SitesBLAST
Comparing GFF3298 FitnessBrowser__Marino:GFF3298 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)
5da0A Structure of the the slc26 transporter slc26dg in complex with a nanobody (see paper)
27% identity, 88% coverage: 21:522/572 of query aligns to 10:451/467 of 5da0A
Sites not aligning to the query:
Q55415 Bicarbonate transporter BicA from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
28% identity, 96% coverage: 10:558/572 of query aligns to 3:540/564 of Q55415
- T69 (= T76) binding ; mutation to A: Alters bicarbonate transport.
- D258 (≠ E285) binding ; mutation D->A,E: Alters bicarbonate transport.
- T262 (≠ C289) binding ; mutation to A: Alters bicarbonate transport.
- G300 (≠ A327) binding
- A301 (= A328) binding
- T302 (≠ I329) binding ; mutation to A: Alters bicarbonate transport.
- A471 (≠ G489) mutation to N: Alters bicarbonate transport.
- L476 (≠ M494) mutation to S: Alters bicarbonate transport.
- A486 (≠ G504) mutation to E: Alters bicarbonate transport.
- L490 (= L508) mutation to Q: Alters bicarbonate transport.
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
26% identity, 95% coverage: 14:559/572 of query aligns to 20:572/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (≠ M112), R127 (= R113), W130 (≠ R116)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (= L114), L131 (≠ F117), E409 (≠ V417), L413 (≠ T421), G417 (≠ L425), A421 (≠ V429)
- binding sulfate ion: A84 (= A77), S321 (≠ A328), F322 (≠ I329)
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
30% identity, 72% coverage: 10:420/572 of query aligns to 2:391/392 of 6ki1B
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
26% identity, 91% coverage: 20:539/572 of query aligns to 24:566/597 of 7v74A
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
26% identity, 91% coverage: 20:539/572 of query aligns to 24:574/605 of 7v75A
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, 78% coverage: 29:474/572 of query aligns to 102:556/758 of Q8CIW6
- F552 (= F470) mutation to A: Does not inhibit formate transport in PMA-induced cells.
P58735 Sulfate anion transporter 1; SAT-1; Solute carrier family 26 member 1 from Mus musculus (Mouse) (see paper)
25% identity, 97% coverage: 14:568/572 of query aligns to 63:660/704 of P58735
- T190 (= T99) mutation to M: Decreased sulfate-hydrogencarbonate exchange activity. Loss of localization to plasma membrane.
- S363 (≠ L288) 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.
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, 78% coverage: 29:474/572 of query aligns to 100:555/759 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 (≠ F117) to M: in dbSNP:rs13324142
- ATV 547:549 (≠ GPL 466:468) mutation to NVN: Does not inhibit cell membrane localization. Inhibits interaction with CA2 and bicarbonate transport.
- N553 (≠ A472) 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.
7xujA Human slc26a3 in complex with uk5099
23% identity, 80% coverage: 14:471/572 of query aligns to 60:525/703 of 7xujA
- binding (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid: V79 (≠ I32), Q83 (≠ L36), E271 (≠ V203), S376 (≠ A330), R377 (= R331), V380 (≠ A334), L421 (= L375), A422 (≠ L376), N425 (≠ V379)
- binding cholesterol hemisuccinate: F171 (≠ M109), V311 (≠ A248), Q315 (= Q252)
7xulA Human slc26a3 in complex with tenidap
23% identity, 80% coverage: 14:471/572 of query aligns to 53:516/690 of 7xulA
- binding 5-chloranyl-2-oxidanyl-3-thiophen-2-ylcarbonyl-indole-1-carboxamide: V72 (≠ I32), L75 (≠ P35), Q76 (≠ L36), E262 (≠ V203), S367 (≠ A330), L412 (= L375), N416 (≠ V379)
- binding cholesterol hemisuccinate: I157 (≠ V104), F162 (≠ M109), P209 (≠ K160), K214 (≠ A165), Y217 (≠ L168), V302 (≠ A248), Q306 (= Q252), V309 (≠ S257), V450 (≠ L413)
7xuhA Down-regulated in adenoma in complex with tqr1122
23% identity, 80% coverage: 14:471/572 of query aligns to 60:529/707 of 7xuhA
- binding 2-[4,8-dimethyl-2-oxidanylidene-7-[[3-(trifluoromethyl)phenyl]methoxy]chromen-3-yl]ethanoic acid: P124 (≠ A77), I125 (≠ A78), L187 (≠ I121), I192 (≠ T126), F195 (= F129), V335 (≠ I278), S338 (vs. gap), S380 (≠ A330), M433 (= M383)
- binding cholesterol hemisuccinate: V223 (≠ L161), F226 (≠ L164), K227 (≠ A165), Y230 (≠ L168), F318 (≠ W251), Q319 (= Q252)
7lguA Structure of human prestin in the presence of nacl (see paper)
21% identity, 81% coverage: 14:474/572 of query aligns to 62:538/680 of 7lguA
P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
21% identity, 81% coverage: 14:474/572 of query aligns to 74:550/744 of P58743
- F101 (≠ L40) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ A330) binding
Q9EPH0 Prestin; Solute carrier family 26 member 5 from Rattus norvegicus (Rat) (see 3 papers)
21% identity, 81% coverage: 14:474/572 of query aligns to 74:550/744 of Q9EPH0
- L104 (≠ A43) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- V149 (≠ Q88) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D154 (≠ G93) mutation to N: Shifts the voltage-sensitivity to more negative values.
- D155 (≠ G94) 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 (= R113) mutation to Q: Shifts the voltage-sensitivity to more negative values.
- A202 (≠ I118) 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 (≠ Q149) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (vs. gap) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
- R236 (vs. gap) 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 (≠ M186) 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 (≠ L187) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values.
- R281 (= R191) mutation to Q: No effect; when associated with Q-283 and Q-285.
- K283 (= K193) mutation to Q: No effect; when associated with Q-218 and Q-285.
- K285 (≠ P195) mutation to Q: No effect; when associated with Q-281 and Q-283.
- P331 (= P245) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D332 (≠ E246) mutation to Q: No effect.
- D342 (≠ A274) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K359 (≠ V291) 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 (≠ G321) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S398 (≠ A330) 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 (= R331) 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 (≠ A340) 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 (≠ E341) mutation to Q: No effect.
- L431 (= L363) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S465 (≠ P397) 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 (≠ V417) 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.
P40879 Chloride anion exchanger; Down-regulated in adenoma; Protein DRA; Solute carrier family 26 member 3 from Homo sapiens (Human) (see 3 papers)
23% identity, 80% coverage: 14:471/572 of query aligns to 67:547/764 of P40879
- N153 (≠ Q88) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- N161 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- N165 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- C307 (≠ A218) to W: in dbSNP:rs34407351
Sites not aligning to the query:
- 761:764 PDZ-binding; mutation Missing: Loss of interaction with NHERF4. No effect on localization to cell membrane or its exchanger activity.
Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
21% identity, 81% coverage: 14:474/572 of query aligns to 74:550/744 of Q9JKQ2
- 158:168 (vs. 97:97, 0% identical) Involved in motor function
- S398 (≠ A330) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
- R399 (= R331) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
A0FKN5 Prestin; Solute carrier family 26 member 5 from Gallus gallus (Chicken) (see paper)
21% identity, 80% coverage: 20:474/572 of query aligns to 82:556/742 of A0FKN5
- S404 (≠ A330) 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 (= R331) mutation to C: Fully abolishes anion transport.
Q62273 Sulfate transporter; Diastrophic dysplasia protein homolog; ST-OB; Solute carrier family 26 member 2 from Mus musculus (Mouse) (see paper)
23% identity, 79% coverage: 17:470/572 of query aligns to 106:589/739 of Q62273
- F368 (≠ A248) mutation to A: Reduced sulfate-chloride exchange activity.
- E417 (= E306) mutation E->A,K: Loss of sulfate-chloride exchange activity.
D7PC76 Prestin; Solute carrier family 26 member 5 from Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) (see paper)
21% identity, 81% coverage: 14:474/572 of query aligns to 74:550/741 of D7PC76
- GG 274:275 (≠ AC 184:185) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
- S398 (≠ A330) binding
Query Sequence
>GFF3298 FitnessBrowser__Marino:GFF3298
MAHAFREACIDEPYRGRRFLRDVMAGLTVGIIAIPLAMALAIASGVAPQYGLYTAIIAGF
VIALTGGSRFSISGPTAAFVVILYPIAQSYGLGGLLLATLMSGVLLILMALMRLGRFIEY
IPESVTLGFTGGIAVVIATLQIRDFLGLQVSDMPEHYWDKLALLAGALPEFDGMSALVAG
VTLACMLLWPRLKTPVPPHLPAVVIGSLLALWLNAQGAAIDTIGSRFSYLLPDGTEGAGI
PPFLPEFAWPWQQAGASGEPVGLSWSLVRDLLPAAFAIAMLGAIESLLCAVVLDGMTGKR
HSANSELMGQGLGNIITPFFGGITATAAIARSAANYRAGAESPVSAMVHSLVVLLALVSL
AGLLAYLPMPAMAALLVMVAWNMSEAPKSLHLLKTAPRSDILVFLTCFSLTVLLDMVIAI
TTGVLLAAVLFMREMAQMTRVTDITQSKRIAESRLPDGWQVFKINGPLFFAAADRIFGEL
AVLARNARGFILYMDGVTILDAGGLSALNKLIATCERDGTQIVIADLQFQPLRTLARAGV
APIAGVSRYTSSLDEALRLISCPASETDRASG
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