SitesBLAST
Comparing 5207981 Shew_0497 putative sulfate transporter YchM (RefSeq) 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, 91% coverage: 8:522/565 of query aligns to 2:506/564 of Q55415
- T69 (= T75) binding ; mutation to A: Alters bicarbonate transport.
- D258 (≠ E285) binding ; mutation D->A,E: Alters bicarbonate transport.
- T262 (≠ C289) binding ; mutation to A: Alters bicarbonate transport.
- G300 (≠ A327) binding
- A301 (= A328) binding
- T302 (≠ I329) binding ; mutation to A: Alters bicarbonate transport.
- A471 (≠ V487) mutation to N: Alters bicarbonate transport.
- L476 (≠ M492) mutation to S: Alters bicarbonate transport.
- A486 (= A502) mutation to E: Alters bicarbonate transport.
- L490 (≠ M506) 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: 12:509/565 of query aligns to 2:440/467 of 5da0A
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
26% identity, 96% coverage: 13:554/565 of query aligns to 12:569/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (≠ G111), R127 (≠ K112), W130 (≠ K115)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (= L113), L131 (= L116), E409 (≠ T417), L413 (≠ A421), G417 (= G425), A421 (≠ M429)
- binding sulfate ion: A84 (= A76), S321 (≠ A328), F322 (≠ I329)
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
31% identity, 73% coverage: 8:420/565 of query aligns to 1:391/392 of 6ki1B
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
26% identity, 92% coverage: 21:538/565 of query aligns to 26:567/597 of 7v74A
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
26% identity, 92% coverage: 21:538/565 of query aligns to 26:575/605 of 7v75A
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, 88% coverage: 28:523/565 of query aligns to 102:612/758 of Q8CIW6
- F552 (= F468) mutation to 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)
23% identity, 79% coverage: 28:472/565 of query aligns to 100:555/759 of Q9BXS9
- N167 (≠ L95) 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 (≠ L116) to M: in dbSNP:rs13324142
- ATV 547:549 (≠ GPL 464:466) mutation to NVN: Does not inhibit cell membrane localization. Inhibits interaction with CA2 and bicarbonate transport.
- N553 (≠ S470) 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.
Q9URY8 Probable sulfate permease C869.05c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
24% identity, 63% coverage: 20:377/565 of query aligns to 123:480/840 of Q9URY8
Sites not aligning to the query:
- 823 modified: Phosphoserine
D7PC76 Prestin; Solute carrier family 26 member 5 from Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus) (see paper)
23% identity, 85% coverage: 1:483/565 of query aligns to 63:564/741 of D7PC76
- GG 274:275 (≠ AW 187:188) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
- S398 (≠ A330) binding
7xulA Human slc26a3 in complex with tenidap
23% identity, 80% coverage: 20:470/565 of query aligns to 61:517/690 of 7xulA
- binding 5-chloranyl-2-oxidanyl-3-thiophen-2-ylcarbonyl-indole-1-carboxamide: V72 (≠ I31), L75 (≠ P34), Q76 (≠ L35), E262 (≠ A209), S367 (≠ A330), L412 (= L375), N416 (≠ V379)
- binding cholesterol hemisuccinate: I157 (≠ V103), F162 (≠ M108), P209 (≠ K159), K214 (≠ Q165), Y217 (≠ T168), V302 (≠ F247), Q306 (≠ W251), V309 (≠ I261), V450 (≠ L413)
P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
23% identity, 86% coverage: 1:485/565 of query aligns to 63:566/744 of P58743
- F101 (≠ L39) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ A330) binding
7lguA Structure of human prestin in the presence of nacl (see paper)
23% identity, 86% coverage: 1:485/565 of query aligns to 51:554/680 of 7lguA
7xujA Human slc26a3 in complex with uk5099
23% identity, 80% coverage: 20:470/565 of query aligns to 68:526/703 of 7xujA
- binding (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid: V79 (≠ I31), Q83 (≠ L35), E271 (≠ A209), S376 (≠ A330), R377 (= R331), V380 (≠ A334), L421 (= L375), A422 (≠ L376), N425 (≠ V379)
- binding cholesterol hemisuccinate: F171 (≠ M108), V311 (≠ F247), Q315 (≠ W251)
7xuhA Down-regulated in adenoma in complex with tqr1122
23% identity, 80% coverage: 20:470/565 of query aligns to 68:530/707 of 7xuhA
- binding 2-[4,8-dimethyl-2-oxidanylidene-7-[[3-(trifluoromethyl)phenyl]methoxy]chromen-3-yl]ethanoic acid: P124 (= P84), I125 (= I85), L187 (≠ V120), I192 (≠ T125), F195 (= F128), V335 (≠ S274), S338 (≠ T277), S380 (≠ A330), M433 (= M383)
- binding cholesterol hemisuccinate: V223 (≠ L160), F226 (≠ L164), K227 (≠ Q165), Y230 (≠ T168), F318 (≠ P250), Q319 (≠ W251)
Q9EPH0 Prestin; Solute carrier family 26 member 5 from Rattus norvegicus (Rat) (see 3 papers)
23% identity, 85% coverage: 1:483/565 of query aligns to 63:564/744 of Q9EPH0
- L104 (≠ A42) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- V149 (≠ Q87) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D154 (≠ G92) mutation to N: Shifts the voltage-sensitivity to more negative values.
- D155 (≠ G93) 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 (≠ K112) mutation to Q: Shifts the voltage-sensitivity to more negative values.
- A202 (≠ I117) 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 (≠ E148) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (≠ A150) 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 (≠ P189) 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 (≠ K190) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values.
- R281 (≠ K194) mutation to Q: No effect; when associated with Q-283 and Q-285.
- K283 (≠ P196) mutation to Q: No effect; when associated with Q-218 and Q-285.
- K285 (≠ H198) mutation to Q: No effect; when associated with Q-281 and Q-283.
- P331 (= P260) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D332 (≠ I261) mutation to Q: No effect.
- D342 (≠ S274) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K359 (≠ V291) 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 (≠ G321) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S398 (≠ A330) 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 (= R331) 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 (= G340) 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 (≠ S341) mutation to Q: No effect.
- L431 (= L363) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S465 (≠ L393) 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 (= D415) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- K557 (= K476) mutation to Q: No effect; when associated with Q-558 and Q-559.
- R558 (≠ T477) mutation to Q: No effect; when associated with Q-557 and Q-559.
- K559 (≠ I478) 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.
Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
23% identity, 85% coverage: 1:483/565 of query aligns to 63:564/744 of Q9JKQ2
- 158:168 (vs. 96:98, 9% identical) Involved in motor function
- S398 (≠ A330) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
- R399 (= R331) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
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, 80% coverage: 20:470/565 of query aligns to 75:548/764 of P40879
- N153 (vs. gap) 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 (≠ A222) 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.
8sieC Pendrin in complex with bicarbonate
21% identity, 92% coverage: 20:537/565 of query aligns to 46:588/613 of 8sieC
- binding Lauryl Maltose Neopentyl Glycol: G198 (≠ Y156), S296 (≠ R269), T300 (≠ P273), F303 (≠ I276)
- binding bicarbonate ion: Y65 (≠ L39), F101 (≠ L83), L356 (≠ I329), S357 (≠ A330), V403 (≠ L376), N406 (≠ V379)
- binding cholesterol: L226 (= L180), V255 (≠ G205), I262 (≠ M212), Y272 (≠ L236), F411 (vs. gap), V414 (≠ A386), V414 (≠ A386), C415 (≠ K387), C415 (≠ K387), I436 (≠ F408), M452 (= M424), F453 (≠ G425)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: W421 (≠ L393), V429 (= V401), V432 (≠ L404), F433 (≠ V405), I436 (≠ F408)
8shcC Pendrin in complex with niflumic acid
21% identity, 92% coverage: 20:537/565 of query aligns to 46:588/613 of 8shcC
- binding cholesterol: I199 (≠ L157), A223 (≠ I177), V255 (≠ G205), Y272 (≠ L236), M412 (≠ S384), C415 (≠ K387), M452 (= M424), F453 (≠ G425)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: Q156 (≠ K112), W421 (≠ L393), V432 (≠ L404), F433 (≠ V405), F455 (≠ A427)
- binding 2-{[3-(trifluoromethyl)phenyl]amino}nicotinic acid: Y65 (≠ L39), F101 (≠ L83), T173 (= T129), E252 (≠ L202), I312 (≠ E285), L356 (≠ I329), S357 (≠ A330), V402 (≠ L375), N406 (≠ V379)
Query Sequence
>5207981 Shew_0497 putative sulfate transporter YchM (RefSeq)
MFSAVKKSISAKPSFQEIQTNILAGLTVGVIALPLSMALAIASGVPPQHGLYTAMIAGIV
IALCGGSKVNISGPTAAFVVILLPIVQQFGLGGLLLSGLMAGVILLLMGLGKLGKLIEIV
PYPVTVGFTAGIGVVIATFQIKDFFGLEVAAGGEHYLEKLSYILQALTSISWQETLIGAL
TLAVLLAWPKLKSKVPAHLAALLVGALIAWVMTQMIGGFSVATIGSRFHYELDGLLGSGI
PPIMPSFEWPWNLPGADGQPIGMSFELVRELLPSAITIAILGALESLLCAVVADGMSGKK
HNPNDELIGQGLGNILVPLFGGIPATAAIARTAANVKAGGSMPLASVVHGLFILAGILLL
APLLSYIPMASMAALLLVVAWNMSEAKHFVRTLKVAPRDDVLILVLCFALTVLFDMTIAV
AVGMGLAAMLFIRRSISLTDARAVETNHQAYEVPESVVVYDINGPLFFGSAHKALKTIAL
VRPDVRVVILDMSEVTLLDMSAIVAMESIAQDLSGKQVALIINNLQPRMLLKLRRAGIRK
RRGQVEYARTMDDSFALAQRMTAQA
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