SitesBLAST
Comparing 209213 MicrobesOnline__882:209213 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)
31% identity, 92% coverage: 33:553/568 of query aligns to 15:542/564 of Q55415
- T69 (= T87) binding ; mutation to A: Alters bicarbonate transport.
- D258 (≠ E272) binding ; mutation D->A,E: Alters bicarbonate transport.
- T262 (≠ S276) binding ; mutation to A: Alters bicarbonate transport.
- G300 (= G314) binding
- A301 (= A315) binding
- T302 (≠ I316) binding ; mutation to A: Alters bicarbonate transport.
- A471 (≠ V482) mutation to N: Alters bicarbonate transport.
- L476 (≠ M487) mutation to S: Alters bicarbonate transport.
- A486 (= A497) mutation to E: Alters bicarbonate transport.
- L490 (= L501) mutation to Q: Alters bicarbonate transport.
5da0A Structure of the the slc26 transporter slc26dg in complex with a nanobody (see paper)
30% identity, 88% coverage: 32:531/568 of query aligns to 10:467/467 of 5da0A
Sites not aligning to the query:
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
34% identity, 66% coverage: 33:406/568 of query aligns to 14:391/392 of 6ki1B
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
28% identity, 91% coverage: 25:539/568 of query aligns to 20:559/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (≠ C123), R127 (= R124), W130 (≠ A127)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (≠ F125), L131 (= L128), E409 (≠ T403), L413 (≠ Y407), G417 (≠ M411), A421 (≠ L416)
- binding sulfate ion: A84 (≠ G88), S321 (≠ A315), F322 (≠ I316)
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
28% identity, 93% coverage: 33:560/568 of query aligns to 26:597/597 of 7v74A
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
28% identity, 93% coverage: 33:560/568 of query aligns to 26:605/605 of 7v75A
7lguA Structure of human prestin in the presence of nacl (see paper)
22% identity, 78% coverage: 33:473/568 of query aligns to 71:544/680 of 7lguA
P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
22% identity, 78% coverage: 33:473/568 of query aligns to 83:556/744 of P58743
- F101 (= F51) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ A317) binding
Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
22% identity, 78% coverage: 33:473/568 of query aligns to 83:556/744 of Q9JKQ2
- 158:168 (vs. 108:108, 0% identical) Involved in motor function
- S398 (≠ A317) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
- R399 (= R318) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
Q9BXS9 Solute carrier family 26 member 6; Anion exchange transporter; Pendrin-like protein 1; Pendrin-L1 from Homo sapiens (Human) (see 3 papers)
24% identity, 76% coverage: 40:473/568 of query aligns to 100:561/759 of Q9BXS9
- N167 (= N96) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- N172 (≠ M99) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- V206 (≠ L128) to M: in dbSNP:rs13324142
- ATV 547:549 (≠ GPF 459:461) mutation to NVN: Does not inhibit cell membrane localization. Inhibits interaction with CA2 and bicarbonate transport.
- N553 (≠ V465) 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.
Q9EPH0 Prestin; Solute carrier family 26 member 5 from Rattus norvegicus (Rat) (see 3 papers)
21% identity, 78% coverage: 33:473/568 of query aligns to 83:556/744 of Q9EPH0
- L104 (≠ A54) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- V149 (≠ M99) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D154 (= D104) 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 (≠ S160) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (≠ Q162) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
- R236 (≠ S163) 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 (vs. gap) 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 (vs. gap) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values.
- R281 (≠ K202) mutation to Q: No effect; when associated with Q-283 and Q-285.
- K283 (≠ I204) mutation to Q: No effect; when associated with Q-218 and Q-285.
- K285 (≠ R206) mutation to Q: No effect; when associated with Q-281 and Q-283.
- P331 (= P248) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D332 (≠ T249) mutation to Q: No effect.
- D342 (= D261) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K359 (≠ V278) 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 (≠ G308) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S398 (≠ A317) 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 (= R318) 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 (= G327) 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 (≠ R328) mutation to Q: No effect.
- L431 (= L350) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S465 (≠ P383) 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 (≠ T403) 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.
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, 76% coverage: 40:473/568 of query aligns to 102:562/758 of Q8CIW6
- F552 (= F463) mutation to A: Does not inhibit formate transport in PMA-induced cells.
D7PC76 Prestin; Solute carrier family 26 member 5 from Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) (see paper)
21% identity, 80% coverage: 33:489/568 of query aligns to 83:572/741 of D7PC76
- GG 274:275 (vs. gap) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
- S398 (≠ A317) binding
Q9URY8 Probable sulfate permease C869.05c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 69% coverage: 24:413/568 of query aligns to 115:526/840 of Q9URY8
Sites not aligning to the query:
- 823 modified: Phosphoserine
7xujA Human slc26a3 in complex with uk5099
22% identity, 94% coverage: 33:567/568 of query aligns to 69:597/703 of 7xujA
- binding (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid: V79 (= V43), Q83 (≠ L47), E271 (≠ V212), S376 (≠ A317), R377 (= R318), V380 (≠ T321), L421 (vs. gap), A422 (≠ P355), N425 (≠ S358)
- binding cholesterol hemisuccinate: F171 (= F120), V311 (≠ L252), Q315 (≠ R256)
7xulA Human slc26a3 in complex with tenidap
24% identity, 87% coverage: 33:526/568 of query aligns to 62:565/690 of 7xulA
- binding 5-chloranyl-2-oxidanyl-3-thiophen-2-ylcarbonyl-indole-1-carboxamide: V72 (= V43), L75 (≠ P46), Q76 (≠ L47), E262 (≠ V212), S367 (≠ A317), L412 (vs. gap), N416 (≠ S358)
- binding cholesterol hemisuccinate: I157 (≠ A115), F162 (= F120), P209 (= P165), K214 (≠ E170), Y217 (≠ Q173), V302 (≠ L252), Q306 (≠ R256), V309 (≠ L259), V450 (= V399)
7xuhA Down-regulated in adenoma in complex with tqr1122
22% identity, 94% coverage: 33:567/568 of query aligns to 69:601/707 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 (≠ E272), S338 (≠ L275), S380 (≠ A317), M433 (≠ V362)
- binding cholesterol hemisuccinate: V223 (≠ P166), F226 (= F169), K227 (≠ E170), Y230 (≠ Q173), F318 (≠ V255), Q319 (≠ R256)
P58735 Sulfate anion transporter 1; SAT-1; Solute carrier family 26 member 1 from Mus musculus (Mouse) (see paper)
22% identity, 93% coverage: 33:558/568 of query aligns to 72:699/704 of P58735
- T190 (= T110) mutation to M: Decreased sulfate-hydrogencarbonate exchange activity. Loss of localization to plasma membrane.
- S363 (≠ L275) 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)
25% identity, 59% coverage: 33:365/568 of query aligns to 84:452/742 of A0FKN5
- S404 (≠ A317) 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 (= R318) mutation to C: Fully abolishes anion transport.
8sieC Pendrin in complex with bicarbonate
22% identity, 88% coverage: 33:532/568 of query aligns to 47:588/613 of 8sieC
- binding Lauryl Maltose Neopentyl Glycol: G198 (vs. gap), S296 (≠ R256), T300 (≠ P260), F303 (≠ M263)
- binding bicarbonate ion: Y65 (≠ F51), F101 (≠ T87), L356 (≠ I316), S357 (≠ A317), V403 (≠ L363), N406 (≠ V366)
- binding cholesterol: L226 (≠ C187), V255 (≠ A217), I262 (≠ L224), Y272 (≠ R234), F411 (vs. gap), V414 (≠ M373), V414 (≠ M373), C415 (≠ H374), C415 (≠ H374), I436 (≠ A395), M452 (= M411), F453 (≠ L412)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: W421 (≠ L380), V429 (≠ L388), V432 (≠ C391), F433 (≠ L392), I436 (≠ A395)
Query Sequence
>209213 MicrobesOnline__882:209213
MAIPSGATGKEPFLPRTLTVLREGYDGGTFFKDLAAGLTVGIVALPLAMAFAIASGTTPE
RGLFTAIVAGFLISLLGGSRYQIGGPTGAFVIIIFNVIMKHGYDGLVVTTLLAGAMLLVF
GLCRFGALIKYIPYPVTTGFTAGIAVLIFSQQVKDFLGLSMQSVPPDFFEKWQAYIHNAA
TFDPATCGIAFLALGAIILTRKTIPRIPGPVVGVVLASLTVWALGLDVETIGSRFGGIPT
ELPTFTLPTVTLERVRQLLPDAMTIALLAGIESLLSCVVADGMTGDKHNSNVELAAQGAA
NIASVMFGGIPATGAIARTVTNIRSGGRTPVAGMIHAAVLVGFILYLAPLASFIPLASLA
AVLMVVAWDMSEMHKFLRLLHAPKSDVLVMCLTFALTVVIDLTVAVYVGVMLASLLFMRR
MSEVTQICTCLDGEATKVQGRETAELDVPEGVKVYEIDGPFFFGVADRFQNVLAALDRQP
EVFILRMRKVSTLDSTAVNALEVFWRKCRSDGTQLLLSGVRETMRTTLRRMGTLSLIGEG
NICENIDAALARAGQVLAERREAEDRPQ
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