SitesBLAST
Comparing 352708 FitnessBrowser__Btheta:352708 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)
29% identity, 96% coverage: 20:554/559 of query aligns to 10:542/564 of Q55415
- T69 (= T79) binding ; mutation to A: Alters bicarbonate transport.
- D258 (≠ E270) binding ; mutation D->A,E: Alters bicarbonate transport.
- T262 (≠ S274) binding ; mutation to A: Alters bicarbonate transport.
- G300 (= G312) binding
- A301 (= A313) binding
- T302 (≠ I314) binding ; mutation to A: Alters bicarbonate transport.
- A471 (≠ N482) mutation to N: Alters bicarbonate transport.
- L476 (≠ M488) mutation to S: Alters bicarbonate transport.
- A486 (≠ G498) mutation to E: Alters bicarbonate transport.
- L490 (= L502) mutation to Q: Alters bicarbonate transport.
5da0A Structure of the the slc26 transporter slc26dg in complex with a nanobody (see paper)
29% identity, 91% coverage: 25:531/559 of query aligns to 11:466/467 of 5da0A
Sites not aligning to the query:
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
28% identity, 96% coverage: 3:536/559 of query aligns to 4:569/597 of 7v74A
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
33% identity, 69% coverage: 20:404/559 of query aligns to 9:391/392 of 6ki1B
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
28% identity, 96% coverage: 3:536/559 of query aligns to 4:577/605 of 7v75A
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
25% identity, 97% coverage: 1:541/559 of query aligns to 1:560/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (≠ F115), R127 (≠ K116), W130 (≠ A119)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (= L117), L131 (≠ V120), E409 (≠ T401), L413 (≠ E405), G417 (≠ I409), A421 (≠ V413)
- binding sulfate ion: A84 (≠ G80), S321 (≠ A313), F322 (≠ I314)
Q62273 Sulfate transporter; Diastrophic dysplasia protein homolog; ST-OB; Solute carrier family 26 member 2 from Mus musculus (Mouse) (see paper)
24% identity, 95% coverage: 4:534/559 of query aligns to 90:699/739 of Q62273
- F368 (≠ V244) mutation to A: Reduced sulfate-chloride exchange activity.
- E417 (= E291) mutation E->A,K: Loss of sulfate-chloride exchange activity.
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)
22% identity, 91% coverage: 32:541/559 of query aligns to 102:629/758 of Q8CIW6
- F552 (= F464) mutation to A: Does not inhibit formate transport in PMA-induced cells.
7lguA Structure of human prestin in the presence of nacl (see paper)
22% identity, 93% coverage: 19:536/559 of query aligns to 65:649/680 of 7lguA
Q9BXS9 Solute carrier family 26 member 6; Anion exchange transporter; Pendrin-like protein 1; Pendrin-L1 from Homo sapiens (Human) (see 3 papers)
23% identity, 80% coverage: 32:476/559 of query aligns to 100:563/759 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 (= V120) to M: in dbSNP:rs13324142
- ATV 547:549 (≠ GPY 460:462) mutation to NVN: Does not inhibit cell membrane localization. Inhibits interaction with CA2 and bicarbonate transport.
- N553 (≠ I466) mutation to A: Does not inhibit interaction with CA2. Inhibits interaction with CA2 and bicarbonate transport in PMA-induced cells.
Sites not aligning to the query:
- 582 S→A: Does not inhibit interaction with CA2. Does not inhibit interaction with CA2 and bicarbonate transport in PMA-induced cells.
8sieC Pendrin in complex with bicarbonate
24% identity, 93% coverage: 19:536/559 of query aligns to 41:591/613 of 8sieC
- binding Lauryl Maltose Neopentyl Glycol: G198 (≠ V158), S296 (≠ W250), T300 (≠ K254), F303 (= F257)
- binding bicarbonate ion: Y65 (≠ F43), F101 (vs. gap), L356 (≠ I314), S357 (≠ A315), V403 (≠ L361), N406 (= N367)
- binding cholesterol: L226 (≠ V186), V255 (= V211), I262 (vs. gap), Y272 (= Y221), F411 (≠ R372), V414 (vs. gap), V414 (vs. gap), C415 (vs. gap), C415 (vs. gap), I436 (≠ F393), M452 (≠ I409), F453 (≠ I410)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: W421 (≠ L378), V429 (≠ T386), V432 (≠ L389), F433 (≠ I390), I436 (≠ F393)
8shcC Pendrin in complex with niflumic acid
24% identity, 93% coverage: 19:536/559 of query aligns to 41:591/613 of 8shcC
- binding cholesterol: I199 (≠ P159), A223 (≠ V183), V255 (= V211), Y272 (= Y221), M412 (≠ V373), C415 (vs. gap), M452 (≠ I409), F453 (≠ I410)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: Q156 (≠ K116), W421 (≠ L378), V432 (≠ L389), F433 (≠ I390), F455 (≠ C412)
- binding 2-{[3-(trifluoromethyl)phenyl]amino}nicotinic acid: Y65 (≠ F43), F101 (vs. gap), T173 (= T133), E252 (≠ I208), I312 (≠ L266), L356 (≠ I314), S357 (≠ A315), V402 (= V360), N406 (= N367)
8sgwC Pendrin in complex with chloride
24% identity, 93% coverage: 19:536/559 of query aligns to 41:591/613 of 8sgwC
- binding Lauryl Maltose Neopentyl Glycol: G198 (≠ V158), S296 (≠ W250), T300 (≠ K254), F303 (= F257)
- binding cholesterol: I228 (= I188), V255 (= V211), I262 (vs. gap), Y272 (= Y221), K408 (≠ S369), F411 (≠ R372), M412 (≠ V373), M412 (≠ V373), V414 (vs. gap), C415 (vs. gap), V417 (≠ F374), I439 (≠ V396)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: F159 (≠ A119), Y163 (≠ F123), F284 (≠ E239), P286 (= P241), I289 (≠ V244), F343 (≠ V301), F346 (≠ L304), W421 (≠ L378), F433 (≠ I390), I436 (≠ F393), F455 (≠ C412), F464 (≠ E421), P465 (≠ T422)
A0FKN5 Prestin; Solute carrier family 26 member 5 from Gallus gallus (Chicken) (see paper)
25% identity, 76% coverage: 2:424/559 of query aligns to 61:510/742 of A0FKN5
- S404 (≠ A315) 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 (= R316) mutation to C: Fully abolishes anion transport.
Q9EPH0 Prestin; Solute carrier family 26 member 5 from Rattus norvegicus (Rat) (see 3 papers)
23% identity, 84% coverage: 19:490/559 of query aligns to 77:577/744 of Q9EPH0
- L104 (≠ A46) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- V149 (≠ Q91) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D154 (≠ A96) 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 (≠ K116) 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 (≠ S152) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (≠ E156) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
- R236 (≠ K157) 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 (≠ P195) 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 (≠ R196) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values.
- R281 (≠ K200) mutation to Q: No effect; when associated with Q-283 and Q-285.
- K283 (≠ P202) mutation to Q: No effect; when associated with Q-218 and Q-285.
- K285 (≠ S204) mutation to Q: No effect; when associated with Q-281 and Q-283.
- P331 (vs. gap) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D332 (= D249) mutation to Q: No effect.
- D342 (≠ V259) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K359 (≠ T276) 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 (≠ G306) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S398 (≠ A315) 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 (= R316) 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 (= G325) 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 (= K326) mutation to Q: No effect.
- L431 (= L348) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S465 (≠ P381) 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 (≠ T401) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- K557 (≠ A475) mutation to Q: No effect; when associated with Q-558 and Q-559.
- R558 (≠ Q476) mutation to Q: No effect; when associated with Q-557 and Q-559.
- K559 (vs. gap) mutation to Q: No effect; when associated with Q-557 and Q-558.
- R571 (= R484) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-572 and Q-577.
- R572 (≠ I485) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-571 and Q-577.
- K577 (= K490) 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
7xujA Human slc26a3 in complex with uk5099
23% identity, 87% coverage: 19:503/559 of query aligns to 63:568/703 of 7xujA
- binding (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid: V79 (= V35), Q83 (≠ L39), E271 (≠ I208), S376 (≠ A315), R377 (= R316), V380 (≠ T319), L421 (= L357), A422 (= A358), N425 (vs. gap)
- binding cholesterol hemisuccinate: F171 (≠ L112), V311 (≠ W250), Q315 (≠ K254)
7xulA Human slc26a3 in complex with tenidap
23% identity, 84% coverage: 19:490/559 of query aligns to 56:541/690 of 7xulA
- binding 5-chloranyl-2-oxidanyl-3-thiophen-2-ylcarbonyl-indole-1-carboxamide: V72 (= V35), L75 (≠ P38), Q76 (≠ L39), E262 (≠ I208), S367 (≠ A315), L412 (= L357), N416 (vs. gap)
- binding cholesterol hemisuccinate: I157 (≠ V107), F162 (≠ L112), P209 (= P159), K214 (≠ G164), Y217 (≠ M167), V302 (≠ W250), Q306 (≠ K254), V309 (≠ F257), V450 (≠ I397)
Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
22% identity, 82% coverage: 19:476/559 of query aligns to 77:558/744 of Q9JKQ2
- 158:168 (vs. 100:101, 0% identical) Involved in motor function
- S398 (≠ A315) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
- R399 (= R316) 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, 84% coverage: 19:490/559 of query aligns to 77:577/744 of P58743
- F101 (= F43) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ A315) binding
7xuhA Down-regulated in adenoma in complex with tqr1122
22% identity, 87% coverage: 19:503/559 of query aligns to 63:572/707 of 7xuhA
- binding 2-[4,8-dimethyl-2-oxidanylidene-7-[[3-(trifluoromethyl)phenyl]methoxy]chromen-3-yl]ethanoic acid: P124 (≠ G80), I125 (≠ A81), L187 (≠ I124), I192 (= I129), F195 (= F132), V335 (≠ E270), S338 (≠ L273), S380 (≠ A315), M433 (≠ V360)
- binding cholesterol hemisuccinate: V223 (≠ G160), F226 (≠ V163), K227 (≠ G164), Y230 (≠ M167), F318 (≠ I253), Q319 (≠ K254)
Query Sequence
>352708 FitnessBrowser__Btheta:352708
MKLFEFKPKLVSCLKNYSKETFMADLMAGVIVGIVALPLAIAFGIASGVSPEKGIITAII
AGFIISLLGGSKVQIGGPTGAFIVIIYGIIQQYGEAGLIVATLMAGVLLILLGVFKLGAV
IKFIPYPIIVGFTSGIAVTIFTTQIADIFGLSFGGEKVPGDFVGKWMIYFRHFDTVNWWN
TIVSIVSIIIIAITPRFSKKIPGSLIAIIVVTVAVYLMKTYGGIDCIPTIGDRFTIKSEL
PDAVVPALDWEAIKNLFPVAITIAVLGAIESLLSATVADGVIGDRHDSNTELIAQGAANI
VAPLFGGIPATGAIARTMTNINNGGKTPIAGIIHAIVLLLILLFLMPLAQYIPMACLAGV
LVIVSYNMSGWRVFKALLKNPKSDVTVLLITFFLTVIFDLTVAIEVGLIIACVLFMKRVM
ETTEISVITDEIDPNKESDIAVNEENIMIPKGVEVYEITGPYFFGIATKFEETMAQLGDR
PNVRIIRMRKVPFIDSTGIHNLTTLCEMSQKEKITVILSGVNEKVYKVLEKSGFYELLGK
ENICPNFKIALDRAEEVMK
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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