SitesBLAST
Comparing GFF1051 FitnessBrowser__Marino:GFF1051 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)
64% identity, 96% coverage: 6:479/495 of query aligns to 1:466/467 of 5da0A
Q55415 Bicarbonate transporter BicA from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
26% identity, 95% coverage: 12:482/495 of query aligns to 11:522/564 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 (≠ N431) 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)
28% identity, 71% coverage: 12:362/495 of query aligns to 10:381/392 of 6ki1B
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
25% identity, 93% coverage: 8:469/495 of query aligns to 21:502/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (= L106), R127 (≠ K107), W130 (≠ S110)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (= L108), L131 (= L111), E409 (≠ L372), L413 (= L376), G417 (≠ L380), A421 (≠ N384)
- binding sulfate ion: A84 (= A71), S321 (≠ M279), F322 (≠ I280)
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
26% identity, 97% coverage: 6:484/495 of query aligns to 16:569/597 of 7v74A
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
26% identity, 97% coverage: 6:484/495 of query aligns to 16:577/605 of 7v75A
D7PC76 Prestin; Solute carrier family 26 member 5 from Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) (see paper)
22% identity, 95% coverage: 8:478/495 of query aligns to 69:594/741 of D7PC76
- GG 274:275 (≠ VG 166:167) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
- S398 (≠ G281) binding
P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
23% identity, 96% coverage: 15:488/495 of query aligns to 82:604/744 of P58743
- F101 (= F34) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ G281) binding
7lguA Structure of human prestin in the presence of nacl (see paper)
21% identity, 95% coverage: 15:483/495 of query aligns to 70:613/680 of 7lguA
7xulA Human slc26a3 in complex with tenidap
23% identity, 65% coverage: 7:326/495 of query aligns to 47:412/690 of 7xulA
- binding 5-chloranyl-2-oxidanyl-3-thiophen-2-ylcarbonyl-indole-1-carboxamide: V72 (≠ A26), L75 (≠ P29), Q76 (≠ E30), E262 (≠ V175), S367 (≠ G281), L412 (≠ V326)
- binding cholesterol hemisuccinate: I157 (≠ V98), F162 (≠ A103), P209 (≠ T150), K214 (≠ G155), Y217 (= Y158), V302 (≠ L216), Q306 (≠ M220), V309 (≠ L223)
Sites not aligning to the query:
Q9EPH0 Prestin; Solute carrier family 26 member 5 from Rattus norvegicus (Rat) (see 3 papers)
22% identity, 94% coverage: 15:478/495 of query aligns to 82:594/744 of Q9EPH0
- L104 (≠ I37) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- V149 (= V75) 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 (vs. gap) mutation to Q: No effect.
- K177 (≠ Q87) 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 (= K168) 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 (≠ V169) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values.
- R281 (vs. gap) mutation to Q: No effect; when associated with Q-283 and Q-285.
- K283 (vs. gap) mutation to Q: No effect; when associated with Q-218 and Q-285.
- K285 (vs. gap) 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 (≠ E217) 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 (≠ V314) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S465 (≠ L348) 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 (≠ A368) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- K557 (≠ D424) mutation to Q: No effect; when associated with Q-558 and Q-559.
- R558 (≠ F425) mutation to Q: No effect; when associated with Q-557 and Q-559.
- K559 (= K426) mutation to Q: No effect; when associated with Q-557 and Q-558.
- R571 (≠ L450) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-572 and Q-577.
- R572 (≠ D451) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-571 and Q-577.
- K577 (= K456) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values; when associated with Q-571 and Q-572.
Sites not aligning to the query:
- 505:718 Extended region for STAS domain
Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
23% identity, 96% coverage: 15:490/495 of query aligns to 82:611/744 of Q9JKQ2
- 158:168 (vs. 82:86, 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.
7xujA Human slc26a3 in complex with uk5099
23% identity, 65% coverage: 7:326/495 of query aligns to 54:421/703 of 7xujA
Sites not aligning to the query:
7xuhA Down-regulated in adenoma in complex with tqr1122
22% identity, 65% coverage: 7:326/495 of query aligns to 54:425/707 of 7xuhA
- binding 2-[4,8-dimethyl-2-oxidanylidene-7-[[3-(trifluoromethyl)phenyl]methoxy]chromen-3-yl]ethanoic acid: P124 (≠ A72), I125 (≠ M73), L187 (≠ V115), I192 (≠ V120), F195 (= F123), V335 (≠ E236), S338 (≠ M239), S380 (≠ G281)
- binding cholesterol hemisuccinate: V223 (≠ A151), F226 (≠ L154), K227 (≠ G155), Y230 (= Y158), F318 (≠ L219), Q319 (≠ M220)
Sites not aligning to the query:
A0FKN5 Prestin; Solute carrier family 26 member 5 from Gallus gallus (Chicken) (see paper)
22% identity, 86% coverage: 15:438/495 of query aligns to 83:577/742 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.
P40879 Chloride anion exchanger; Down-regulated in adenoma; Protein DRA; Solute carrier family 26 member 3 from Homo sapiens (Human) (see 3 papers)
22% identity, 65% coverage: 7:326/495 of query aligns to 61:443/764 of P40879
- N153 (≠ A74) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- N161 (≠ K82) 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.
Q9BXS9 Solute carrier family 26 member 6; Anion exchange transporter; Pendrin-like protein 1; Pendrin-L1 from Homo sapiens (Human) (see 3 papers)
22% identity, 82% coverage: 23:430/495 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
23% identity, 66% coverage: 8:335/495 of query aligns to 33:411/613 of 8sieC
- binding Lauryl Maltose Neopentyl Glycol: G198 (≠ A152), S296 (≠ T218), T300 (≠ I222), F303 (≠ Y225)
- binding bicarbonate ion: Y65 (≠ F34), F101 (≠ A71), L356 (≠ I280), S357 (≠ G281), V403 (≠ M327), N406 (≠ V330)
- binding cholesterol: L226 (vs. gap), V255 (= V178), I262 (≠ V185), 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
23% identity, 66% coverage: 8:335/495 of query aligns to 33:411/613 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 (≠ A71), T173 (≠ V124), E252 (≠ V175), I312 (≠ E236), L356 (≠ I280), S357 (≠ G281), V402 (= V326), N406 (≠ V330)
Sites not aligning to the query:
8sgwC Pendrin in complex with chloride
23% identity, 66% coverage: 8:335/495 of query aligns to 33:411/613 of 8sgwC
- binding Lauryl Maltose Neopentyl Glycol: G198 (≠ A152), S296 (≠ T218), T300 (≠ I222), F303 (≠ Y225)
- binding cholesterol: I228 (vs. gap), V255 (= V178), I262 (≠ V185), Y272 (≠ G195), K408 (≠ I332), F411 (= F335)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: F159 (≠ S110), Y163 (≠ F114), F284 (= F207), P286 (≠ W209), I289 (≠ V212), F343 (≠ G267), F346 (≠ L270)
Sites not aligning to the query:
- binding cholesterol: 412, 412, 414, 415, 417, 439
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: 421, 433, 436, 455, 464, 465
Query Sequence
>GFF1051 FitnessBrowser__Marino:GFF1051
MVNSLKANWLSNIRGDVLAGIVVALALIPEAIAFSIIAGVDPKVGLYASFCIAVIIAFVG
GRPGMISAATAAMAVLMVTLVKEHGLQYLLAATLMTGVLQLIAGYLKLGSLMRFVSRSVV
TGFVNALAILIFMAQLPELTNVTWHVYAMTAAGLGIIYLFPLLPVVGKVLPSPLVCIVVL
TAVAVVTGMDIRTVGDMGDLPDTLPVFLWPDVPLNLETLMIILPYSIPLAIVGLLESMMT
ATIVDDLTDTTSDRNRECKGQGIANIGSGLIGGMAGCAMIGQSIINVKSGGRTRLSTLTA
GLFLLVMVLLLDSVLVQIPMAALVAVMIMVSIGTFSWDSIRNLREHPLSTNIVMLVTVIV
VVATHNLAFGVLAGVLLAALFFANKVGHYMLVTSELDETTDTRTYRVVGQVFFSSSEKFM
ESFDFKEAVDNVVIDLSRAHFWDITAVGALDKAVIKFRREGSEVEVIGLNEASATIVDRF
GVHDKPDAVDQLMGH
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