SitesBLAST
Comparing AO353_10315 FitnessBrowser__pseudo3_N2E3:AO353_10315 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)
32% identity, 96% coverage: 21:550/552 of query aligns to 15:549/564 of Q55415
- T69 (= T75) binding ; mutation to A: Alters bicarbonate transport.
- D258 (≠ E262) binding ; mutation D->A,E: Alters bicarbonate transport.
- T262 (≠ S266) binding ; mutation to A: Alters bicarbonate transport.
- G300 (= G304) binding
- A301 (= A305) binding
- T302 (≠ I306) binding ; mutation to A: Alters bicarbonate transport.
- A471 (≠ T472) mutation to N: Alters bicarbonate transport.
- L476 (= L477) mutation to S: Alters bicarbonate transport.
- A486 (≠ G487) mutation to E: Alters bicarbonate transport.
- L490 (= L491) mutation to Q: Alters bicarbonate transport.
5da0A Structure of the the slc26 transporter slc26dg in complex with a nanobody (see paper)
29% identity, 89% coverage: 20:511/552 of query aligns to 10:457/467 of 5da0A
Sites not aligning to the query:
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
29% identity, 93% coverage: 16:531/552 of query aligns to 20:576/597 of 7v74A
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
29% identity, 93% coverage: 16:531/552 of query aligns to 20:584/605 of 7v75A
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
35% identity, 68% coverage: 21:397/552 of query aligns to 14:391/392 of 6ki1B
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
23% identity, 95% coverage: 8:532/552 of query aligns to 16:562/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (≠ T111), R127 (≠ K112), W130 (≠ A115)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (= L113), L131 (≠ I116), E409 (≠ A394), L413 (≠ N398), G417 (≠ I402), A421 (≠ S415)
- binding sulfate ion: A84 (≠ G76), S321 (≠ A305), F322 (≠ I306)
Q9JKQ2 Prestin; Solute carrier family 26 member 5 from Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus) (see 2 papers)
25% identity, 86% coverage: 8:479/552 of query aligns to 70:572/744 of Q9JKQ2
- 158:168 (vs. 81:91, 45% identical) Involved in motor function
- S398 (≠ A307) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
- R399 (= R308) mutation to E: Removes salicylate competition with anions. Retains the displacement currents.
7lguA Structure of human prestin in the presence of nacl (see paper)
23% identity, 97% coverage: 8:542/552 of query aligns to 58:668/680 of 7lguA
Q9EPH0 Prestin; Solute carrier family 26 member 5 from Rattus norvegicus (Rat) (see 3 papers)
25% identity, 85% coverage: 8:474/552 of query aligns to 70:568/744 of Q9EPH0
- L104 (≠ A42) 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 (vs. gap) mutation to Q: No effect.
- K177 (≠ A97) 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 (≠ P148) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-235 and Q-236.
- K235 (≠ I150) mutation to Q: Shifts the voltage-sensitivity to more negative values; when associated with Q-233 and Q-236.
- R236 (≠ S151) 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 (≠ P188) 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 (≠ K189) mutation to Q: Shifts the voltage-sensitivity to slightly more positive values.
- R281 (vs. gap) mutation to Q: No effect; when associated with Q-283 and Q-285.
- K283 (≠ I193) mutation to Q: No effect; when associated with Q-218 and Q-285.
- K285 (≠ R195) mutation to Q: No effect; when associated with Q-281 and Q-283.
- P331 (= P238) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- D332 (≠ A239) mutation to Q: No effect.
- D342 (≠ P251) mutation to Q: Shifts the voltage-sensitivity to more positive values.
- K359 (≠ V268) 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 (≠ G298) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S398 (≠ A307) 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 (= R308) 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 (= G317) 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 (≠ N318) mutation to Q: No effect.
- L431 (= L340) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- S465 (≠ P374) 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 (≠ A394) mutation to C: Is accessible from the extracellular side after extracellular application of thiol-reactive reagents.
- K557 (≠ A464) mutation to Q: No effect; when associated with Q-558 and Q-559.
- R558 (vs. gap) mutation to Q: No effect; when associated with Q-557 and Q-559.
- K559 (≠ Q465) 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)
24% identity, 83% coverage: 8:465/552 of query aligns to 70:558/741 of D7PC76
- GG 274:275 (≠ TA 186:187) mutation to LV: Abolishes non-linear capacitance. Does not affect protein expression.
- S398 (≠ A307) binding
P58743 Prestin; Solute carrier family 26 member 5 from Homo sapiens (Human) (see paper)
25% identity, 85% coverage: 8:474/552 of query aligns to 70:568/744 of P58743
- F101 (= F39) mutation to Y: Decreases salicylate inhibition.
- S398 (≠ A307) binding
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)
27% identity, 82% coverage: 28:479/552 of query aligns to 102:579/758 of Q8CIW6
- F552 (= F453) 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)
26% identity, 79% coverage: 28:465/552 of query aligns to 100:563/759 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 (≠ I116) to M: in dbSNP:rs13324142
- ATV 547:549 (≠ GPL 449:451) mutation to NVN: Does not inhibit cell membrane localization. Inhibits interaction with CA2 and bicarbonate transport.
- N553 (≠ A455) 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.
A0FKN5 Prestin; Solute carrier family 26 member 5 from Gallus gallus (Chicken) (see paper)
24% identity, 84% coverage: 16:479/552 of query aligns to 79:579/742 of A0FKN5
- S404 (≠ A307) 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 (= R308) mutation to C: Fully abolishes anion transport.
8sieC Pendrin in complex with bicarbonate
23% identity, 93% coverage: 14:525/552 of query aligns to 39:591/613 of 8sieC
- binding Lauryl Maltose Neopentyl Glycol: G198 (≠ H154), S296 (≠ Q244), T300 (≠ G250), F303 (= F253)
- binding bicarbonate ion: Y65 (≠ F39), F101 (vs. gap), L356 (≠ I306), S357 (≠ A307), V403 (≠ L353), N406 (≠ E362)
- binding cholesterol: L226 (≠ V182), V255 (= V206), I262 (≠ F213), Y272 (≠ S223), F411 (= F366), V414 (≠ M369), V414 (≠ M369), C415 (≠ V370), C415 (≠ V370), I436 (≠ S386), M452 (≠ I402), F453 (≠ L403)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: W421 (vs. gap), V429 (≠ A379), V432 (≠ L382), F433 (≠ I383), I436 (≠ S386)
8shcC Pendrin in complex with niflumic acid
23% identity, 93% coverage: 14:525/552 of query aligns to 39:591/613 of 8shcC
- binding cholesterol: I199 (≠ F155), A223 (≠ S179), V255 (= V206), Y272 (≠ S223), M412 (≠ Q367), C415 (≠ V370), M452 (≠ I402), F453 (≠ L403)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: Q156 (≠ K112), W421 (vs. gap), V432 (≠ L382), F433 (≠ I383), F455 (≠ M405)
- binding 2-{[3-(trifluoromethyl)phenyl]amino}nicotinic acid: Y65 (≠ F39), F101 (vs. gap), T173 (= T129), E252 (≠ M203), I312 (= I261), L356 (≠ I306), S357 (≠ A307), V402 (≠ I352), N406 (≠ E362)
8sgwC Pendrin in complex with chloride
23% identity, 93% coverage: 14:525/552 of query aligns to 39:591/613 of 8sgwC
- binding Lauryl Maltose Neopentyl Glycol: G198 (≠ H154), S296 (≠ Q244), T300 (≠ G250), F303 (= F253)
- binding cholesterol: I228 (≠ V184), V255 (= V206), I262 (≠ F213), Y272 (≠ S223), K408 (= K364), F411 (= F366), M412 (≠ Q367), M412 (≠ Q367), V414 (≠ M369), C415 (≠ V370), V417 (vs. gap), I439 (≠ V389)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: F159 (≠ A115), Y163 (≠ F119), F284 (≠ L232), P286 (≠ E234), I289 (≠ L237), F343 (≠ V293), F346 (≠ L296), W421 (vs. gap), F433 (≠ I383), I436 (≠ S386), F455 (≠ M405), F464 (vs. gap), P465 (vs. gap)
Q9URY8 Probable sulfate permease C869.05c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 72% coverage: 17:413/552 of query aligns to 119:539/840 of Q9URY8
Sites not aligning to the query:
- 823 modified: Phosphoserine
7xujA Human slc26a3 in complex with uk5099
25% identity, 88% coverage: 7:494/552 of query aligns to 55:567/703 of 7xujA
- binding (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid: V79 (= V31), Q83 (≠ L35), E271 (≠ M203), S376 (≠ A307), R377 (= R308), V380 (≠ T311), L421 (= L349), A422 (= A350), N425 (≠ V355)
- binding cholesterol hemisuccinate: F171 (≠ L108), V311 (= V235), Q315 (≠ A239)
P58735 Sulfate anion transporter 1; SAT-1; Solute carrier family 26 member 1 from Mus musculus (Mouse) (see paper)
23% identity, 94% coverage: 6:524/552 of query aligns to 47:668/704 of P58735
- A56 (≠ P15) mutation to T: Decreased sulfate-hydrogencarbonate exchange activity. Does not affect localization to plasma membrane.
- T190 (vs. gap) mutation to M: Decreased sulfate-hydrogencarbonate exchange activity. Loss of localization to plasma membrane.
- S363 (≠ L265) mutation to L: Decreased sulfate-hydrogencarbonate exchange activity. Increased accumulation of protein in ER.
Query Sequence
>AO353_10315 FitnessBrowser__pseudo3_N2E3:AO353_10315
MIAIREAWKAGLLRPEHWLRNIVSGVIVGVVALPLAMAFAIASGVKPEQGIYTAIVSGLL
VSLFGGSRLQIAGPTGAFVVILSGVTAKYGVDGLQIATMMAGAILLLLGITKLGAIIKFI
PDPVIVGFTAGIGVIIWVGQWKDFFGLPKISGEHFHERLWHLVQALPSFHVPTTLLALSS
LVLVITAPKIPGIRRVPGPLIAMVVVTALQAFFQFAGVATIGSAFGGIPQGLPEVGLPAI
TLPQVIELIGPAFAIAMLGAIESLLSAVVADGMAGTKHDSNQELIGQGIANLVTPLFGGF
AATGAIARTATNIRNGGNSPIAGFVHALTLILLILFLAPLASDIPLCALAAILFVVAYNM
SELKHFQRMVKRAPKADVAILLITFSLTVFSDLAIAVNIGVILAMLQFMRRMASSVEVQQ
MVEKELEVELRINGHVRLPPGVLVYTIEGPLFFGAAETFERVLAQTHTDPGTLIIRLKRV
PFMDITGLQTLLEVIEHLRKRSIVVKLCEANEKVLGKLDKAGILQALGPEHYHADFSGAL
GSFEIDKTPHLG
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