SitesBLAST
Comparing 8500834 FitnessBrowser__Miya:8500834 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, 92% coverage: 34:555/570 of query aligns to 15:543/564 of Q55415
- T69 (= T88) binding ; mutation to A: Alters bicarbonate transport.
- D258 (≠ E273) binding ; mutation D->A,E: Alters bicarbonate transport.
- T262 (≠ S277) binding ; mutation to A: Alters bicarbonate transport.
- G300 (= G315) binding
- A301 (= A316) binding
- T302 (≠ I317) binding ; mutation to A: Alters bicarbonate transport.
- A471 (≠ E482) 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, 88% coverage: 33:531/570 of query aligns to 10:466/467 of 5da0A
Sites not aligning to the query:
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
27% identity, 93% coverage: 22:552/570 of query aligns to 17:571/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (≠ C124), R127 (= R125), W130 (≠ V128)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (≠ I126), L131 (= L129), E409 (≠ T404), L413 (≠ Y408), G417 (≠ M412), A421 (≠ L417)
- binding sulfate ion: A84 (≠ G89), S321 (≠ A316), F322 (≠ I317)
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
28% identity, 96% coverage: 13:561/570 of query aligns to 6:597/597 of 7v74A
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
28% identity, 96% coverage: 13:561/570 of query aligns to 6:605/605 of 7v75A
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
34% identity, 66% coverage: 34:407/570 of query aligns to 14:391/392 of 6ki1B
D7PC76 Prestin; Solute carrier family 26 member 5 from Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) (see paper)
24% identity, 84% coverage: 14:492/570 of query aligns to 64:574/741 of D7PC76
- GG 274:275 (≠ AC 196:197) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
- S398 (≠ A318) binding
Q9EPH0 Prestin; Solute carrier family 26 member 5 from Rattus norvegicus (Rat) (see 3 papers)
24% identity, 84% coverage: 14:491/570 of query aligns to 64:574/744 of Q9EPH0
- L104 (≠ A55) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- V149 (≠ Y100) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D154 (= D105) mutation to N: Shifts the voltage-sensitivity to more negative values.
- D155 (≠ G106) 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 (= R125) mutation to Q: Shifts the voltage-sensitivity to more negative values.
- A202 (≠ I130) 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 (≠ Q161) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (≠ D163) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
- R236 (≠ A164) 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 (≠ I198) 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 (≠ L199) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values.
- R281 (= R203) mutation to Q: No effect; when associated with Q-283 and Q-285.
- K283 (≠ I205) mutation to Q: No effect; when associated with Q-218 and Q-285.
- K285 (≠ R207) mutation to Q: No effect; when associated with Q-281 and Q-283.
- P331 (= P244) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D332 (≠ S245) mutation to Q: No effect.
- D342 (= D262) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K359 (≠ V279) 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 (≠ G309) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S398 (≠ A318) 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 (= R319) 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 (= G328) 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 (≠ Q329) mutation to Q: No effect.
- L431 (= L351) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S465 (≠ P384) 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 (≠ T404) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- K557 (≠ Q478) mutation to Q: No effect; when associated with Q-558 and Q-559.
- R558 (≠ K479) mutation to Q: No effect; when associated with Q-557 and Q-559.
- K559 (≠ Q480) mutation to Q: No effect; when associated with Q-557 and Q-558.
- R571 (≠ M488) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-572 and Q-577.
- R572 (= R489) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-571 and Q-577.
Sites not aligning to the query:
- 505:718 Extended region for STAS domain
- 577 K→Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-571 and Q-572.
7lguA Structure of human prestin in the presence of nacl (see paper)
24% identity, 84% coverage: 14:491/570 of query aligns to 52:562/680 of 7lguA
P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
24% identity, 84% coverage: 14:491/570 of query aligns to 64:574/744 of P58743
- F101 (= F52) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ A318) binding
Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
24% identity, 82% coverage: 14:480/570 of query aligns to 64:559/744 of Q9JKQ2
- 158:168 (vs. 109:109, 9% identical) Involved in motor function
- S398 (≠ A318) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
- R399 (= R319) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
Q9URY8 Probable sulfate permease C869.05c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
27% identity, 71% coverage: 19:424/570 of query aligns to 109:540/840 of Q9URY8
Sites not aligning to the query:
- 823 modified: Phosphoserine
8sieC Pendrin in complex with bicarbonate
23% identity, 92% coverage: 32:553/570 of query aligns to 45:609/613 of 8sieC
- binding Lauryl Maltose Neopentyl Glycol: G198 (≠ P167), S296 (≠ A254), T300 (≠ P261), F303 (≠ M264)
- binding bicarbonate ion: Y65 (≠ F52), F101 (≠ T88), L356 (≠ I317), S357 (≠ A318), V403 (≠ L364), N406 (≠ V367)
- binding cholesterol: L226 (= L193), V255 (≠ G214), I262 (≠ A221), Y272 (≠ T231), F411 (vs. gap), V414 (≠ L374), V414 (≠ L374), C415 (≠ H375), C415 (≠ H375), I436 (≠ V396), M452 (= M412), F453 (≠ L413)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: W421 (≠ L381), V429 (≠ T389), V432 (≠ C392), F433 (≠ L393), I436 (≠ V396)
8shcC Pendrin in complex with niflumic acid
23% identity, 92% coverage: 32:553/570 of query aligns to 45:609/613 of 8shcC
- binding cholesterol: I199 (vs. gap), A223 (≠ V190), V255 (≠ G214), Y272 (≠ T231), M412 (≠ S372), C415 (≠ H375), M452 (= M412), F453 (≠ L413)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: Q156 (≠ R125), W421 (≠ L381), V432 (≠ C392), F433 (≠ L393), F455 (≠ S415)
- binding 2-{[3-(trifluoromethyl)phenyl]amino}nicotinic acid: Y65 (≠ F52), F101 (≠ T88), T173 (= T142), E252 (vs. gap), I312 (≠ E273), L356 (≠ I317), S357 (≠ A318), V402 (= V363), N406 (≠ V367)
8sgwC Pendrin in complex with chloride
23% identity, 92% coverage: 32:553/570 of query aligns to 45:609/613 of 8sgwC
- binding Lauryl Maltose Neopentyl Glycol: G198 (≠ P167), S296 (≠ A254), T300 (≠ P261), F303 (≠ M264)
- binding cholesterol: I228 (≠ L195), V255 (≠ G214), I262 (≠ A221), Y272 (≠ T231), K408 (≠ W369), F411 (vs. gap), M412 (≠ S372), M412 (≠ S372), V414 (≠ L374), C415 (≠ H375), V417 (≠ F377), I439 (≠ V399)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: F159 (≠ V128), Y163 (= Y132), F284 (vs. gap), P286 (= P244), I289 (≠ V247), F343 (≠ A304), F346 (≠ L307), W421 (≠ L381), F433 (≠ L393), I436 (≠ V396), F455 (≠ S415), F464 (≠ E424), P465 (≠ V425)
P58735 Sulfate anion transporter 1; SAT-1; Solute carrier family 26 member 1 from Mus musculus (Mouse) (see paper)
24% identity, 78% coverage: 26:470/570 of query aligns to 63:559/704 of P58735
- T190 (= T111) mutation to M: Decreased sulfate-hydrogencarbonate exchange activity. Loss of localization to plasma membrane.
- S363 (≠ L276) 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.
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, 79% coverage: 41:488/570 of query aligns to 102:573/758 of Q8CIW6
- F552 (= F464) mutation to A: Does not inhibit formate transport in PMA-induced cells.
7xujA Human slc26a3 in complex with uk5099
23% identity, 76% coverage: 32:465/570 of query aligns to 67:525/703 of 7xujA
- binding (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid: V79 (= V44), Q83 (≠ L48), E271 (vs. gap), S376 (≠ A318), R377 (= R319), V380 (≠ T322), L421 (= L360), A422 (= A361), N425 (≠ M366)
- binding cholesterol hemisuccinate: F171 (= F121), V311 (≠ T250), Q315 (≠ R257)
7xulA Human slc26a3 in complex with tenidap
23% identity, 76% coverage: 32:465/570 of query aligns to 60:516/690 of 7xulA
- binding 5-chloranyl-2-oxidanyl-3-thiophen-2-ylcarbonyl-indole-1-carboxamide: V72 (= V44), L75 (≠ P47), Q76 (≠ L48), E262 (vs. gap), S367 (≠ A318), L412 (= L360), N416 (≠ M366)
- binding cholesterol hemisuccinate: I157 (≠ A116), F162 (= F121), P209 (= P166), K214 (≠ D171), Y217 (≠ L174), V302 (≠ T250), Q306 (≠ R257), V309 (≠ L260), V450 (= V400)
7xuhA Down-regulated in adenoma in complex with tqr1122
23% identity, 76% coverage: 32:465/570 of query aligns to 67:529/707 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 (≠ I133), I192 (≠ T138), F195 (= F141), V335 (≠ E273), S338 (≠ L276), S380 (≠ A318), M433 (≠ D370)
- binding cholesterol hemisuccinate: V223 (≠ P167), F226 (= F170), K227 (≠ D171), Y230 (≠ L174), F318 (= F253), Q319 (≠ R257)
Query Sequence
>8500834 FitnessBrowser__Miya:8500834
MAGTDNMSDEATSFLPRTITELRAGYSTQKFIRDLLAGLTVGVVALPLAMAFAIASGTTP
ERGLFTAIVAGFLISLLGGSRYQIGGPTGAFVVIIYNVIYRHGYDGLVITTLLAGAMLLI
FGLCRIGVLIKYIPYPVTTGFTAGIAVLIFSSQMKDFFGLQMDAVPPEFFDKWLAYAEHL
GTINTTTLCVAGLALACILATRRFIPRIPAPVVGVAVASLAVWALGLQVETIGSRFGGIP
RELPSFVWPTFTFARVRELLPDAMTIALLAGIESLLSCVVADGMTGDKHNSNVELTAQGV
ANIASVLFGGIPATGAIARTVTNIRSGGQTPVAGMVHAAVLVAFVLFLAPLASFIPLASL
AAVLIMVSWDMSELHKFLRLLRAPKSDITVMCLTFVLTVVIDLTVAVYVGVMLASLLFMR
RMSEVTAICSCAIDDKPVIQGRETAELVVPEGVQVYEIDGPFFFGVADRFQSVSQALQKQ
PEVFILRMRKASTVDSTGANALEAFCRTCRRRGTVLLLSGVRPAARRMMERFGTLDLIGR
ENLFENVDRAIEHAVRLLADKHGVPPTAKK
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