SitesBLAST
Comparing Ac3H11_3820 FitnessBrowser__acidovorax_3H11:Ac3H11_3820 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)
30% identity, 93% coverage: 26:538/553 of query aligns to 15:519/564 of Q55415
- T69 (≠ A80) binding ; mutation to A: Alters bicarbonate transport.
- D258 (≠ E283) binding ; mutation D->A,E: Alters bicarbonate transport.
- T262 (≠ C287) binding ; mutation to A: Alters bicarbonate transport.
- G300 (= G329) binding
- A301 (≠ T330) binding
- T302 (≠ I331) binding ; mutation to A: Alters bicarbonate transport.
- A471 (= A484) mutation to N: Alters bicarbonate transport.
- L476 (≠ A495) mutation to S: Alters bicarbonate transport.
- A486 (≠ G505) mutation to E: Alters bicarbonate transport.
- L490 (= L509) mutation to Q: Alters bicarbonate transport.
5da0A Structure of the the slc26 transporter slc26dg in complex with a nanobody (see paper)
28% identity, 94% coverage: 20:538/553 of query aligns to 1:466/467 of 5da0A
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
32% identity, 72% coverage: 26:421/553 of query aligns to 14:391/392 of 6ki1B
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
25% identity, 95% coverage: 15:540/553 of query aligns to 17:552/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (≠ F116), R127 (= R117), W130 (≠ T120)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (= L118), L131 (= L121), E409 (≠ T418), L413 (≠ E422), G417 (≠ F426), A421 (= A430)
- binding sulfate ion: A84 (≠ G81), S321 (≠ T330), F322 (≠ I331)
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
28% identity, 97% coverage: 3:541/553 of query aligns to 3:575/605 of 7v75A
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
28% identity, 97% coverage: 3:541/553 of query aligns to 3:567/597 of 7v74A
A0FKN5 Prestin; Solute carrier family 26 member 5 from Gallus gallus (Chicken) (see paper)
23% identity, 77% coverage: 20:444/553 of query aligns to 78:511/742 of A0FKN5
- S404 (≠ A332) 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 (= R333) mutation to C: Fully abolishes anion transport.
Q9URY8 Probable sulfate permease C869.05c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
24% identity, 76% coverage: 11:428/553 of query aligns to 109:526/840 of Q9URY8
Sites not aligning to the query:
- 823 modified: Phosphoserine
P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
23% identity, 77% coverage: 20:443/553 of query aligns to 77:504/744 of P58743
- F101 (= F44) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ A332) binding
7lguA Structure of human prestin in the presence of nacl (see paper)
23% identity, 77% coverage: 20:443/553 of query aligns to 65:492/680 of 7lguA
D7PC76 Prestin; Solute carrier family 26 member 5 from Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) (see paper)
23% identity, 77% coverage: 20:443/553 of query aligns to 77:504/741 of D7PC76
- GG 274:275 (≠ WP 193:194) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
- S398 (≠ A332) binding
Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
23% identity, 78% coverage: 20:449/553 of query aligns to 77:518/744 of Q9JKQ2
- 158:168 (vs. 101:102, 9% identical) Involved in motor function
- S398 (≠ A332) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
- R399 (= R333) 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)
22% identity, 77% coverage: 20:443/553 of query aligns to 77:504/744 of Q9EPH0
- L104 (≠ A47) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- V149 (≠ E92) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D154 (≠ A97) mutation to N: Shifts the voltage-sensitivity to more negative values.
- D155 (≠ N98) 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 (= R117) mutation to Q: Shifts the voltage-sensitivity to more negative values.
- A202 (≠ V122) 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 (≠ S153) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (≠ E155) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
- R236 (= R156) 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 (= K195) 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 (≠ Q209) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values.
- R281 (= R213) mutation to Q: No effect; when associated with Q-283 and Q-285.
- K283 (≠ F215) mutation to Q: No effect; when associated with Q-218 and Q-285.
- K285 (≠ R217) mutation to Q: No effect; when associated with Q-281 and Q-283.
- P331 (= P259) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D332 (= D260) mutation to Q: No effect.
- D342 (≠ P272) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K359 (≠ R289) 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 (≠ G323) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S398 (≠ A332) 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 (= R333) 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 (≠ A342) 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 (≠ T343) mutation to Q: No effect.
- L431 (= L365) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S465 (≠ Y401) 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 (≠ E422) 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.
8sieC Pendrin in complex with bicarbonate
25% identity, 67% coverage: 11:379/553 of query aligns to 31:404/613 of 8sieC
- binding Lauryl Maltose Neopentyl Glycol: G198 (= G159), S296 (≠ T271), T300 (= T275), F303 (≠ L278)
- binding bicarbonate ion: Y65 (≠ F44), F101 (vs. gap), L356 (≠ I331), S357 (≠ A332), V403 (≠ L378)
- binding cholesterol: L226 (= L196), V255 (≠ L228), I262 (≠ L235), Y272 (≠ R245)
Sites not aligning to the query:
- binding bicarbonate ion: 406
- binding cholesterol: 411, 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
25% identity, 67% coverage: 11:379/553 of query aligns to 31:404/613 of 8shcC
- binding cholesterol: I199 (≠ F161), A223 (= A188), V255 (≠ L228), Y272 (≠ R245)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: Q156 (≠ R117)
- binding 2-{[3-(trifluoromethyl)phenyl]amino}nicotinic acid: Y65 (≠ F44), F101 (vs. gap), T173 (= T134), E252 (≠ L225), I312 (≠ C287), L356 (≠ I331), S357 (≠ A332), V402 (≠ I377)
Sites not aligning to the query:
8sgwC Pendrin in complex with chloride
25% identity, 67% coverage: 11:379/553 of query aligns to 31:404/613 of 8sgwC
- binding Lauryl Maltose Neopentyl Glycol: G198 (= G159), S296 (≠ T271), T300 (= T275), F303 (≠ L278)
- binding cholesterol: I228 (≠ M198), V255 (≠ L228), I262 (≠ L235), Y272 (≠ R245)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: F159 (≠ T120), Y163 (≠ F124), F284 (≠ A257), P286 (= P259), I289 (≠ T265), F343 (≠ V318), F346 (= F321)
Sites not aligning to the query:
- binding cholesterol: 408, 411, 412, 412, 414, 415, 417, 439
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: 421, 433, 436, 455, 464, 465
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, 73% coverage: 33:437/553 of query aligns to 102:510/758 of Q8CIW6
Sites not aligning to the query:
- 552 T→A: Does not inhibit formate transport in PMA-induced cells.
7xulA Human slc26a3 in complex with tenidap
24% identity, 78% coverage: 15:443/553 of query aligns to 50:473/690 of 7xulA
- binding 5-chloranyl-2-oxidanyl-3-thiophen-2-ylcarbonyl-indole-1-carboxamide: V72 (= V36), L75 (≠ P39), Q76 (≠ L40), E262 (≠ L225), S367 (≠ A332), L412 (≠ I377), N416 (≠ F380)
- binding cholesterol hemisuccinate: I157 (≠ V108), F162 (≠ L113), P209 (= P158), K214 (≠ S163), Y217 (≠ G166), V302 (≠ F261), Q306 (≠ R267), V309 (= V270), V450 (= V414)
7xujA Human slc26a3 in complex with uk5099
24% identity, 78% coverage: 15:443/553 of query aligns to 57:482/703 of 7xujA
- binding (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid: V79 (= V36), Q83 (≠ L40), E271 (≠ L225), S376 (≠ A332), R377 (= R333), V380 (≠ T336), L421 (≠ I377), A422 (≠ L378), N425 (≠ V381)
- binding cholesterol hemisuccinate: F171 (≠ L113), V311 (≠ F261), Q315 (≠ R267)
Q62273 Sulfate transporter; Diastrophic dysplasia protein homolog; ST-OB; Solute carrier family 26 member 2 from Mus musculus (Mouse) (see paper)
24% identity, 77% coverage: 4:427/553 of query aligns to 89:533/739 of Q62273
- F368 (≠ L253) mutation to A: Reduced sulfate-chloride exchange activity.
- E417 (= E308) mutation E->A,K: Loss of sulfate-chloride exchange activity.
Query Sequence
>Ac3H11_3820 FitnessBrowser__acidovorax_3H11:Ac3H11_3820
MPLSFAFHPRLIDALRGYDKSRWLADVGAGVTVGIVALPLAMAFAIASGLKPEAGLWTAI
IAGFLISALGGTNVQIGGPAGAFIVIVYGIVERYGVANLLISTACAGVLLVLLGLFRLGT
LVRFVPVSIVIGFTNGIAVLIALSQVKDWLGLSIERMPGNFFSQVGTLAQHLGSFNPYAF
GLGAACVAGLFLWPKLTMKESPVMRVLEQHTVRSFARVPAPVVALVTLSLLAWALQLPVE
TIGSRFGGIPQALPVFALPDFSWETVRLLVTPTLTIALLGAIESLLCARVADQLATDPHH
KKHDPNQELVAQGLANIVVPFFGGMPATGTIARTVTNIRSGATSPVAGMMHALTLAVIVL
VAAPLALHIPLAVLAGILLFVAWNMGEWHEFVRLKHFSNHYRLLMLGTFFLTVVFDLTVA
VEVGLFMACALFVRRMSALFRVERQPDPEAATAPRHPAATWRLHGALFFGAAAKLDTIIQ
AVEAGPPGLDVVLDASELVALDTTGLDALAQVLKAVAARGGRLRIEHLHEQPRSLIERSG
FAARLAAQHDLPV
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