SitesBLAST
Comparing 202654 FitnessBrowser__MR1:202654 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)
27% identity, 94% coverage: 25:575/588 of query aligns to 3:542/564 of Q55415
- T69 (= T91) binding ; mutation to A: Alters bicarbonate transport.
- D258 (≠ E300) binding ; mutation D->A,E: Alters bicarbonate transport.
- T262 (≠ C304) binding ; mutation to A: Alters bicarbonate transport.
- G300 (≠ A342) binding
- A301 (= A343) binding
- T302 (≠ I344) binding ; mutation to A: Alters bicarbonate transport.
- A471 (≠ V504) mutation to N: Alters bicarbonate transport.
- L476 (= L509) mutation to S: Alters bicarbonate transport.
- A486 (≠ G519) mutation to E: Alters bicarbonate transport.
- L490 (= L523) mutation to Q: Alters bicarbonate transport.
5da0A Structure of the the slc26 transporter slc26dg in complex with a nanobody (see paper)
25% identity, 88% coverage: 27:543/588 of query aligns to 1:457/467 of 5da0A
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
29% identity, 70% coverage: 25:436/588 of query aligns to 2:392/392 of 6ki1B
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
24% identity, 93% coverage: 28:572/588 of query aligns to 21:570/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (= L127), R127 (= R128), W130 (≠ R131)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (= L129), L131 (= L132), E409 (≠ V432), L413 (≠ S436), G417 (≠ I440), A421 (≠ L444)
- binding sulfate ion: A84 (= A92), S321 (≠ A343), F322 (≠ I344)
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
25% identity, 84% coverage: 37:531/588 of query aligns to 26:551/605 of 7v75A
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
25% identity, 84% coverage: 37:531/588 of query aligns to 26:543/597 of 7v74A
7xulA Human slc26a3 in complex with tenidap
26% identity, 77% coverage: 37:486/588 of query aligns to 62:516/690 of 7xulA
- binding 5-chloranyl-2-oxidanyl-3-thiophen-2-ylcarbonyl-indole-1-carboxamide: V72 (≠ I47), L75 (≠ P50), Q76 (≠ L51), E262 (≠ A225), S367 (≠ A345), L412 (= L390), N416 (≠ V394)
- binding cholesterol hemisuccinate: I157 (≠ M119), F162 (≠ M124), P209 (= P169), K214 (≠ A174), Y217 (≠ M177), V302 (≠ L267), Q306 (≠ P271), V309 (vs. gap), V450 (≠ I428)
7xujA Human slc26a3 in complex with uk5099
26% identity, 77% coverage: 37:486/588 of query aligns to 69:525/703 of 7xujA
- binding (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid: V79 (≠ I47), Q83 (≠ L51), E271 (≠ A225), S376 (≠ A345), R377 (= R346), V380 (≠ A349), L421 (= L390), A422 (≠ L391), N425 (≠ V394)
- binding cholesterol hemisuccinate: F171 (≠ M124), V311 (≠ L267), Q315 (≠ P271)
7xuhA Down-regulated in adenoma in complex with tqr1122
25% identity, 77% coverage: 37:486/588 of query aligns to 69:529/707 of 7xuhA
- binding 2-[4,8-dimethyl-2-oxidanylidene-7-[[3-(trifluoromethyl)phenyl]methoxy]chromen-3-yl]ethanoic acid: P124 (= P100), I125 (= I101), L187 (≠ I136), I192 (≠ T141), F195 (= F144), V335 (≠ A289), S338 (≠ A292), S380 (≠ A345), M433 (= M398)
- binding cholesterol hemisuccinate: V223 (≠ E170), F226 (= F173), K227 (≠ A174), Y230 (≠ M177), F318 (≠ G270), Q319 (≠ P271)
P40879 Chloride anion exchanger; Down-regulated in adenoma; Protein DRA; Solute carrier family 26 member 3 from Homo sapiens (Human) (see 3 papers)
26% identity, 77% coverage: 37:486/588 of query aligns to 76:547/764 of P40879
- N153 (≠ A93) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- N161 (≠ I101) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- N165 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- C307 (≠ T240) 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.
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, 68% coverage: 44:445/588 of query aligns to 102:504/758 of Q8CIW6
Sites not aligning to the query:
- 552 T→A: Does not inhibit formate transport in PMA-induced cells.
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, 68% coverage: 44:445/588 of query aligns to 100:503/759 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 (≠ L132) 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.
Q9URY8 Probable sulfate permease C869.05c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 61% coverage: 36:392/588 of query aligns to 123:480/840 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)
22% identity, 78% coverage: 29:489/588 of query aligns to 74:550/744 of Q9EPH0
- L104 (≠ A58) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- V149 (≠ Q103) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D154 (≠ A108) mutation to N: Shifts the voltage-sensitivity to more negative values.
- D155 (≠ G109) 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 (= R128) mutation to Q: Shifts the voltage-sensitivity to more negative values.
- A202 (≠ I133) 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 (≠ Q164) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (≠ E166) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
- R236 (≠ H167) 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 (= R206) mutation to Q: No effect; when associated with Q-283 and Q-285.
- K283 (= K208) mutation to Q: No effect; when associated with Q-218 and Q-285.
- K285 (≠ P210) mutation to Q: No effect; when associated with Q-281 and Q-283.
- P331 (= P271) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D332 (≠ N279) mutation to Q: No effect.
- D342 (≠ A289) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K359 (≠ V306) 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 (≠ G336) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S398 (≠ A345) 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 (= R346) 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 (≠ A355) 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 (≠ Q356) mutation to Q: No effect.
- L431 (≠ I378) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S465 (≠ L408) 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 (≠ I428) 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.
Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
21% identity, 78% coverage: 29:489/588 of query aligns to 74:550/744 of Q9JKQ2
- 158:168 (vs. 112:112, 9% identical) Involved in motor function
- S398 (≠ A345) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
- R399 (= R346) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
A0FKN5 Prestin; Solute carrier family 26 member 5 from Gallus gallus (Chicken) (see paper)
22% identity, 65% coverage: 28:411/588 of query aligns to 74:471/742 of A0FKN5
- S404 (≠ A345) 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 (= R346) mutation to C: Fully abolishes anion transport.
3ny7A Stas domain of ychm bound to acp (see paper)
39% identity, 16% coverage: 478:574/588 of query aligns to 22:117/118 of 3ny7A
7lguA Structure of human prestin in the presence of nacl (see paper)
20% identity, 78% coverage: 29:489/588 of query aligns to 62:538/680 of 7lguA
P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
21% identity, 78% coverage: 29:489/588 of query aligns to 74:550/744 of P58743
- F101 (≠ L55) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ A345) binding
D7PC76 Prestin; Solute carrier family 26 member 5 from Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) (see paper)
21% identity, 78% coverage: 29:489/588 of query aligns to 74:550/741 of D7PC76
- GG 274:275 (vs. gap) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
- S398 (≠ A345) binding
Query Sequence
>202654 FitnessBrowser__MR1:202654
MDPHVSHSAHLFSLRIAHALNEACVKDRYSFKRFGQDLLAGLTVGIIAIPLAMALAIASG
VPPQYGLYTAIVGGFIIAMTGGSRYSVSGPTAAFVVLLYPIAQQFGLAGLLIATVMSGMM
LVAMAMLRLGRLILYIPESVTLGFTAGIGVVIATLQLKDFFGLQIEHMPEQYFAKLMALG
QALPSLHLPSLFIAAATLATMLLWPRLKIPVPAHLPAIALGSILALILNAMGAEIETIGT
RFHYQLTDGGIGSGIPAVLPHFEWPWLQTGPNGQAFEFNLAAFQALLPAAFAIAMLGAIE
SLLCAVVLDGMTGKRHSANSELLGQGIGNIIAPFFGGIPATAAIARSAANVKAGAQSPIA
SMIHALVVLIGLVALAGILAYLPMSAMAALLLVVAWNMSEAPKAVHLLKTAPTSDILVFL
SCFSLTVIFDMVIAISVGIILAALLFMKEIAEMTKLYDISSNKRYVDQSLPADWAVLKIN
GPLFFAAADRIFAEIASLTQDKQVIVLYLDGVSILDAGGLAALSKLIEKCKLNQTKLLIT
DLQFQPIRTLAKAKIQPVEGVLKFYPTLREALTEAPSPELEATPEATD
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