SitesBLAST
Comparing 6936893 FitnessBrowser__SB2B:6936893 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)
28% identity, 94% coverage: 29:568/572 of query aligns to 11:543/564 of Q55415
- T69 (= T87) binding ; mutation to A: Alters bicarbonate transport.
- D258 (≠ E296) binding ; mutation D->A,E: Alters bicarbonate transport.
- T262 (≠ C300) binding ; mutation to A: Alters bicarbonate transport.
- G300 (≠ A338) binding
- A301 (= A339) binding
- T302 (≠ I340) binding ; mutation to A: Alters bicarbonate transport.
- A471 (≠ P495) mutation to N: Alters bicarbonate transport.
- L476 (≠ W501) mutation to S: Alters bicarbonate transport.
- A486 (≠ G511) mutation to E: Alters bicarbonate transport.
- L490 (= L515) mutation to Q: Alters bicarbonate transport.
5da0A Structure of the the slc26 transporter slc26dg in complex with a nanobody (see paper)
27% identity, 89% coverage: 23:531/572 of query aligns to 1:453/467 of 5da0A
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
28% identity, 94% coverage: 24:559/572 of query aligns to 16:570/597 of 7v74A
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
28% identity, 94% coverage: 24:559/572 of query aligns to 16:578/605 of 7v75A
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
25% identity, 98% coverage: 7:565/572 of query aligns to 7:571/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (≠ M123), R127 (= R124), W130 (≠ R127)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (= L125), L131 (= L128), E409 (≠ V428), L413 (vs. gap), G417 (= G434), A421 (= A438)
- binding sulfate ion: A84 (= A88), S321 (≠ A339), F322 (≠ I340)
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
28% identity, 71% coverage: 29:432/572 of query aligns to 10:392/392 of 6ki1B
7lguA Structure of human prestin in the presence of nacl (see paper)
21% identity, 97% coverage: 7:560/572 of query aligns to 55:625/680 of 7lguA
Q9EPH0 Prestin; Solute carrier family 26 member 5 from Rattus norvegicus (Rat) (see 3 papers)
22% identity, 85% coverage: 7:493/572 of query aligns to 67:561/744 of Q9EPH0
- L104 (≠ A54) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- V149 (≠ A99) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D154 (≠ G104) mutation to N: Shifts the voltage-sensitivity to more negative values.
- D155 (≠ G105) 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 (= R124) mutation to Q: Shifts the voltage-sensitivity to more negative values.
- A202 (≠ I129) 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 (≠ P160) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (≠ E162) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
- R236 (≠ A163) 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 (≠ P201) 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 (≠ K202) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values.
- R281 (≠ K206) mutation to Q: No effect; when associated with Q-283 and Q-285.
- K283 (≠ P208) mutation to Q: No effect; when associated with Q-218 and Q-285.
- K285 (≠ H210) mutation to Q: No effect; when associated with Q-281 and Q-283.
- P331 (≠ L274) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D332 (≠ N275) mutation to Q: No effect.
- D342 (≠ S285) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K359 (≠ V302) 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 (≠ G332) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S398 (≠ A341) 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 (= R342) 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 (≠ A351) 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 (= K352) mutation to Q: No effect.
- L431 (≠ V374) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S465 (≠ H408) 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 (≠ A424) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- K557 (≠ H489) mutation to Q: No effect; when associated with Q-558 and Q-559.
- R558 (= R490) mutation to Q: No effect; when associated with Q-557 and Q-559.
- K559 (≠ Q491) mutation to Q: No effect; when associated with Q-557 and Q-558.
Sites not aligning to the query:
- 505:718 Extended region for STAS domain
- 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)
22% identity, 86% coverage: 7:499/572 of query aligns to 67:568/744 of Q9JKQ2
- 158:168 (vs. 108:108, 0% identical) Involved in motor function
- S398 (≠ A341) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
- R399 (= R342) 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)
22% identity, 85% coverage: 7:493/572 of query aligns to 67:561/744 of P58743
- F101 (≠ L51) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ A341) binding
7xulA Human slc26a3 in complex with tenidap
24% identity, 91% coverage: 7:526/572 of query aligns to 46:554/690 of 7xulA
- binding 5-chloranyl-2-oxidanyl-3-thiophen-2-ylcarbonyl-indole-1-carboxamide: V72 (≠ I43), L75 (≠ P46), Q76 (≠ L47), E262 (≠ I214), S367 (≠ A341), L412 (= L386), N416 (≠ V390)
- binding cholesterol hemisuccinate: I157 (≠ V115), F162 (≠ M120), P209 (= P165), K214 (≠ H170), Y217 (≠ S173), V302 (≠ W276), Q306 (= Q280), V309 (≠ L283), V450 (≠ A430)
D7PC76 Prestin; Solute carrier family 26 member 5 from Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) (see paper)
21% identity, 85% coverage: 7:493/572 of query aligns to 67:561/741 of D7PC76
- GG 274:275 (≠ FW 199:200) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
- S398 (≠ A341) binding
Q9URY8 Probable sulfate permease C869.05c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
27% identity, 67% coverage: 5:388/572 of query aligns to 101:480/840 of Q9URY8
Sites not aligning to the query:
- 823 modified: Phosphoserine
7xujA Human slc26a3 in complex with uk5099
23% identity, 91% coverage: 7:526/572 of query aligns to 53:563/703 of 7xujA
- binding (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid: V79 (≠ I43), Q83 (≠ L47), E271 (≠ G217), S376 (≠ A341), R377 (= R342), V380 (≠ A345), L421 (= L386), A422 (≠ L387), N425 (≠ V390)
- binding cholesterol hemisuccinate: F171 (≠ M120), V311 (≠ W276), Q315 (= Q280)
7xuhA Down-regulated in adenoma in complex with tqr1122
23% identity, 91% coverage: 7:526/572 of query aligns to 53:567/707 of 7xuhA
- binding 2-[4,8-dimethyl-2-oxidanylidene-7-[[3-(trifluoromethyl)phenyl]methoxy]chromen-3-yl]ethanoic acid: P124 (vs. gap), I125 (vs. gap), L187 (≠ I132), I192 (≠ T137), F195 (= F140), V335 (≠ E296), S338 (≠ L299), S380 (≠ A341), M433 (= M394)
- binding cholesterol hemisuccinate: V223 (≠ E166), F226 (≠ W169), K227 (≠ H170), Y230 (≠ S173), F318 (≠ V279), Q319 (= Q280)
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, 91% coverage: 7:526/572 of query aligns to 60:585/764 of P40879
- N153 (≠ A89) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- N161 (≠ I97) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- N165 (≠ Y101) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- C307 (≠ V231) 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.
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)
23% identity, 87% coverage: 40:534/572 of query aligns to 102:609/758 of Q8CIW6
- F552 (= F477) 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)
22% identity, 80% coverage: 40:496/572 of query aligns to 100:569/759 of Q9BXS9
- N167 (≠ G104) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- N172 (≠ A109) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- V206 (≠ L128) to M: in dbSNP:rs13324142
- ATV 547:549 (≠ GPL 473:475) mutation to NVN: Does not inhibit cell membrane localization. Inhibits interaction with CA2 and bicarbonate transport.
- N553 (≠ A479) 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.
3ny7A Stas domain of ychm bound to acp (see paper)
47% identity, 17% coverage: 470:566/572 of query aligns to 22:117/118 of 3ny7A
8sieC Pendrin in complex with bicarbonate
21% identity, 91% coverage: 24:546/572 of query aligns to 37:588/613 of 8sieC
- binding Lauryl Maltose Neopentyl Glycol: G198 (≠ E166), S296 (≠ G269), T300 (= T273), F303 (≠ W276)
- binding bicarbonate ion: Y65 (≠ L51), F101 (vs. gap), L356 (≠ I340), S357 (≠ A341), V403 (≠ L387), N406 (≠ V390)
- binding cholesterol: L226 (= L188), V255 (≠ G217), I262 (≠ L224), Y272 (≠ L247), F411 (≠ S395), V414 (≠ K398), V414 (≠ K398), C415 (≠ K399), C415 (≠ K399), I436 (≠ L419), M452 (vs. gap), F453 (vs. gap)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: W421 (≠ R405), V429 (≠ A413), V432 (≠ L415), F433 (≠ L416), I436 (≠ L419)
Query Sequence
>6936893 FitnessBrowser__SB2B:6936893
MPHRHHLTSLIPAFALRQSLLGERYSRAELLADLLAGITVGVIAIPLAMALAIASGVAPQ
YGLYTAIIAGIIIAISGGSKLSVSGPTAAFVVLLAPISAQYGLGGLLLATVMSGVILLLM
SLMRLGRLIQYIPEPVTLGFTGGIAIVIAMLQIKDMFALPVEALPEDFWHKVSTLFHAMP
HAQWPSILVAAITLSVLVFWPKFTQKLPPHLPAILAGTLCALALGGLGFDVETIGSRFSF
TLDDGTLMAGIPSVLPSFLLPWELPGVGGEPLTLNWQLVQNLLPSAMAIAMLGAIESLLC
AVVVDGMTGNRHSANSELFGQGLGNLIAPFFGAIPATAAIARSAANVRAGAKSPLAAVFH
ALTVLLALVLLAPVLAYIPMATMAALLLVVAWHMSEAKKSLHLIRRAHVSDVAVLLTCLM
LTVAFDMVIAIGVGIVLASLLLMGQLAASTRLVALDCGSDAGSPNIEAFRIDGPLFFAAA
DNLFSELMHRQNGAPILVLDWQNVSLLDAGGLSALERTVAWAQKQGREIRIVSVPFQALR
ALVKAGVQEKPGVLSFYPDMTAALQDTVTNTD
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