Q: No effect; when associated with Q-558 and Q-559.
- 558 R→Q: No effect; when associated with Q-557 and Q-559.
- 559 K→Q: No effect; when associated with Q-557 and Q-558.
- 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.
Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
24% identity, 77% coverage: 35:465/560 of query aligns to 83:549/744 of Q9JKQ2
- 158:168 (vs. 99:105, 36% identical) Involved in motor function
- S398 (≠ A316) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
- R399 (= R317) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
D7PC76 Prestin; Solute carrier family 26 member 5 from Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) (see paper)
24% identity, 77% coverage: 35:465/560 of query aligns to 83:549/741 of D7PC76
- GG 274:275 (≠ AG 201:202) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
- S398 (≠ A316) binding salicylate
Q8CIW6 Solute carrier family 26 member 6; Anion exchange transporter; Chloride-formate exchanger; Pendrin-L1; Pendrin-like protein 1; Putative anion transporter-1; Pat-1 from Mus musculus (Mouse) (see paper)
24% identity, 81% coverage: 41:492/560 of query aligns to 101:585/758 of Q8CIW6