SitesBLAST
Comparing RR42_RS16025 FitnessBrowser__Cup4G11:RR42_RS16025 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
30% identity, 93% coverage: 29:582/596 of query aligns to 15:542/564 of Q55415
- T69 (≠ A83) binding ; mutation to A: Alters bicarbonate transport.
- D258 (≠ E299) binding ; mutation D->A,E: Alters bicarbonate transport.
- T262 (≠ C303) binding ; mutation to A: Alters bicarbonate transport.
- G300 (= G341) binding
- A301 (≠ T342) binding
- T302 (≠ I343) binding ; mutation to A: Alters bicarbonate transport.
- A471 (= A510) mutation to N: Alters bicarbonate transport.
- L476 (≠ V516) mutation to S: Alters bicarbonate transport.
- A486 (≠ G526) mutation to E: Alters bicarbonate transport.
- L490 (= L530) mutation to Q: Alters bicarbonate transport.
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
34% identity, 68% coverage: 29:435/596 of query aligns to 14:391/392 of 6ki1B
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
27% identity, 98% coverage: 7:589/596 of query aligns to 4:597/597 of 7v74A
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
27% identity, 98% coverage: 7:589/596 of query aligns to 4:605/605 of 7v75A
5da0A Structure of the the slc26 transporter slc26dg in complex with a nanobody (see paper)
30% identity, 51% coverage: 255:559/596 of query aligns to 183:466/467 of 5da0A
Sites not aligning to the query:
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
25% identity, 92% coverage: 18:567/596 of query aligns to 17:558/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (≠ F119), R127 (= R120), W130 (≠ T123)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (= L121), L131 (= L124), E409 (≠ T432), L413 (≠ Q436), G417 (≠ V440), A421 (≠ L444)
- binding sulfate ion: A84 (≠ G84), S321 (≠ T342), F322 (≠ I343)
Q9URY8 Probable sulfate permease C869.05c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
28% identity, 64% coverage: 14:392/596 of query aligns to 109:481/840 of Q9URY8
Sites not aligning to the query:
- 823 modified: Phosphoserine
A0FKN5 Prestin; Solute carrier family 26 member 5 from Gallus gallus (Chicken) (see paper)
25% identity, 71% coverage: 29:449/596 of query aligns to 84:508/742 of A0FKN5
- S404 (≠ A344) Controls the anion transport; mutation to A: Alters anion selectivity.; mutation to C: Abolishes sulfate transport. Does not affect oxalate transport. Is accesible both from extracellular and intracellular side by methane-thiosulphonate (MTS) reagents. Inhibits divalent transport upon extracellular application of (2-sulphonatoethyl)methane-thiosulphonate (MTSES) but not [2-(trimethylammonium)ethyl]methane-thiosulphonate (MTSET). Abolishes anion transport upon intracellular MTSET application.
- R405 (= R345) mutation to C: Fully abolishes anion transport.
Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
23% identity, 95% coverage: 29:595/596 of query aligns to 83:609/744 of Q9JKQ2
- 158:168 (vs. 104:104, 9% identical) Involved in motor function
- S398 (≠ A344) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
- R399 (= R345) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
23% identity, 95% coverage: 29:593/596 of query aligns to 83:607/744 of P58743
- F101 (= F47) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ A344) binding
7lguA Structure of human prestin in the presence of nacl (see paper)
25% identity, 71% coverage: 29:452/596 of query aligns to 71:493/680 of 7lguA
8sieC Pendrin in complex with bicarbonate
22% identity, 93% coverage: 14:565/596 of query aligns to 31:592/613 of 8sieC
- binding Lauryl Maltose Neopentyl Glycol: G198 (= G162), S296 (≠ Q283), T300 (≠ A287), F303 (≠ L290)
- binding bicarbonate ion: Y65 (≠ F47), F101 (vs. gap), L356 (≠ I343), S357 (≠ A344), V403 (≠ L390), N406 (≠ V393)
- binding cholesterol: L226 (≠ V191), V255 (≠ A240), I262 (≠ A247), Y272 (≠ T257), F411 (≠ G398), V414 (≠ M402), V414 (≠ M402), C415 (≠ F403), C415 (≠ F403), I436 (≠ V424), M452 (≠ V440), F453 (≠ L441)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: W421 (≠ K409), V429 (≠ I417), V432 (≠ L420), F433 (≠ G421), I436 (≠ V424)
8shcC Pendrin in complex with niflumic acid
22% identity, 93% coverage: 14:565/596 of query aligns to 31:592/613 of 8shcC
- binding cholesterol: I199 (≠ F164), A223 (≠ S188), V255 (≠ A240), Y272 (≠ T257), M412 (≠ W400), C415 (≠ F403), M452 (≠ V440), F453 (≠ L441)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: Q156 (≠ R120), W421 (≠ K409), V432 (≠ L420), F433 (≠ G421), F455 (≠ C443)
- binding 2-{[3-(trifluoromethyl)phenyl]amino}nicotinic acid: Y65 (≠ F47), F101 (vs. gap), T173 (= T137), E252 (≠ T237), I312 (≠ E299), L356 (≠ I343), S357 (≠ A344), V402 (≠ I389), N406 (≠ V393)
8sgwC Pendrin in complex with chloride
22% identity, 93% coverage: 14:565/596 of query aligns to 31:592/613 of 8sgwC
- binding Lauryl Maltose Neopentyl Glycol: G198 (= G162), S296 (≠ Q283), T300 (≠ A287), F303 (≠ L290)
- binding cholesterol: I228 (≠ V193), V255 (≠ A240), I262 (≠ A247), Y272 (≠ T257), K408 (≠ W395), F411 (≠ G398), M412 (≠ W400), M412 (≠ W400), V414 (≠ M402), C415 (≠ F403), V417 (≠ L405), I439 (≠ V427)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: F159 (≠ T123), Y163 (≠ F127), F284 (≠ L269), P286 (= P271), I289 (≠ L274), F343 (≠ V330), F346 (= F333), W421 (≠ K409), F433 (≠ G421), I436 (≠ V424), F455 (≠ C443), F464 (vs. gap), P465 (vs. gap)
Q9EPH0 Prestin; Solute carrier family 26 member 5 from Rattus norvegicus (Rat) (see 3 papers)
23% identity, 91% coverage: 29:570/596 of query aligns to 83:586/744 of Q9EPH0
- L104 (≠ A50) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- V149 (≠ A95) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D154 (≠ A100) mutation to N: Shifts the voltage-sensitivity to more negative values.
- D155 (≠ N101) 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 (= R120) mutation to Q: Shifts the voltage-sensitivity to more negative values.
- A202 (≠ I125) 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 (≠ Q156) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (≠ G158) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
- R236 (≠ K159) 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 (= K205) 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 (≠ R206) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values.
- R281 (= R226) mutation to Q: No effect; when associated with Q-283 and Q-285.
- K283 (≠ G228) mutation to Q: No effect; when associated with Q-218 and Q-285.
- K285 (≠ A230) mutation to Q: No effect; when associated with Q-281 and Q-283.
- P331 (= P275) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D332 (≠ Q276) mutation to Q: No effect.
- D342 (≠ P288) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K359 (≠ R305) 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 (≠ G335) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S398 (≠ A344) 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 (= R345) 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 (= G354) 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 (≠ R355) mutation to Q: No effect.
- L431 (= L377) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S465 (= S412) 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 (≠ T432) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- K557 (≠ A538) mutation to Q: No effect; when associated with Q-558 and Q-559.
- R558 (= R539) mutation to Q: No effect; when associated with Q-557 and Q-559.
- K559 (≠ R540) mutation to Q: No effect; when associated with Q-557 and Q-558.
- R571 (≠ M557) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-572 and Q-577.
- R572 (= R558) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-571 and Q-577.
- K577 (≠ G561) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-571 and Q-572.
Sites not aligning to the query:
- 505:718 Extended region for STAS domain
Q9BXS9 Solute carrier family 26 member 6; Anion exchange transporter; Pendrin-like protein 1; Pendrin-L1 from Homo sapiens (Human) (see 3 papers)
25% identity, 73% coverage: 36:469/596 of query aligns to 100:523/759 of Q9BXS9
- N167 (vs. gap) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- N172 (vs. gap) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- V206 (≠ L124) to M: in dbSNP:rs13324142
Sites not aligning to the query:
- 547:549 DVD→NVN: Does not inhibit cell membrane localization. Inhibits interaction with CA2 and bicarbonate transport.
- 553 S→A: Does not inhibit interaction with CA2. Inhibits interaction with CA2 and bicarbonate transport in PMA-induced cells.
- 582 S→A: Does not inhibit interaction with CA2. Does not inhibit interaction with CA2 and bicarbonate transport in PMA-induced cells.
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, 70% coverage: 36:450/596 of query aligns to 102:509/758 of Q8CIW6
Sites not aligning to the query:
- 552 T→A: Does not inhibit formate transport in PMA-induced cells.
D7PC76 Prestin; Solute carrier family 26 member 5 from Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) (see paper)
25% identity, 72% coverage: 29:456/596 of query aligns to 83:509/741 of D7PC76
- GG 274:275 (≠ AG 203:204) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
- S398 (≠ A344) binding
7xulA Human slc26a3 in complex with tenidap
25% identity, 75% coverage: 5:449/596 of query aligns to 44:471/690 of 7xulA
- binding 5-chloranyl-2-oxidanyl-3-thiophen-2-ylcarbonyl-indole-1-carboxamide: V72 (= V39), L75 (≠ P42), Q76 (≠ L43), E262 (≠ T237), S367 (≠ A344), L412 (≠ I389), N416 (= N396)
- binding cholesterol hemisuccinate: I157 (≠ G111), F162 (≠ M116), P209 (≠ F164), K214 (≠ R169), Y217 (≠ G172), V302 (≠ L277), Q306 (= Q283), V309 (= V286), V450 (= V428)
7xujA Human slc26a3 in complex with uk5099
25% identity, 75% coverage: 5:449/596 of query aligns to 51:480/703 of 7xujA
- binding (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid: V79 (= V39), Q83 (≠ L43), E271 (≠ T237), S376 (≠ A344), R377 (= R345), V380 (≠ T348), L421 (≠ I389), A422 (≠ L390), N425 (= N396)
- binding cholesterol hemisuccinate: F171 (≠ M116), V311 (≠ L277), Q315 (= Q283)
Query Sequence
>RR42_RS16025 FitnessBrowser__Cup4G11:RR42_RS16025
MRQPFPLAAFHPRLLDSLRDYNRALFFKDLAAGLTVGVVALPLAMAFAIASGMPPQAGLF
TAIIAGFLIAALGGSPVQIGGPAGAFIVIVYGIVARYGVANLLIATILAGGLLFAMGLFR
LGTLIRFIPVAIVIGFTNGIAVLIMVSQIADFLGLQTGKLPGNFLSQMRVLGRALPTVSW
PTVALAVSSLVVVAGWSRLALLAGKRWRPVSTVAANPANPPNAHGRLGRALAMVPGTVIA
LVLATAANGLLHLPVETIGTRFGGIPQGLPPFALPQLSWQLVQQLVAPTLTIALLGAIES
LLCARVADSLIDDRHDPNQELMAQGIANIVTPFFGGLPATGTIARTVTNVRSGGRTPVAG
MIHAATLLLIVLVAAPLASAIPLATLAAILLYVAWNMGEWHMFGLTHLKRYSNNYRIILL
GTFVLTVVFDLTVAVQVGLVLACLFFIYRMAALTQIEAIAPAALPPAADGRPLPAGEVAA
YHMTGALFFGAVNKVEALIDPRDRTQPVPAVLILDVGKLVALDTTGLDTLDALRKTLARR
GGTLVICAAPAQVMSLMRRAGFLEQMGTANYCDTLAAACARAGVLLAERAERPAAG
Or try a new SitesBLAST search
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