SitesBLAST
Comparing SMc00476 FitnessBrowser__Smeli:SMc00476 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)
32% identity, 92% coverage: 21:527/551 of query aligns to 11:522/564 of Q55415
- T69 (≠ A79) binding ; mutation to A: Alters bicarbonate transport.
- D258 (≠ E265) binding ; mutation D->A,E: Alters bicarbonate transport.
- T262 (≠ S269) binding ; mutation to A: Alters bicarbonate transport.
- G300 (= G307) binding
- A301 (≠ T308) binding
- T302 (≠ I309) binding ; mutation to A: Alters bicarbonate transport.
- A471 (≠ N476) mutation to N: Alters bicarbonate transport.
- L476 (≠ C481) mutation to S: Alters bicarbonate transport.
- A486 (= A491) mutation to E: Alters bicarbonate transport.
- L490 (≠ I495) mutation to Q: Alters bicarbonate transport.
5da0A Structure of the the slc26 transporter slc26dg in complex with a nanobody (see paper)
31% identity, 88% coverage: 23:506/551 of query aligns to 9:448/467 of 5da0A
Sites not aligning to the query:
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
33% identity, 68% coverage: 21:395/551 of query aligns to 10:387/392 of 6ki1B
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
26% identity, 91% coverage: 22:522/551 of query aligns to 23:562/597 of 7v74A
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
26% identity, 91% coverage: 22:522/551 of query aligns to 23:570/605 of 7v75A
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
25% identity, 91% coverage: 19:519/551 of query aligns to 23:545/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (= L115), R127 (= R116), W130 (≠ R119)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (= L117), L131 (≠ Y120), E409 (≠ T396), L413 (≠ V400), G417 (≠ A404), A421 (≠ V408)
- binding sulfate ion: A84 (≠ G80), S321 (≠ T308), F322 (≠ I309)
P58735 Sulfate anion transporter 1; SAT-1; Solute carrier family 26 member 1 from Mus musculus (Mouse) (see paper)
24% identity, 79% coverage: 22:459/551 of query aligns to 69:555/704 of P58735
- T190 (vs. gap) mutation to M: Decreased sulfate-hydrogencarbonate exchange activity. Loss of localization to plasma membrane.
- S363 (≠ V271) mutation to L: Decreased sulfate-hydrogencarbonate exchange activity. Increased accumulation of protein in ER.
Sites not aligning to the query:
- 56 A→T: Decreased sulfate-hydrogencarbonate exchange activity. Does not affect localization to plasma membrane.
A0FKN5 Prestin; Solute carrier family 26 member 5 from Gallus gallus (Chicken) (see paper)
24% identity, 72% coverage: 22:416/551 of query aligns to 81:511/742 of A0FKN5
- S404 (≠ A310) 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 (= R311) mutation to C: Fully abolishes anion transport.
Q9URY8 Probable sulfate permease C869.05c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
24% identity, 83% coverage: 16:475/551 of query aligns to 115:618/840 of Q9URY8
Sites not aligning to the query:
- 823 modified: Phosphoserine
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)
25% identity, 81% coverage: 32:478/551 of query aligns to 102:581/758 of Q8CIW6
- F552 (= F457) mutation to A: Does not inhibit formate transport in PMA-induced cells.
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, 78% coverage: 32:463/551 of query aligns to 100:549/759 of Q9BXS9
- N167 (≠ D96) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- N172 (≠ A101) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- V206 (≠ Y120) to M: in dbSNP:rs13324142
- ATV 547:549 (= ATV 461:463) mutation to NVN: Does not inhibit cell membrane localization. Inhibits interaction with CA2 and bicarbonate transport.
Sites not aligning to the query:
- 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.
7lguA Structure of human prestin in the presence of nacl (see paper)
21% identity, 91% coverage: 25:525/551 of query aligns to 71:645/680 of 7lguA
8sieC Pendrin in complex with bicarbonate
23% identity, 91% coverage: 22:524/551 of query aligns to 44:586/613 of 8sieC
- binding Lauryl Maltose Neopentyl Glycol: G198 (vs. gap), S296 (≠ P253), T300 (≠ S257), F303 (≠ L260)
- binding bicarbonate ion: Y65 (≠ I43), F101 (= F63), L356 (≠ I309), S357 (≠ A310), V403 (= V359), N406 (= N362)
- binding cholesterol: L226 (= L185), V255 (≠ A206), I262 (≠ F213), Y272 (≠ T223), F411 (= F369), V414 (vs. gap), V414 (vs. gap), C415 (vs. gap), C415 (vs. gap), I436 (≠ L388), M452 (≠ A404), F453 (≠ L405)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: W421 (≠ L373), V429 (= V381), V432 (≠ L384), F433 (≠ A385), I436 (≠ L388)
8shcC Pendrin in complex with niflumic acid
23% identity, 91% coverage: 22:524/551 of query aligns to 44:586/613 of 8shcC
- binding cholesterol: I199 (≠ P158), A223 (≠ T182), V255 (≠ A206), Y272 (≠ T223), M412 (= M370), C415 (vs. gap), M452 (≠ A404), F453 (≠ L405)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: Q156 (≠ R116), W421 (≠ L373), V432 (≠ L384), F433 (≠ A385), F455 (≠ A407)
- binding 2-{[3-(trifluoromethyl)phenyl]amino}nicotinic acid: Y65 (≠ I43), F101 (= F63), T173 (= T133), E252 (≠ M203), I312 (≠ S269), L356 (≠ I309), S357 (≠ A310), V402 (≠ I358), N406 (= N362)
8sgwC Pendrin in complex with chloride
23% identity, 91% coverage: 22:524/551 of query aligns to 44:586/613 of 8sgwC
- binding Lauryl Maltose Neopentyl Glycol: G198 (vs. gap), S296 (≠ P253), T300 (≠ S257), F303 (≠ L260)
- binding cholesterol: I228 (≠ V187), V255 (≠ A206), I262 (≠ F213), Y272 (≠ T223), K408 (= K366), F411 (= F369), M412 (= M370), M412 (= M370), V414 (vs. gap), C415 (vs. gap), V417 (vs. gap), I439 (≠ V391)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: F159 (≠ R119), Y163 (≠ F123), F284 (≠ L235), P286 (≠ L237), I289 (≠ L240), F343 (≠ C296), F346 (≠ L299), W421 (≠ L373), F433 (≠ A385), I436 (≠ L388), F455 (≠ A407), F464 (≠ R416), P465 (vs. gap)
Q62273 Sulfate transporter; Diastrophic dysplasia protein homolog; ST-OB; Solute carrier family 26 member 2 from Mus musculus (Mouse) (see paper)
24% identity, 71% coverage: 25:416/551 of query aligns to 111:548/739 of Q62273
- F368 (≠ L235) mutation to A: Reduced sulfate-chloride exchange activity.
- E417 (= E286) mutation E->A,K: Loss of sulfate-chloride exchange activity.
P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
24% identity, 68% coverage: 25:400/551 of query aligns to 83:489/744 of P58743
- F101 (≠ I43) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ A310) binding
D7PC76 Prestin; Solute carrier family 26 member 5 from Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) (see paper)
23% identity, 83% coverage: 25:479/551 of query aligns to 83:568/741 of D7PC76
- GG 274:275 (≠ AL 192:193) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
- S398 (≠ A310) binding
Q9EPH0 Prestin; Solute carrier family 26 member 5 from Rattus norvegicus (Rat) (see 3 papers)
24% identity, 68% coverage: 25:400/551 of query aligns to 83:489/744 of Q9EPH0
- L104 (≠ A46) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- V149 (≠ A91) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D154 (= D96) mutation to N: Shifts the voltage-sensitivity to more negative values.
- D155 (≠ G97) 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 (= R116) mutation to Q: Shifts the voltage-sensitivity to more negative values.
- A202 (≠ I121) 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 (vs. gap) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (≠ L153) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
- R236 (≠ A154) 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 (≠ R194) 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 (≠ R195) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values.
- R281 (≠ H199) 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 (≠ P242) mutation to Q: No effect.
- D342 (= D254) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K359 (≠ V271) 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 (≠ G301) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S398 (≠ A310) 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 (= R311) 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 (≠ A320) 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 (≠ T321) mutation to Q: No effect.
- L431 (= L343) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S465 (= S376) 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 (≠ T396) 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, 68% coverage: 25:400/551 of query aligns to 83:489/744 of Q9JKQ2
- 158:168 (vs. 100:100, 0% identical) Involved in motor function
- S398 (≠ A310) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
- R399 (= R311) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
Query Sequence
>SMc00476 FitnessBrowser__Smeli:SMc00476
MPDSLVPKTVSILAEGYGAARLKADAFAGLTVAIVALPLSMAIAIASGVTPDRGLYTAIV
GGFLVSLLGGSRVQIGGPAGAFIVLVAATVARHGVDGLLLATLMSGFMLIAAGYLRLGRY
IKFIPYPVTVGFTAGIAVIIFASQLRDLFGLTLAGAEPGPIVDKVAALAQAAGTVSWAAV
LTAALTVGIILALRRVRPHWPGMLIAVAAASTFVALLQLPTETIGSRFGGIPRGLPLPAL
PPLSLEKAAAVFPDALSFALLGAIESLLSAVVADGMTGRRHRSSVELVAQGAANICSALF
GGICVTGTIARTATNVRAGATSPVSGILHSAFLLLFMLLAAPLASYIPLASLAGVLAIVA
WNMIEKPAFMALLRSSYGDAVVLLATFLIVVFRELTEGIVVGFALGAVLFIDRMARSISV
QEARPLSAQRQENGDERPVIADDPDTVIYRLSGIFFFGSAATVGTVLDRIADQRRNFILD
CSDVPFMDSTAANVIEGTLRKAERTGVRFIITGARSQVRRALYQHHVRPPRVMMRASVAA
ALDTIRTERVP
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