SitesBLAST
Comparing Pf1N1B4_2936 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_2936 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)
Q55415 Bicarbonate transporter BicA from Synechocystis sp. (strain PCC 6803 / Kazusa) (see paper)
29% identity, 92% coverage: 22:547/573 of query aligns to 9:524/564 of Q55415
- T69 (= T82) binding ; mutation to A: Alters bicarbonate transport.
- D258 (≠ E290) binding ; mutation D->A,E: Alters bicarbonate transport.
- T262 (≠ C294) binding ; mutation to A: Alters bicarbonate transport.
- G300 (≠ A332) binding
- A301 (= A333) binding
- T302 (≠ I334) binding ; 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 (≠ F513) mutation to Q: Alters bicarbonate transport.
5da0A Structure of the the slc26 transporter slc26dg in complex with a nanobody (see paper)
28% identity, 88% coverage: 26:531/573 of query aligns to 9:455/467 of 5da0A
Sites not aligning to the query:
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
31% identity, 71% coverage: 22:425/573 of query aligns to 8:391/392 of 6ki1B
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
25% identity, 93% coverage: 12:545/573 of query aligns to 16:553/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (≠ I118), R127 (= R119), W130 (≠ R122)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (≠ A120), L131 (= L123), E409 (≠ V422), L413 (≠ A426), G417 (≠ L430), A421 (≠ G434)
- binding sulfate ion: A84 (= A83), S321 (≠ A333), F322 (≠ I334)
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
28% identity, 93% coverage: 16:548/573 of query aligns to 13:578/605 of 7v75A
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
28% identity, 93% coverage: 16:548/573 of query aligns to 13:570/597 of 7v74A
Q9URY8 Probable sulfate permease C869.05c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
27% identity, 64% coverage: 16:382/573 of query aligns to 112:480/840 of Q9URY8
Sites not aligning to the query:
- 823 modified: Phosphoserine
7xujA Human slc26a3 in complex with uk5099
23% identity, 83% coverage: 15:490/573 of query aligns to 55:542/703 of 7xujA
- binding (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid: V79 (≠ I38), Q83 (≠ L42), E271 (≠ G212), S376 (≠ A335), R377 (= R336), V380 (≠ T339), L421 (= L380), A422 (≠ L381), N425 (≠ V384)
- binding cholesterol hemisuccinate: F171 (≠ L115), V311 (≠ Y270), Q315 (≠ R274)
7xulA Human slc26a3 in complex with tenidap
23% identity, 81% coverage: 15:476/573 of query aligns to 48:516/690 of 7xulA
- binding 5-chloranyl-2-oxidanyl-3-thiophen-2-ylcarbonyl-indole-1-carboxamide: V72 (≠ I38), L75 (≠ P41), Q76 (≠ L42), E262 (≠ G212), S367 (≠ A335), L412 (= L380), N416 (≠ V384)
- binding cholesterol hemisuccinate: I157 (≠ A110), F162 (≠ L115), P209 (vs. gap), K214 (≠ E165), Y217 (≠ G168), V302 (≠ Y270), Q306 (≠ R274), V309 (≠ M277), V450 (= V422)
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, 71% coverage: 35:441/573 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.
P58735 Sulfate anion transporter 1; SAT-1; Solute carrier family 26 member 1 from Mus musculus (Mouse) (see paper)
24% identity, 93% coverage: 16:550/573 of query aligns to 59:672/704 of P58735
- T190 (= T105) mutation to M: Decreased sulfate-hydrogencarbonate exchange activity. Loss of localization to plasma membrane.
- S363 (≠ L293) mutation to L: Decreased sulfate-hydrogencarbonate exchange activity. Increased accumulation of protein in ER.
Sites not aligning to the query:
- 56 A→T: Decreased sulfate-hydrogencarbonate exchange activity. Does not affect localization to plasma membrane.
7lguA Structure of human prestin in the presence of nacl (see paper)
22% identity, 92% coverage: 16:542/573 of query aligns to 58:644/680 of 7lguA
7xuhA Down-regulated in adenoma in complex with tqr1122
22% identity, 83% coverage: 15:490/573 of query aligns to 55:546/707 of 7xuhA
- binding 2-[4,8-dimethyl-2-oxidanylidene-7-[[3-(trifluoromethyl)phenyl]methoxy]chromen-3-yl]ethanoic acid: P124 (≠ A83), I125 (≠ A84), L187 (≠ I127), I192 (≠ T132), F195 (= F135), V335 (≠ E290), S338 (≠ L293), S380 (≠ A335), M433 (= M388)
- binding cholesterol hemisuccinate: V223 (vs. gap), F226 (≠ I164), K227 (≠ E165), Y230 (≠ G168), F318 (≠ I273), Q319 (≠ R274)
Q9EPH0 Prestin; Solute carrier family 26 member 5 from Rattus norvegicus (Rat) (see 3 papers)
23% identity, 82% coverage: 16:487/573 of query aligns to 70:558/744 of Q9EPH0
- L104 (≠ A49) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- V149 (vs. gap) 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 (≠ G99) mutation to Q: No effect.
- K177 (vs. gap) mutation to Q: No effect.
- R197 (= R119) mutation to Q: Shifts the voltage-sensitivity to more negative values.
- A202 (≠ I124) 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 (≠ S155) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (≠ T157) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
- R236 (≠ G158) 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 (≠ P196) 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 (≠ R197) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values.
- R281 (= R201) mutation to Q: No effect; when associated with Q-283 and Q-285.
- K283 (≠ P203) mutation to Q: No effect; when associated with Q-218 and Q-285.
- K285 (≠ H205) mutation to Q: No effect; when associated with Q-281 and Q-283.
- P331 (= P261) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D332 (≠ Y262) mutation to Q: No effect.
- D342 (≠ P279) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K359 (≠ V296) 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 (≠ G326) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S398 (≠ A335) 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 (= R336) 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 (≠ A345) 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 (≠ F346) mutation to Q: No effect.
- L431 (= L368) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S465 (≠ L398) 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 (≠ L418) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- K557 (≠ R486) mutation to Q: No effect; when associated with Q-558 and Q-559.
- R558 (≠ K487) mutation to Q: No effect; when associated with Q-557 and Q-559.
Sites not aligning to the query:
- 505:718 Extended region for STAS domain
- 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)
23% identity, 82% coverage: 16:487/573 of query aligns to 70:558/744 of Q9JKQ2
- 158:168 (vs. 90:98, 18% identical) Involved in motor function
- S398 (≠ A335) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
- R399 (= R336) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
Q62273 Sulfate transporter; Diastrophic dysplasia protein homolog; ST-OB; Solute carrier family 26 member 2 from Mus musculus (Mouse) (see paper)
22% identity, 95% coverage: 16:561/573 of query aligns to 98:715/739 of Q62273
- F368 (≠ D253) mutation to A: Reduced sulfate-chloride exchange activity.
- E417 (= E311) mutation E->A,K: Loss of sulfate-chloride exchange activity.
P40879 Chloride anion exchanger; Down-regulated in adenoma; Protein DRA; Solute carrier family 26 member 3 from Homo sapiens (Human) (see 3 papers)
23% identity, 83% coverage: 15:487/573 of query aligns to 62:554/764 of P40879
- N153 (≠ Q94) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- N161 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- N165 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
- C307 (≠ A227) 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.
P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
23% identity, 82% coverage: 16:487/573 of query aligns to 70:558/744 of P58743
- F101 (≠ L46) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ A335) binding
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, 77% coverage: 35:478/573 of query aligns to 100:546/759 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 (≠ L123) 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.
8sieC Pendrin in complex with bicarbonate
21% identity, 93% coverage: 16:549/573 of query aligns to 34:593/613 of 8sieC
- binding Lauryl Maltose Neopentyl Glycol: G198 (≠ E161), S296 (≠ R274), T300 (≠ A278), F303 (= F281)
- binding bicarbonate ion: Y65 (≠ L46), F101 (vs. gap), L356 (≠ I334), S357 (≠ A335), V403 (≠ L381), N406 (≠ V384)
- binding cholesterol: L226 (vs. gap), V255 (≠ L215), I262 (≠ G222), Y272 (≠ R232), F411 (≠ S389), V414 (≠ R392), V414 (≠ R392), C415 (≠ H393), C415 (≠ H393), I436 (≠ L413), M452 (≠ L429), F453 (≠ L430)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: W421 (≠ R399), V429 (≠ L407), V432 (≠ L409), F433 (≠ L410), I436 (≠ L413)
Query Sequence
>Pf1N1B4_2936 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_2936
MSFSMPPLFAAWRQTWRAGYSLRRLRGDISAGVTVGIIAIPLAMALAIAVGVAPQQGLYT
VLIAAPLIALTGGSRFNVSGPTAAFVVILLPITQQYGLGGLLLCTMLAGAILIALGLIRA
GRLIQYIPYPVTLGFTAGIGIVIATLQLKDLLGLSTTGHAEHYIEQLGGLLQALPSARLG
DGIIGVMCLAVLIVWPRFVPRIPGHLVALAVGALLGVALESGGLAVATLGERFSYIVDGV
SHPGIPPFLPSFDWPWNLPGPYGQPLHLSYDLIRQLMAPAFAIAMLGAIESLLCAVVADG
MTGSKHDPNAELLGQGLGNLVAPLFGGITATAAIARSATNVRSGAFSPLAAIIHSAVVLL
AILALAPLFSYLPMAALAALLVMVAWNMSEARHVVHTLRIAPRSDVLVLLTCLSLTVLFD
MVLAVAVGLLLAAGLFIKRMSDLTDTAELPREFHQALEDMPEHVRCYAIRGPLFFGAAEK
ALGVLRKFSPEVKVVIVEMSAVPMLDMTALAAFDNILRDYRTDGIGLILVGTAPRVRLKL
RRAGIHREQRQLAYVNNLEQARRKSERWLVGQG
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