SitesBLAST
Comparing WP_011841529.1 NCBI__GCF_000015985.1:WP_011841529.1 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)
32% identity, 89% coverage: 30:512/545 of query aligns to 9:457/467 of 5da0A
Sites not aligning to the query:
Q55415 Bicarbonate transporter BicA from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
30% identity, 90% coverage: 27:519/545 of query aligns to 10:517/564 of Q55415
- T69 (≠ A86) binding hydrogencarbonate; mutation to A: Alters bicarbonate transport.
- D258 (≠ E272) binding Na(+); mutation D->A,E: Alters bicarbonate transport.
- T262 (≠ S276) binding Na(+); mutation to A: Alters bicarbonate transport.
- G300 (= G314) binding Na(+)
- A301 (≠ T315) binding hydrogencarbonate
- T302 (≠ I316) binding Na(+); mutation to A: Alters bicarbonate transport.
- A471 (= A473) mutation to N: Alters bicarbonate transport.
- L476 (≠ F478) mutation to S: Alters bicarbonate transport.
- A486 (≠ G488) mutation to E: Alters bicarbonate transport.
- L490 (≠ F492) mutation to Q: Alters bicarbonate transport.
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
33% identity, 69% coverage: 27:402/545 of query aligns to 9:387/392 of 6ki1B
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
27% identity, 90% coverage: 24:515/545 of query aligns to 17:558/597 of 7v74A
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
27% identity, 90% coverage: 24:515/545 of query aligns to 17:566/605 of 7v75A
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
26% identity, 91% coverage: 29:526/545 of query aligns to 26:555/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (= L122), R127 (≠ K123), W130 (≠ S126)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (= L124), L131 (≠ Y127), E409 (≠ T403), L413 (≠ V407), G417 (≠ A411), A421 (≠ L415)
- binding sulfate ion: A84 (≠ G87), S321 (≠ T315), F322 (≠ I316)
7lguA Structure of human prestin in the presence of nacl (see paper)
21% identity, 92% coverage: 12:515/545 of query aligns to 52:638/680 of 7lguA
A0FKN5 Prestin; Solute carrier family 26 member 5 from Gallus gallus (Chicken) (see paper)
25% identity, 74% coverage: 29:434/545 of query aligns to 81:522/742 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.
P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
22% identity, 83% coverage: 12:466/545 of query aligns to 64:558/744 of P58743
- F101 (≠ I50) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ A317) binding salicylate
Q9URY8 Probable sulfate permease C869.05c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
24% identity, 73% coverage: 11:409/545 of query aligns to 101:526/840 of Q9URY8
Sites not aligning to the query:
- 823 modified: Phosphoserine
Q9EPH0 Prestin; Solute carrier family 26 member 5 from Rattus norvegicus (Rat) (see 3 papers)
21% identity, 83% coverage: 12:466/545 of query aligns to 64:558/744 of Q9EPH0
- L104 (≠ A53) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- V149 (≠ M98) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D154 (≠ E103) mutation to N: Shifts the voltage-sensitivity to more negative values.
- D155 (≠ G104) 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 (≠ K123) mutation to Q: Shifts the voltage-sensitivity to more negative values.
- A202 (≠ I128) 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 (vs. gap) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (≠ L160) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
- R236 (≠ A161) 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 (= K201) 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 (≠ R202) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values.
- R281 (= R206) 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 (≠ L210) mutation to Q: No effect; when associated with Q-281 and Q-283.
- P331 (≠ R252) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D332 (≠ E253) mutation to Q: No effect.
- D342 (vs. gap) 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 (≠ S327) 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 (= S383) 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.
- K557 (≠ D465) mutation to Q: No effect; when associated with Q-558 and Q-559.
- R558 (= R466) mutation to Q: No effect; when associated with Q-557 and Q-559.
Sites not aligning to the query:
- 505:718 Extended region for STAS domain
- 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.
D7PC76 Prestin; Solute carrier family 26 member 5 from Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) (see paper)
21% identity, 85% coverage: 12:476/545 of query aligns to 64:568/741 of D7PC76
- GG 274:275 (≠ GL 199:200) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
- S398 (≠ A317) binding salicylate
Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
21% identity, 83% coverage: 12:466/545 of query aligns to 64:558/744 of Q9JKQ2
- 158:168 (vs. 107:107, 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.
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, 79% coverage: 39:466/545 of query aligns to 102:564/758 of Q8CIW6
- F552 (= F454) mutation to A: Does not inhibit formate transport in PMA-induced cells.
7xulA Human slc26a3 in complex with tenidap
23% identity, 79% coverage: 24:453/545 of query aligns to 53:496/690 of 7xulA
- binding 5-chloranyl-2-oxidanyl-3-thiophen-2-ylcarbonyl-indole-1-carboxamide: V72 (= V42), L75 (≠ P45), Q76 (≠ L46), E262 (≠ S218), S367 (≠ A317), L412 (= L359), N416 (≠ V365)
- binding cholesterol hemisuccinate: I157 (≠ F114), F162 (≠ M119), P209 (= P165), K214 (≠ E170), Y217 (≠ E173), V302 (≠ L250), Q306 (≠ R252), V309 (≠ I255), V450 (≠ F399)
8tnyB Substrate binding plasticity revealed by cryo-em structures of slc26a2 (see paper)
23% identity, 95% coverage: 29:545/545 of query aligns to 5:545/545 of 8tnyB
7xujA Human slc26a3 in complex with uk5099
23% identity, 79% coverage: 24:453/545 of query aligns to 60:505/703 of 7xujA
- binding (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid: V79 (= V42), Q83 (≠ L46), E271 (≠ S218), S376 (≠ A317), R377 (= R318), V380 (≠ T321), L421 (= L359), A422 (= A360), N425 (≠ V365)
- binding cholesterol hemisuccinate: F171 (≠ M119), V311 (≠ L250), Q315 (≠ R252)
7xuhA Down-regulated in adenoma in complex with tqr1122
23% identity, 79% coverage: 24:453/545 of query aligns to 60:509/707 of 7xuhA
- binding 2-[4,8-dimethyl-2-oxidanylidene-7-[[3-(trifluoromethyl)phenyl]methoxy]chromen-3-yl]ethanoic acid: P124 (≠ G87), I125 (≠ A88), L187 (≠ I131), I192 (≠ T136), F195 (= F139), V335 (= V263), S338 (≠ T266), S380 (≠ A317), M433 (≠ N369)
- binding cholesterol hemisuccinate: V223 (≠ S166), F226 (≠ V169), K227 (≠ E170), Y230 (≠ E173), F318 (vs. gap), Q319 (≠ R252)
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, 73% coverage: 39:434/545 of query aligns to 100:521/759 of Q9BXS9
- N167 (≠ I102) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- N172 (≠ L107) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- V206 (≠ Y127) to M: in dbSNP:rs13324142
Sites not aligning to the query:
- 547:549 DVD→NVN: Does not inhibit cell membrane localization. Inhibits interaction with CA2 and bicarbonate transport.
- 553 S→A: Does not inhibit interaction with CA2. Inhibits interaction with CA2 and bicarbonate transport in PMA-induced cells.
- 582 S→A: Does not inhibit interaction with CA2. Does not inhibit interaction with CA2 and bicarbonate transport in PMA-induced cells.
Q62273 Sulfate transporter; Diastrophic dysplasia protein homolog; ST-OB; Solute carrier family 26 member 2 from Mus musculus (Mouse) (see paper)
22% identity, 90% coverage: 27:519/545 of query aligns to 106:694/739 of Q62273
- F368 (≠ L242) mutation to A: Reduced sulfate-chloride exchange activity.
- E417 (= E293) mutation E->A,K: Loss of sulfate-chloride exchange activity.
Query Sequence
>WP_011841529.1 NCBI__GCF_000015985.1:WP_011841529.1
MRGTSLTFWDHFLPKIVTVFREGYGLRDLRADALAGLTVAIVALPLSTAIAIASGVGPER
GLYTAIVGGFLVSALGGSRFQIGGPAGAFIVLVAACVMQTGIEGLILATFLSGFLLIAMG
TLKLGSYIRFIPYPVTVGFTAGIAVIIAASQMKELLGLTLAGPEPSALVEKVEALWAARE
TITPAALGVAVGTIAMIEGLKRLSPRLPSLLIAIVLASVAVLVLKLPVETIGTRFGELPK
MLPTPALPALDREAILAALPWAVSFTLLGAIESLLSAVVADGMAGTQHRPNAELIAQGWA
NVGSALFGGFCVTGTIARTATNVRAGSRGPVSGMLHALFVLGFLLVAAPLAAYIPLAALA
GLLAVVAWNMFEKEEFWALLRTSRGDAMVVLATFLLVVFRDLTEGIVVGFALGGLVFIRR
MSDAASAEPAQVPEAGGAVTAERVVYRLRGPYFFGAAAMLGSALDRFAERPRAFVLDFAE
VPFIDSSGARSFELLAHKMHRRGGQLFLTGANLEVRRVLLAQGLREPLVRYAPDIAGADA
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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