SitesBLAST
Comparing WP_035628996.1 NCBI__GCF_000711315.1:WP_035628996.1 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)
Q55415 Bicarbonate transporter BicA from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
29% identity, 95% coverage: 17:565/575 of query aligns to 7:542/564 of Q55415
- T69 (= T79) binding hydrogencarbonate; mutation to A: Alters bicarbonate transport.
- D258 (≠ E289) binding Na(+); mutation D->A,E: Alters bicarbonate transport.
- T262 (≠ C293) binding Na(+); mutation to A: Alters bicarbonate transport.
- G300 (≠ A331) binding Na(+)
- A301 (= A332) binding hydrogencarbonate
- T302 (≠ I333) binding Na(+); mutation to A: Alters bicarbonate transport.
- A471 (≠ V494) mutation to N: Alters bicarbonate transport.
- L476 (≠ M499) mutation to S: Alters bicarbonate transport.
- A486 (= A509) mutation to E: Alters bicarbonate transport.
- L490 (= L513) mutation to Q: Alters bicarbonate transport.
5da0A Structure of the the slc26 transporter slc26dg in complex with a nanobody (see paper)
28% identity, 89% coverage: 23:533/575 of query aligns to 9:457/467 of 5da0A
Sites not aligning to the query:
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
31% identity, 71% coverage: 17:425/575 of query aligns to 6:392/392 of 6ki1B
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
24% identity, 98% coverage: 2:565/575 of query aligns to 3:573/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (≠ T115), R127 (≠ N116), W130 (≠ R119)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (≠ M117), L131 (= L120), E409 (≠ V421), L413 (≠ S425), G417 (= G429), A421 (≠ L433)
- binding sulfate ion: A84 (= A80), S321 (≠ A332), F322 (≠ I333)
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
25% identity, 95% coverage: 1:544/575 of query aligns to 3:566/597 of 7v74A
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
25% identity, 95% coverage: 1:544/575 of query aligns to 3:574/605 of 7v75A
Q9URY8 Probable sulfate permease C869.05c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 66% coverage: 5:381/575 of query aligns to 112:480/840 of Q9URY8
Sites not aligning to the query:
- 823 modified: Phosphoserine
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, 80% coverage: 32:491/575 of query aligns to 100:570/759 of Q9BXS9
- N167 (≠ G96) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- N172 (≠ S101) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- V206 (≠ L120) to M: in dbSNP:rs13324142
- ATV 547:549 (≠ GPL 471:473) mutation to NVN: Does not inhibit cell membrane localization. Inhibits interaction with CA2 and bicarbonate transport.
- N553 (≠ S477) 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.
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)
22% identity, 78% coverage: 32:479/575 of query aligns to 102:556/758 of Q8CIW6
- F552 (= F475) mutation to A: Does not inhibit formate transport in PMA-induced cells.
Q62273 Sulfate transporter; Diastrophic dysplasia protein homolog; ST-OB; Solute carrier family 26 member 2 from Mus musculus (Mouse) (see paper)
22% identity, 98% coverage: 4:568/575 of query aligns to 91:722/739 of Q62273
- F368 (≠ S252) mutation to A: Reduced sulfate-chloride exchange activity.
- E417 (= E310) mutation E->A,K: Loss of sulfate-chloride exchange activity.
8sieC Pendrin in complex with bicarbonate (see paper)
22% identity, 97% coverage: 4:562/575 of query aligns to 33:607/613 of 8sieC
- binding Lauryl Maltose Neopentyl Glycol: G198 (= G158), S296 (≠ G262), T300 (≠ H266), F303 (= F269)
- binding bicarbonate ion: Y65 (≠ L43), F101 (= F82), L356 (≠ I333), S357 (≠ A334), V403 (≠ L380), N406 (≠ V383)
- binding cholesterol: L226 (= L184), V255 (≠ G209), I262 (≠ L216), Y272 (≠ E226), F411 (= F393), V414 (≠ I396), V414 (≠ I396), C415 (≠ L397), C415 (≠ L397), I436 (≠ F412), M452 (= M428), F453 (≠ L430)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: W421 (vs. gap), V429 (≠ A406), V432 (≠ L408), F433 (≠ L409), I436 (≠ F412)
8shcC Pendrin in complex with niflumic acid (see paper)
22% identity, 97% coverage: 4:562/575 of query aligns to 33:607/613 of 8shcC
- binding cholesterol: I199 (vs. gap), A223 (≠ I181), V255 (≠ G209), Y272 (≠ E226), M412 (≠ I394), C415 (≠ L397), M452 (= M428), F453 (≠ L430)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: Q156 (≠ N116), W421 (vs. gap), V432 (≠ L408), F433 (≠ L409), F455 (≠ A432)
- binding 2-{[3-(trifluoromethyl)phenyl]amino}nicotinic acid: Y65 (≠ L43), F101 (= F82), T173 (= T133), E252 (≠ L206), I312 (= I280), L356 (≠ I333), S357 (≠ A334), V402 (≠ L379), N406 (≠ V383)
8sh3C Pendrin in complex with iodide (see paper)
22% identity, 97% coverage: 4:562/575 of query aligns to 33:607/613 of 8sh3C
- binding Lauryl Maltose Neopentyl Glycol: S114 (= S101), G198 (= G158), E297 (≠ K263), T300 (≠ H266), F303 (= F269)
- binding cholesterol: I199 (vs. gap), A223 (≠ I181), V255 (≠ G209), I258 (≠ T212), I262 (≠ L216), Y272 (≠ E226), F411 (= F393), V414 (≠ I396), C415 (≠ L397), V417 (≠ I399), I439 (≠ T415), M452 (= M428), F453 (≠ L430)
- binding iodide ion: Y65 (≠ L43), N406 (≠ V383)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L155 (≠ T115), F159 (≠ R119), W421 (vs. gap), V429 (≠ A406), V432 (≠ L408), F433 (≠ L409), I436 (≠ F412), L451 (≠ G427), F455 (≠ A432), F464 (vs. gap), P465 (vs. gap)
8sgwC Pendrin in complex with chloride (see paper)
22% identity, 97% coverage: 4:562/575 of query aligns to 33:607/613 of 8sgwC
- binding Lauryl Maltose Neopentyl Glycol: G198 (= G158), S296 (≠ G262), T300 (≠ H266), F303 (= F269)
- binding chloride ion: Y65 (≠ L43), N406 (≠ V383)
- binding cholesterol: I228 (≠ L186), V255 (≠ G209), I262 (≠ L216), Y272 (≠ E226), K408 (≠ W385), F411 (= F393), M412 (≠ I394), M412 (≠ I394), V414 (≠ I396), C415 (≠ L397), V417 (≠ I399), I439 (≠ T415)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: F159 (≠ R119), Y163 (≠ V123), F284 (≠ G243), P286 (= P245), I289 (≠ L248), F343 (≠ V320), F346 (= F323), W421 (vs. gap), F433 (≠ L409), I436 (≠ F412), F455 (≠ A432), F464 (vs. gap), P465 (vs. gap)
Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
22% identity, 81% coverage: 25:490/575 of query aligns to 83:564/744 of Q9JKQ2
- 158:168 (vs. 100:102, 9% identical) Involved in motor function
- S398 (≠ A334) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
- R399 (= R335) 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, 81% coverage: 25:490/575 of query aligns to 83:564/744 of Q9EPH0
- L104 (≠ A46) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- V149 (≠ Y91) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D154 (≠ G96) mutation to N: Shifts the voltage-sensitivity to more negative values.
- D155 (≠ G97) 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 (≠ N116) mutation to Q: Shifts the voltage-sensitivity to more negative values.
- A202 (≠ I121) 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 (≠ P152) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (≠ P154) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
- R236 (≠ T155) 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 (≠ V187) 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 (≠ T188) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values.
- R281 (≠ W192) mutation to Q: No effect; when associated with Q-283 and Q-285.
- K283 (= K194) mutation to Q: No effect; when associated with Q-218 and Q-285.
- K285 (= K196) mutation to Q: No effect; when associated with Q-281 and Q-283.
- P331 (= P249) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D332 (≠ E250) mutation to Q: No effect.
- D342 (≠ P278) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K359 (≠ V295) 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 (≠ G325) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S398 (≠ A334) 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 (= R335) 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 (≠ A344) 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 (≠ S345) mutation to Q: No effect.
- L431 (≠ V367) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S465 (≠ L397) 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 (≠ V421) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- K557 (≠ H483) mutation to Q: No effect; when associated with Q-558 and Q-559.
- R558 (≠ S484) mutation to Q: No effect; when associated with Q-557 and Q-559.
- K559 (≠ M485) mutation to Q: No effect; when associated with Q-557 and Q-558.
Sites not aligning to the query:
- 505:718 Extended region for STAS domain
- 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.
D7PC76 Prestin; Solute carrier family 26 member 5 from Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) (see paper)
22% identity, 81% coverage: 25:490/575 of query aligns to 83:564/741 of D7PC76
- GG 274:275 (vs. gap) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
- S398 (≠ A334) binding salicylate
7lguA Structure of human prestin in the presence of nacl (see paper)
21% identity, 81% coverage: 25:490/575 of query aligns to 71:552/680 of 7lguA
P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
21% identity, 81% coverage: 25:490/575 of query aligns to 83:564/744 of P58743
- F101 (≠ L43) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ A334) binding salicylate
P58735 Sulfate anion transporter 1; SAT-1; Solute carrier family 26 member 1 from Mus musculus (Mouse) (see paper)
23% identity, 84% coverage: 1:485/575 of query aligns to 49:563/704 of P58735
- A56 (≠ N8) mutation to T: Decreased sulfate-hydrogencarbonate exchange activity. Does not affect localization to plasma membrane.
- T190 (≠ G102) mutation to M: Decreased sulfate-hydrogencarbonate exchange activity. Loss of localization to plasma membrane.
- S363 (≠ L292) mutation to L: Decreased sulfate-hydrogencarbonate exchange activity. Increased accumulation of protein in ER.
Query Sequence
>WP_035628996.1 NCBI__GCF_000711315.1:WP_035628996.1
MLQNWFPNLQSFWQSLLHPSDLKPNVLAGLTVGIIALPLSMALAIAIDVPPQHGLYTAMI
GGVVIALFGGSKINISGPTAAFVVVLLPIVYQYGLGGLLLSGLMAGILLIIMGLTNMGRL
IEVVPYPVTVGFTSGIAVVIATLQIKDLLGLPLPTLTGHFIENAGTILQSLPQFHWQEAL
IGLLTLVTFILWSKQKSYIPPHLIALLVGTLTALALPYFLPAFQVETIGSRFHYLMDGVS
GQGIPPFLPELSLPWNQPGADGKPLHLSFELIHDLLGPAITIALLGSIESLLCAVVADGM
TGTKHQPNKELIGQGIGNIVVPFFGGIPATAAIARTAASIRSGASSPLASVVHALFVLGA
IVFFAPVLSHIPMAALAALLIMVAWNMSEAKHFIRILKIAPRADVAVLLTCFSITVLFDM
VMAVSIGMGLAALLFISRSIQLTEVKKWEHQSEHPHLKNLPKEVLVYDINGPLFFGSAQK
ALHSMATVNPDTKVLILDMSDVSMLDMSAIMVLETIYSRLQAQKIAIIINQCNERLILKL
QKAGIHKQTGRVDFSKNLEEAIEIAKNSMLNPKLE
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