SitesBLAST
Comparing WP_011610815.1 NCBI__GCF_000014265.1:WP_011610815.1 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)
54% identity, 99% coverage: 1:542/550 of query aligns to 1:543/564 of Q55415
- T69 (= T69) binding hydrogencarbonate; mutation to A: Alters bicarbonate transport.
- D258 (= D257) binding Na(+); mutation D->A,E: Alters bicarbonate transport.
- T262 (= T261) binding Na(+); mutation to A: Alters bicarbonate transport.
- G300 (= G299) binding Na(+)
- A301 (= A300) binding hydrogencarbonate
- T302 (= T301) binding Na(+); mutation to A: Alters bicarbonate transport.
- A471 (≠ V470) mutation to N: Alters bicarbonate transport.
- L476 (= L475) mutation to S: Alters bicarbonate transport.
- A486 (≠ M485) mutation to E: Alters bicarbonate transport.
- L490 (= L489) mutation to Q: Alters bicarbonate transport.
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
57% identity, 71% coverage: 2:391/550 of query aligns to 1:391/392 of 6ki1B
5da0A Structure of the the slc26 transporter slc26dg in complex with a nanobody (see paper)
27% identity, 93% coverage: 9:519/550 of query aligns to 5:467/467 of 5da0A
Sites not aligning to the query:
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
30% identity, 69% coverage: 15:395/550 of query aligns to 29:416/575 of 7lhvA
Sites not aligning to the query:
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
27% identity, 92% coverage: 12:518/550 of query aligns to 23:564/597 of 7v74A
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
28% identity, 92% coverage: 12:518/550 of query aligns to 23:572/605 of 7v75A
7lguA Structure of human prestin in the presence of nacl (see paper)
25% identity, 82% coverage: 14:464/550 of query aligns to 70:550/680 of 7lguA
P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
25% identity, 82% coverage: 14:464/550 of query aligns to 82:562/744 of P58743
- F101 (= F33) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ M302) binding salicylate
Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
24% identity, 82% coverage: 14:464/550 of query aligns to 82:562/744 of Q9JKQ2
- 158:168 (vs. 87:92, 18% identical) Involved in motor function
- S398 (≠ M302) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
- R399 (= R303) 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, 82% coverage: 14:464/550 of query aligns to 82:562/744 of Q9EPH0
- L104 (≠ S36) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- V149 (≠ T81) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D154 (= D86) 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 (= E93) mutation to Q: No effect.
- K177 (vs. gap) mutation to Q: No effect.
- R197 (≠ Q113) mutation to Q: Shifts the voltage-sensitivity to more negative values.
- A202 (≠ I118) 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 (vs. gap) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (vs. gap) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
- R236 (vs. gap) 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 (= R188) 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 (= K189) mutation to Q: No effect; when associated with Q-281 and Q-283.
- P331 (= P233) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D332 (≠ V234) mutation to Q: No effect.
- D342 (= D246) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K359 (≠ L263) 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 (≠ G293) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S398 (≠ M302) 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 (= R303) 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 (= G312) 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 (= K313) mutation to Q: No effect.
- L431 (= L335) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S465 (≠ H365) 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 (≠ V388) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- K557 (≠ S459) mutation to Q: No effect; when associated with Q-558 and Q-559.
- R558 (= R460) mutation to Q: No effect; when associated with Q-557 and Q-559.
- K559 (≠ H461) 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)
23% identity, 82% coverage: 14:464/550 of query aligns to 82:562/741 of D7PC76
- GG 274:275 (vs. gap) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
- S398 (≠ M302) binding salicylate
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)
26% identity, 70% coverage: 23:406/550 of query aligns to 103:509/758 of Q8CIW6
Sites not aligning to the query:
- 552 T→A: Does not inhibit formate transport in PMA-induced cells.
Q9URY8 Probable sulfate permease C869.05c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
23% identity, 70% coverage: 14:398/550 of query aligns to 123:526/840 of Q9URY8
Sites not aligning to the query:
- 823 modified: Phosphoserine
A0FKN5 Prestin; Solute carrier family 26 member 5 from Gallus gallus (Chicken) (see paper)
25% identity, 61% coverage: 12:349/550 of query aligns to 81:451/742 of A0FKN5
- S404 (≠ M302) 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 (= R303) mutation to C: Fully abolishes anion transport.
8sieC Pendrin in complex with bicarbonate (see paper)
23% identity, 94% coverage: 12:530/550 of query aligns to 44:598/613 of 8sieC
- binding Lauryl Maltose Neopentyl Glycol: G198 (≠ A150), S296 (≠ N238), T300 (≠ V245), F303 (≠ L248)
- binding bicarbonate ion: Y65 (≠ F33), F101 (≠ M72), L356 (≠ T301), S357 (≠ M302), V403 (≠ L348), N406 (vs. gap)
- binding cholesterol: L226 (= L178), V255 (≠ A200), I262 (= I207), Y272 (≠ S215), F411 (≠ G352), V414 (≠ I355), V414 (≠ I355), C415 (≠ I356), C415 (≠ I356), I436 (= I380), M452 (≠ F396), F453 (≠ I397)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: W421 (≠ K362), V429 (≠ G373), V432 (≠ Y376), F433 (≠ S377), I436 (= I380)
8shcC Pendrin in complex with niflumic acid (see paper)
23% identity, 94% coverage: 12:530/550 of query aligns to 44:598/613 of 8shcC
- binding cholesterol: I199 (≠ S151), A223 (≠ L175), V255 (≠ A200), Y272 (≠ S215), M412 (≠ V353), C415 (≠ I356), M452 (≠ F396), F453 (≠ I397)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: Q156 (= Q113), W421 (≠ K362), V432 (≠ Y376), F433 (≠ S377), F455 (≠ N399)
- binding 2-{[3-(trifluoromethyl)phenyl]amino}nicotinic acid: Y65 (≠ F33), F101 (≠ M72), T173 (≠ M130), E252 (≠ P197), I312 (≠ D257), L356 (≠ T301), S357 (≠ M302), V402 (≠ I347), N406 (vs. gap)
8sh3C Pendrin in complex with iodide (see paper)
23% identity, 94% coverage: 12:530/550 of query aligns to 44:598/613 of 8sh3C
- binding Lauryl Maltose Neopentyl Glycol: S114 (≠ A85), G198 (≠ A150), E297 (≠ Q239), T300 (≠ V245), F303 (≠ L248)
- binding cholesterol: I199 (≠ S151), A223 (≠ L175), V255 (≠ A200), I258 (≠ T203), I262 (= I207), Y272 (≠ S215), F411 (≠ G352), V414 (≠ I355), C415 (≠ I356), V417 (≠ W358), I439 (≠ V383), M452 (≠ F396), F453 (≠ I397)
- binding iodide ion: Y65 (≠ F33), N406 (vs. gap)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L155 (= L112), F159 (≠ K116), W421 (≠ K362), V429 (≠ G373), V432 (≠ Y376), F433 (≠ S377), I436 (= I380), L451 (≠ I395), F455 (≠ N399), F464 (≠ D408), P465 (≠ M409)
8sgwC Pendrin in complex with chloride (see paper)
23% identity, 94% coverage: 12:530/550 of query aligns to 44:598/613 of 8sgwC
- binding Lauryl Maltose Neopentyl Glycol: G198 (≠ A150), S296 (≠ N238), T300 (≠ V245), F303 (≠ L248)
- binding chloride ion: Y65 (≠ F33), N406 (vs. gap)
- binding cholesterol: I228 (= I180), V255 (≠ A200), I262 (= I207), Y272 (≠ S215), K408 (vs. gap), F411 (≠ G352), M412 (≠ V353), M412 (≠ V353), V414 (≠ I355), C415 (≠ I356), V417 (≠ W358), I439 (≠ V383)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: F159 (≠ K116), Y163 (≠ L120), F284 (vs. gap), P286 (= P228), I289 (≠ H231), F343 (≠ M288), F346 (≠ L291), W421 (≠ K362), F433 (≠ S377), I436 (= I380), F455 (≠ N399), F464 (≠ D408), P465 (≠ M409)
7xulA Human slc26a3 in complex with tenidap
25% identity, 61% coverage: 12:349/550 of query aligns to 59:414/690 of 7xulA
- binding 5-chloranyl-2-oxidanyl-3-thiophen-2-ylcarbonyl-indole-1-carboxamide: V72 (= V25), L75 (≠ P28), Q76 (≠ L29), E262 (≠ L199), S367 (≠ M302), L412 (≠ I347)
- binding cholesterol hemisuccinate: I157 (= I104), F162 (= F109), P209 (= P149), K214 (vs. gap), Y217 (≠ A152), V302 (= V234), Q306 (= Q241), V309 (≠ L244)
Sites not aligning to the query:
7xuhA Down-regulated in adenoma in complex with tqr1122
25% identity, 61% coverage: 12:349/550 of query aligns to 66:427/707 of 7xuhA
- binding 2-[4,8-dimethyl-2-oxidanylidene-7-[[3-(trifluoromethyl)phenyl]methoxy]chromen-3-yl]ethanoic acid: P124 (vs. gap), I125 (vs. gap), L187 (≠ I121), I192 (= I126), F195 (= F129), V335 (≠ D257), S338 (≠ L260), S380 (≠ M302)
- binding cholesterol hemisuccinate: V223 (≠ A150), F226 (vs. gap), K227 (vs. gap), Y230 (≠ A152), F318 (= F237), Q319 (= Q241)
Sites not aligning to the query:
Query Sequence
>WP_011610815.1 NCBI__GCF_000014265.1:WP_011610815.1
MQLVNSLHFNNLRGDLLGGLTAAIVALPLALAFGVSSGAGAITGLYGAIFVGFFAALCGG
TPSQITGPTGPMTVLMATVFTTLLADNPDAGLEMAFTVVMLGGIFQILFGVLQLGKYIVL
IPYAVISGFMSGVGVIIIIIQIGPFLGHPASASVAQSIKKIPEFLINLNPAAVGLGILTI
VILLFTPRKVTAIIPSPLLALLTGTLISVFFLSDSNLILIGEIPTGLPKLHLPVFTFNQL
QNMLVDGLVLGTLGSIDSLLTSLVADNITRSNHDSDHELIGQGIGNIMSGLFGGLPGAGA
TMRTVVNVHAGGKTPLSGIVHSIILLLILLWAGKLTEAIPQAILAGILLKVGVDIIDWGF
LKRAHNLSLKAAGIMYSVLILTVFVNLVTAVAVGIFIANLLTVKRLSDMQINDIKAIVEP
NDEIPLRDQEKQLLKECRGHLLLLHLGGPMSFGAAKALSRHMGMVQQYDVLILDLSDVSY
LGITMSLALENMVTEASRKHREVFIVGASGGVKTRLGKLKIWNFVPRQNLVGTRIKALQQ
TLNLLVERKI
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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