SitesBLAST
Comparing WP_086510061.1 NCBI__GCF_002151265.1:WP_086510061.1 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)
5da0A Structure of the the slc26 transporter slc26dg in complex with a nanobody (see paper)
62% identity, 96% coverage: 6:479/496 of query aligns to 1:466/467 of 5da0A
Q55415 Bicarbonate transporter BicA from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
26% identity, 94% coverage: 5:468/496 of query aligns to 4:508/564 of Q55415
- T69 (= T70) binding ; mutation to A: Alters bicarbonate transport.
- D258 (≠ E236) binding ; mutation D->A,E: Alters bicarbonate transport.
- T262 (= T240) binding ; mutation to A: Alters bicarbonate transport.
- G300 (≠ A278) binding
- A301 (≠ M279) binding
- T302 (≠ I280) binding ; mutation to A: Alters bicarbonate transport.
- A471 (≠ K431) mutation to N: Alters bicarbonate transport.
- L476 (= L436) mutation to S: Alters bicarbonate transport.
- A486 (= A446) mutation to E: Alters bicarbonate transport.
- L490 (= L450) mutation to Q: Alters bicarbonate transport.
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
27% identity, 72% coverage: 5:362/496 of query aligns to 3:383/392 of 6ki1B
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
25% identity, 98% coverage: 8:492/496 of query aligns to 21:521/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (= L106), R127 (≠ K107), W130 (≠ E110)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (= L108), L131 (= L111), E409 (≠ F372), L413 (= L376), G417 (≠ M380), A421 (≠ L390)
- binding sulfate ion: A84 (≠ G71), S321 (≠ M279), F322 (≠ I280)
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
24% identity, 98% coverage: 7:493/496 of query aligns to 20:578/597 of 7v74A
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
24% identity, 98% coverage: 7:493/496 of query aligns to 20:586/605 of 7v75A
7xulA Human slc26a3 in complex with tenidap
22% identity, 61% coverage: 7:309/496 of query aligns to 56:395/690 of 7xulA
- binding 5-chloranyl-2-oxidanyl-3-thiophen-2-ylcarbonyl-indole-1-carboxamide: V72 (≠ A26), L75 (≠ P29), Q76 (≠ E30), E262 (≠ V175), S367 (≠ G281)
- binding cholesterol hemisuccinate: I157 (≠ V98), F162 (≠ A103), P209 (≠ T150), K214 (≠ A155), Y217 (= Y158), V302 (≠ L216), Q306 (≠ W220), V309 (≠ L223)
Sites not aligning to the query:
7xujA Human slc26a3 in complex with uk5099
23% identity, 61% coverage: 7:309/496 of query aligns to 63:404/703 of 7xujA
Sites not aligning to the query:
7xuhA Down-regulated in adenoma in complex with tqr1122
22% identity, 61% coverage: 7:309/496 of query aligns to 63:408/707 of 7xuhA
- binding 2-[4,8-dimethyl-2-oxidanylidene-7-[[3-(trifluoromethyl)phenyl]methoxy]chromen-3-yl]ethanoic acid: P124 (≠ G64), I125 (≠ M65), L187 (≠ V115), I192 (≠ V120), F195 (= F123), V335 (≠ E236), S338 (≠ M239), S380 (≠ G281)
- binding cholesterol hemisuccinate: V223 (= V151), F226 (≠ L154), K227 (≠ A155), Y230 (= Y158), F318 (≠ L219), Q319 (≠ W220)
Sites not aligning to the query:
D7PC76 Prestin; Solute carrier family 26 member 5 from Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) (see paper)
22% identity, 85% coverage: 15:434/496 of query aligns to 82:567/741 of D7PC76
- GG 274:275 (vs. gap) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
- S398 (≠ G281) binding
A0FKN5 Prestin; Solute carrier family 26 member 5 from Gallus gallus (Chicken) (see paper)
23% identity, 65% coverage: 15:336/496 of query aligns to 83:459/742 of A0FKN5
- S404 (≠ G281) 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 (≠ Q282) mutation to C: Fully abolishes anion transport.
7lguA Structure of human prestin in the presence of nacl (see paper)
24% identity, 65% coverage: 15:335/496 of query aligns to 70:440/680 of 7lguA
Sites not aligning to the query:
P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
24% identity, 65% coverage: 15:335/496 of query aligns to 82:452/744 of P58743
- F101 (= F34) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ G281) binding
Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
24% identity, 65% coverage: 15:335/496 of query aligns to 82:452/744 of Q9JKQ2
- 158:168 (vs. 79:79, 9% identical) Involved in motor function
- S398 (≠ G281) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
- R399 (≠ Q282) 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, 65% coverage: 15:335/496 of query aligns to 82:452/744 of Q9EPH0
- L104 (≠ I37) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- V149 (≠ L75) 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 (≠ L80) mutation to Q: No effect.
- K177 (≠ E87) mutation to Q: No effect.
- R197 (≠ K107) mutation to Q: Shifts the voltage-sensitivity to more negative values.
- A202 (≠ M112) 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 (≠ T143) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (≠ H145) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
- R236 (≠ V146) 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 (≠ P161) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values.
- R281 (= R165) mutation to Q: No effect; when associated with Q-283 and Q-285.
- K283 (≠ G167) mutation to Q: No effect; when associated with Q-218 and Q-285.
- K285 (≠ S169) mutation to Q: No effect; when associated with Q-281 and Q-283.
- P331 (≠ L216) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D332 (= D217) mutation to Q: No effect.
- D342 (vs. gap) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K359 (≠ T242) 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 (≠ G272) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S398 (≠ G281) 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 (≠ Q282) 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 (= G291) 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 (≠ R292) mutation to Q: No effect.
- L431 (≠ W314) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
Sites not aligning to the query:
- 465 S→C: Is only accessible to the intracellular side application of thiol-reactive reagents. Is not affected by thiol-reactive reagents extracellular side application.
- 485 D→C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- 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.
P40879 Chloride anion exchanger; Down-regulated in adenoma; Protein DRA; Solute carrier family 26 member 3 from Homo sapiens (Human) (see 3 papers)
21% identity, 61% coverage: 7:309/496 of query aligns to 70:426/764 of P40879
- N153 (≠ A74) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- N161 (≠ R82) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- N165 (≠ L86) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- C307 (≠ M189) 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.
Q96RN1 Testis anion transporter 1; Anion exchange transporter; Solute carrier family 26 member 8 from Homo sapiens (Human) (see 4 papers)
22% identity, 63% coverage: 15:328/496 of query aligns to 94:463/970 of Q96RN1
- I148 (≠ S67) to V: not a cause of male infertility; dbSNP:rs17713154
- S230 (≠ T121) to N: not a cause of male infertility; dbSNP:rs17707331
Sites not aligning to the query:
- 73 V → M: not a cause of male infertility; dbSNP:rs743923
- 87 R → Q: in SPGF3; there is a reduced interactions with CFTR and complete failure to activate CFTR-dependent anion transport; dbSNP:rs140210148
- 639 I → V: not a cause of male infertility; dbSNP:rs2295852
- 664:970 Interaction with RACGAP1
- 812 E → K: in SPGF3; there is a reduced interactions with CFTR and complete failure to activate CFTR-dependent anion transport; dbSNP:rs142724470
- 914 P→S: Not a cause of male infertility.
- 954 R → C: in SPGF3; there is a reduced interactions with CFTR and complete failure to activate CFTR-dependent anion transport; dbSNP:rs398123027
Q9BXS9 Solute carrier family 26 member 6; Anion exchange transporter; Pendrin-like protein 1; Pendrin-L1 from Homo sapiens (Human) (see 3 papers)
21% identity, 82% coverage: 23:430/496 of query aligns to 100:568/759 of Q9BXS9
- N167 (vs. gap) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- N172 (vs. gap) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- V206 (≠ L111) to M: in dbSNP:rs13324142
- ATV 547:549 (≠ GQV 409:411) mutation to NVN: Does not inhibit cell membrane localization. Inhibits interaction with CA2 and bicarbonate transport.
- N553 (≠ S415) 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.
8sieC Pendrin in complex with bicarbonate (see paper)
22% identity, 66% coverage: 7:335/496 of query aligns to 41:411/613 of 8sieC
- binding Lauryl Maltose Neopentyl Glycol: G198 (≠ A152), S296 (≠ W220), T300 (≠ P224), F303 (≠ V227)
- binding bicarbonate ion: Y65 (≠ F34), F101 (≠ G71), L356 (≠ I280), S357 (≠ G281), V403 (≠ M327), N406 (≠ V330)
- binding cholesterol: L226 (vs. gap), V255 (= V178), I262 (≠ L185), Y272 (≠ G195), F411 (= F335)
Sites not aligning to the query:
- binding cholesterol: 414, 414, 415, 415, 436, 452, 453
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: 421, 429, 432, 433, 436
8shcC Pendrin in complex with niflumic acid (see paper)
22% identity, 66% coverage: 7:335/496 of query aligns to 41:411/613 of 8shcC
- binding cholesterol: I199 (≠ G153), A223 (vs. gap), V255 (= V178), Y272 (≠ G195)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: Q156 (≠ K107)
- binding 2-{[3-(trifluoromethyl)phenyl]amino}nicotinic acid: Y65 (≠ F34), F101 (≠ G71), T173 (≠ V124), E252 (≠ V175), I312 (≠ E236), L356 (≠ I280), S357 (≠ G281), V402 (= V326), N406 (≠ V330)
Sites not aligning to the query:
Query Sequence
>WP_086510061.1 NCBI__GCF_002151265.1:WP_086510061.1
MFRSTKQEWFSNIKGDTLAGIVVALALIPEAIAFSIIAGVDPKVGLYASFCIAVIIAFTG
GRPGMISAATGAMALLMVTLVRDHGLEYLLAATLLTGVLQIVAGYLKLAELMRFVSRSVV
TGFVNALAILIFMAQLPELTGVTWHVYAMTVAGLAIIYLFPYLPRVGKSIPSPLVCIVVL
TAVYLLSGMEIRTVGDMGELPDTLPVFLWPDVPLTLDTLWIILPYSVMLAVVGLLESMMT
ATIVDDLTDTPSDKNRECKGQGIANIGSGLLGGMAGCAMIGQSVINVKSGGRGRLSTLVA
GVLLLILVVFLSDWVSLIPMAALVAVMIMVSIGTFSWASIRDLKKHPLSTNVVMLTTVAV
TVGTHNLAIGVFVGVLLAAMFFANKVGNILYIGSEEADAGSRRIYHVVGQVFFASSERFG
SAFDFKETVEKVTIDLSRAHFWDITAVQALDRVVIKFRREGTEVELIGLNEASATIVDRH
AIHDDPAAVEKLMGGH
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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