SitesBLAST
Comparing H281DRAFT_01715 H281DRAFT_01715 sulfate permease, SulP family 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)
40% identity, 95% coverage: 18:541/553 of query aligns to 13:540/564 of Q55415
- T69 (= T74) binding ; mutation to A: Alters bicarbonate transport.
- D258 (= D260) binding ; mutation D->A,E: Alters bicarbonate transport.
- T262 (= T264) binding ; mutation to A: Alters bicarbonate transport.
- G300 (= G302) binding
- A301 (= A303) binding
- T302 (= T304) binding ; mutation to A: Alters bicarbonate transport.
- A471 (vs. gap) mutation to N: Alters bicarbonate transport.
- L476 (≠ M476) mutation to S: Alters bicarbonate transport.
- A486 (≠ G486) mutation to E: Alters bicarbonate transport.
- L490 (= L490) mutation to Q: Alters bicarbonate transport.
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
47% identity, 68% coverage: 18:394/553 of query aligns to 12:391/392 of 6ki1B
5da0A Structure of the the slc26 transporter slc26dg in complex with a nanobody (see paper)
31% identity, 91% coverage: 18:520/553 of query aligns to 9:467/467 of 5da0A
Sites not aligning to the query:
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
25% identity, 86% coverage: 20:492/553 of query aligns to 29:523/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (= L117), R127 (= R118), W130 (≠ S121)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (≠ I119), L131 (≠ Y122), E409 (≠ I391), L413 (≠ A395), G417 (≠ V400), A421 (≠ V404)
- binding sulfate ion: A84 (≠ G75), S321 (≠ A303), F322 (≠ T304)
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
27% identity, 91% coverage: 19:519/553 of query aligns to 25:564/597 of 7v74A
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
26% identity, 91% coverage: 19:519/553 of query aligns to 25:572/605 of 7v75A
7xulA Human slc26a3 in complex with tenidap
25% identity, 67% coverage: 19:388/553 of query aligns to 61:448/690 of 7xulA
- binding 5-chloranyl-2-oxidanyl-3-thiophen-2-ylcarbonyl-indole-1-carboxamide: V72 (= V30), L75 (≠ P33), Q76 (≠ L34), E262 (≠ L206), S367 (≠ M305), L412 (= L350), N416 (≠ V354)
- binding cholesterol hemisuccinate: I157 (≠ F109), F162 (= F114), P209 (= P160), K214 (≠ S165), Y217 (≠ H168), V302 (≠ L240), Q306 (≠ P244), V309 (= V247)
Sites not aligning to the query:
7xuhA Down-regulated in adenoma in complex with tqr1122
25% identity, 67% coverage: 19:388/553 of query aligns to 68:461/707 of 7xuhA
- binding 2-[4,8-dimethyl-2-oxidanylidene-7-[[3-(trifluoromethyl)phenyl]methoxy]chromen-3-yl]ethanoic acid: P124 (≠ G75), I125 (≠ P76), L187 (≠ V126), I192 (= I131), F195 (= F134), V335 (≠ D260), S338 (≠ L263), S380 (≠ M305), M433 (≠ I358)
- binding cholesterol hemisuccinate: V223 (≠ W161), F226 (≠ L164), K227 (≠ S165), Y230 (≠ H168), F318 (≠ L243), Q319 (≠ P244)
7xujA Human slc26a3 in complex with uk5099
25% identity, 67% coverage: 19:388/553 of query aligns to 68:457/703 of 7xujA
- binding (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid: V79 (= V30), Q83 (≠ L34), E271 (≠ L206), S376 (≠ M305), R377 (= R306), V380 (= V309), L421 (= L350), A422 (≠ L351), N425 (≠ V354)
- binding cholesterol hemisuccinate: F171 (= F114), V311 (≠ L240), Q315 (≠ P244)
P40879 Chloride anion exchanger; Down-regulated in adenoma; Protein DRA; Solute carrier family 26 member 3 from Homo sapiens (Human) (see 3 papers)
25% identity, 67% coverage: 19:388/553 of query aligns to 75:479/764 of P40879
- N153 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- N161 (≠ M89) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- N165 (≠ G93) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- C307 (vs. gap) 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.
Q9BXS9 Solute carrier family 26 member 6; Anion exchange transporter; Pendrin-like protein 1; Pendrin-L1 from Homo sapiens (Human) (see 3 papers)
25% identity, 68% coverage: 28:401/553 of query aligns to 101:496/759 of Q9BXS9
- N167 (vs. gap) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- N172 (= N88) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- V206 (≠ Y122) 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.
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)
24% identity, 68% coverage: 28:401/553 of query aligns to 103:501/758 of Q8CIW6
Sites not aligning to the query:
- 552 T→A: Does not inhibit formate transport in PMA-induced cells.
A0FKN5 Prestin; Solute carrier family 26 member 5 from Gallus gallus (Chicken) (see paper)
24% identity, 60% coverage: 19:352/553 of query aligns to 83:451/742 of A0FKN5
- S404 (≠ M305) 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 (= R306) mutation to C: Fully abolishes anion transport.
D7PC76 Prestin; Solute carrier family 26 member 5 from Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) (see paper)
25% identity, 69% coverage: 19:401/553 of query aligns to 82:491/741 of D7PC76
- GG 274:275 (vs. gap) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
- S398 (≠ M305) binding
Q62273 Sulfate transporter; Diastrophic dysplasia protein homolog; ST-OB; Solute carrier family 26 member 2 from Mus musculus (Mouse) (see paper)
21% identity, 91% coverage: 19:519/553 of query aligns to 110:696/739 of Q62273
- F368 (≠ T234) mutation to A: Reduced sulfate-chloride exchange activity.
- E417 (= E281) mutation E->A,K: Loss of sulfate-chloride exchange activity.
Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
21% identity, 83% coverage: 19:478/553 of query aligns to 82:572/744 of Q9JKQ2
- 158:168 (vs. 86:89, 18% identical) Involved in motor function
- S398 (≠ M305) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
- R399 (= R306) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
Q9EPH0 Prestin; Solute carrier family 26 member 5 from Rattus norvegicus (Rat) (see 3 papers)
24% identity, 69% coverage: 19:401/553 of query aligns to 82:491/744 of Q9EPH0
- L104 (≠ A41) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- V149 (vs. gap) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D154 (vs. gap) mutation to N: Shifts the voltage-sensitivity to more negative values.
- D155 (vs. gap) mutation to N: Shifts the voltage-sensitivity to more negative values.
- E169 (≠ H90) mutation to Q: No effect.
- K177 (≠ P98) mutation to Q: No effect.
- R197 (= R118) mutation to Q: Shifts the voltage-sensitivity to more negative values.
- A202 (≠ I123) 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 (≠ N154) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (≠ P156) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
- R236 (≠ G157) 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 (≠ P193) 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 (≠ R194) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values.
- R281 (≠ V198) mutation to Q: No effect; when associated with Q-283 and Q-285.
- K283 (≠ P200) mutation to Q: No effect; when associated with Q-218 and Q-285.
- K285 (≠ S202) mutation to Q: No effect; when associated with Q-281 and Q-283.
- P331 (= P236) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D332 (≠ A237) mutation to Q: No effect.
- D342 (≠ A249) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K359 (≠ L266) 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 (≠ G296) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S398 (≠ M305) 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 (= R306) 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 (= G315) 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 (≠ R316) mutation to Q: No effect.
- L431 (= L338) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S465 (≠ D374) 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 (≠ A395) 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.
P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
22% identity, 81% coverage: 19:466/553 of query aligns to 82:560/744 of P58743
- F101 (= F38) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ M305) binding
7lguA Structure of human prestin in the presence of nacl (see paper)
22% identity, 81% coverage: 19:466/553 of query aligns to 70:548/680 of 7lguA
P58735 Sulfate anion transporter 1; SAT-1; Solute carrier family 26 member 1 from Mus musculus (Mouse) (see paper)
23% identity, 80% coverage: 19:459/553 of query aligns to 71:560/704 of P58735
- T190 (≠ F104) mutation to M: Decreased sulfate-hydrogencarbonate exchange activity. Loss of localization to plasma membrane.
- S363 (≠ L266) 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.
Query Sequence
>H281DRAFT_01715 H281DRAFT_01715 sulfate permease, SulP family
MREMLEPQSTKSSPMIGRGDIFGGVAAGVVALPLALAFGVASGLGPVAGLYGAIVTGIVA
ALFGGTPVQITGPTGPMTLVVAGVLAANMHSSGSANLPLVVGIFVVAGFMQIAFGLLRIG
SYIRYVPYPVISGFMSGIGVIIITQQVFPMFGANAPGSDPWSILSQLHLLGGNIKWSAVA
LSASTIAIALLLPRFTKVIPASLVALIVLTITAVMLKLDVPVIGEIPSGLPTLTMPAFDL
HRLPSLVPAALQLSLLGAIDSLLTALVADNLTRTRHDSNRELIGQGLGNIAAAVIGGLPG
AGATMRTVVNVDAGGRTRLSGVIHGLFLAAVLLGLSGLLQHVPRAILAGLLVTVGIGIID
RRSFRHLLKLSRSDAFLMLLVLALTVFTDLIIAVATGLVVASFVFVKKVGDITEQRTMLT
PVADEPWADELTIPAGLRDRLLIKHVDGPIFFGFASKFLDIARQATLLSRLLVLRMDRIS
YMDQTGVYALDDALVRLNAAGVRVLVVGVSVSQRDLLERLQVIPAVVPERDIFNNFDELR
KALPVIIGDLHAK
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