SitesBLAST
Comparing WP_043765232.1 NCBI__GCF_000733765.1:WP_043765232.1 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 ATCC 27184 / PCC 6803 / Kazusa) (see paper)
28% identity, 91% coverage: 22:543/574 of query aligns to 11:519/564 of Q55415
- T69 (= T80) binding hydrogencarbonate; mutation to A: Alters bicarbonate transport.
- D258 (≠ E291) binding Na(+); mutation D->A,E: Alters bicarbonate transport.
- T262 (≠ C295) binding Na(+); mutation to A: Alters bicarbonate transport.
- G300 (≠ A333) binding Na(+)
- A301 (= A334) binding hydrogencarbonate
- T302 (≠ I335) binding Na(+); mutation to A: Alters bicarbonate transport.
- A471 (≠ T495) mutation to N: Alters bicarbonate transport.
- L476 (≠ M500) mutation to S: Alters bicarbonate transport.
- A486 (= A510) mutation to E: Alters bicarbonate transport.
- L490 (= L514) mutation to Q: Alters bicarbonate transport.
5da0A Structure of the the slc26 transporter slc26dg in complex with a nanobody (see paper)
26% identity, 89% coverage: 24:533/574 of query aligns to 9:456/467 of 5da0A
Sites not aligning to the query:
7v74A Thermostabilized human prestin in complex with sulfate (see paper)
25% identity, 91% coverage: 26:545/574 of query aligns to 26:566/597 of 7v74A
6ki1B The transmembrane domain of a cyanobacterium bicarbonate transporter bica (see paper)
28% identity, 71% coverage: 22:426/574 of query aligns to 10:391/392 of 6ki1B
7v75A Thermostabilized human prestin in complex with salicylate (see paper)
25% identity, 91% coverage: 26:545/574 of query aligns to 26:574/605 of 7v75A
7lhvA Structure of arabidopsis thaliana sulfate transporter atsultr4;1 (see paper)
22% identity, 95% coverage: 5:552/574 of query aligns to 12:559/575 of 7lhvA
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L126 (≠ S116), R127 (≠ G117), W130 (≠ R120)
- binding (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate: L128 (≠ M118), L131 (= L121), E409 (≠ V423), L413 (≠ A427), G417 (= G431), A421 (= A435)
- binding sulfate ion: A84 (= A81), S321 (≠ A334), F322 (≠ I335)
Q9URY8 Probable sulfate permease C869.05c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
27% identity, 64% coverage: 17:382/574 of query aligns to 115:479/840 of Q9URY8
Sites not aligning to the query:
- 823 modified: Phosphoserine
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, 79% coverage: 33:487/574 of query aligns to 102:563/758 of Q8CIW6
- F552 (= F476) mutation to A: Does not inhibit formate transport in PMA-induced cells.
8sieC Pendrin in complex with bicarbonate (see paper)
23% identity, 92% coverage: 23:552/574 of query aligns to 44:595/613 of 8sieC
- binding Lauryl Maltose Neopentyl Glycol: G198 (= G159), S296 (≠ R275), T300 (≠ G279), F303 (= F282)
- binding bicarbonate ion: Y65 (≠ L44), F101 (= F88), L356 (≠ I335), S357 (≠ A336), V403 (= V385), N406 (= N388)
- binding cholesterol: L226 (vs. gap), V255 (= V227), I262 (≠ F234), Y272 (≠ S242), F411 (vs. gap), V414 (≠ A392), V414 (≠ A392), C415 (≠ R393), C415 (≠ R393), I436 (≠ F414), M452 (vs. gap), F453 (vs. gap)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: W421 (≠ L399), V429 (= V407), V432 (≠ L410), F433 (≠ V411), I436 (≠ F414)
8shcC Pendrin in complex with niflumic acid (see paper)
23% identity, 92% coverage: 23:552/574 of query aligns to 44:595/613 of 8shcC
- binding cholesterol: I199 (≠ F161), A223 (vs. gap), V255 (= V227), Y272 (≠ S242), M412 (vs. gap), C415 (≠ R393), M452 (vs. gap), F453 (vs. gap)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: Q156 (≠ G117), W421 (≠ L399), V432 (≠ L410), F433 (≠ V411), F455 (≠ V423)
- binding 2-{[3-(trifluoromethyl)phenyl]amino}nicotinic acid: Y65 (≠ L44), F101 (= F88), T173 (= T134), E252 (≠ D224), I312 (= I290), L356 (≠ I335), S357 (≠ A336), V402 (= V384), N406 (= N388)
8sh3C Pendrin in complex with iodide (see paper)
23% identity, 92% coverage: 23:552/574 of query aligns to 44:595/613 of 8sh3C
- binding Lauryl Maltose Neopentyl Glycol: S114 (vs. gap), G198 (= G159), E297 (≠ D276), T300 (≠ G279), F303 (= F282)
- binding cholesterol: I199 (≠ F161), A223 (vs. gap), V255 (= V227), I258 (= I230), I262 (≠ F234), Y272 (≠ S242), F411 (vs. gap), V414 (≠ A392), C415 (≠ R393), V417 (≠ F395), I439 (≠ T417), M452 (vs. gap), F453 (vs. gap)
- binding iodide ion: Y65 (≠ L44), N406 (= N388)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: L155 (≠ S116), F159 (≠ R120), W421 (≠ L399), V429 (= V407), V432 (≠ L410), F433 (≠ V411), I436 (≠ F414), L451 (vs. gap), F455 (≠ V423), F464 (≠ L432), P465 (≠ A433)
8sgwC Pendrin in complex with chloride (see paper)
23% identity, 92% coverage: 23:552/574 of query aligns to 44:595/613 of 8sgwC
- binding Lauryl Maltose Neopentyl Glycol: G198 (= G159), S296 (≠ R275), T300 (≠ G279), F303 (= F282)
- binding chloride ion: Y65 (≠ L44), N406 (= N388)
- binding cholesterol: I228 (≠ G183), V255 (= V227), I262 (≠ F234), Y272 (≠ S242), K408 (≠ S390), F411 (vs. gap), M412 (vs. gap), M412 (vs. gap), V414 (≠ A392), C415 (≠ R393), V417 (≠ F395), I439 (≠ T417)
- binding 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine: F159 (≠ R120), Y163 (≠ F124), F284 (≠ V254), P286 (= P256), I289 (≠ L259), F343 (≠ A322), F346 (= F325), W421 (≠ L399), F433 (≠ V411), I436 (≠ F414), F455 (≠ V423), F464 (≠ L432), P465 (≠ A433)
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, 78% coverage: 33:480/574 of query aligns to 100:555/759 of Q9BXS9
- N167 (≠ G97) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- N172 (≠ A102) modified: carbohydrate, N-linked (GlcNAc) asparagine; mutation to Q: Reduced chloride oxalate exchanger activity.
- V206 (≠ L121) to M: in dbSNP:rs13324142
- ATV 547:549 (≠ GPL 472:474) mutation to NVN: Does not inhibit cell membrane localization. Inhibits interaction with CA2 and bicarbonate transport.
- N553 (≠ A478) 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.
7xulA Human slc26a3 in complex with tenidap
21% identity, 79% coverage: 23:477/574 of query aligns to 59:516/690 of 7xulA
- binding 5-chloranyl-2-oxidanyl-3-thiophen-2-ylcarbonyl-indole-1-carboxamide: V72 (= V36), L75 (≠ P39), Q76 (≠ L40), E262 (≠ A205), S367 (≠ A336), L412 (= L381), N416 (≠ V385)
- binding cholesterol hemisuccinate: I157 (≠ L108), F162 (≠ L113), P209 (≠ A158), K214 (≠ S163), Y217 (≠ A166), V302 (≠ F271), Q306 (≠ R275), V309 (≠ A278), V450 (≠ L419)
7xujA Human slc26a3 in complex with uk5099
21% identity, 79% coverage: 23:477/574 of query aligns to 66:525/703 of 7xujA
- binding (E)-2-cyano-3-(1-phenylindol-3-yl)prop-2-enoic acid: V79 (= V36), Q83 (≠ L40), E271 (≠ A205), S376 (≠ A336), R377 (= R337), V380 (≠ T340), L421 (= L381), A422 (≠ L382), N425 (≠ V385)
- binding cholesterol hemisuccinate: F171 (≠ L113), V311 (≠ F271), Q315 (≠ R275)
7ch1A The overall structure of slc26a9 (see paper)
22% identity, 91% coverage: 26:546/574 of query aligns to 53:602/640 of 7ch1A
- binding chloride ion: N76 (≠ G49), T106 (≠ P79), F107 (≠ T80), I110 (≠ F83), R141 (vs. gap), H357 (≠ I329), V358 (≠ T330)
- binding sodium ion: Q64 (≠ A37), G68 (≠ S41), S86 (≠ A59), G105 (= G78), T106 (≠ P79)
7xuhA Down-regulated in adenoma in complex with tqr1122
21% identity, 79% coverage: 23:477/574 of query aligns to 66:529/707 of 7xuhA
- binding 2-[4,8-dimethyl-2-oxidanylidene-7-[[3-(trifluoromethyl)phenyl]methoxy]chromen-3-yl]ethanoic acid: P124 (= P89), I125 (= I90), L187 (≠ I125), I192 (≠ V130), F195 (= F133), V335 (≠ E291), S338 (≠ L294), S380 (≠ A336), M433 (= M389)
- binding cholesterol hemisuccinate: V223 (≠ G159), F226 (≠ L162), K227 (≠ S163), Y230 (≠ A166), F318 (≠ I274), Q319 (≠ R275)
Q62273 Sulfate transporter; Diastrophic dysplasia protein homolog; ST-OB; Solute carrier family 26 member 2 from Mus musculus (Mouse) (see paper)
25% identity, 60% coverage: 26:370/574 of query aligns to 111:475/739 of Q62273
- F368 (≠ T229) mutation to A: Reduced sulfate-chloride exchange activity.
- E417 (= E312) mutation E->A,K: Loss of sulfate-chloride exchange activity.
P58735 Sulfate anion transporter 1; SAT-1; Solute carrier family 26 member 1 from Mus musculus (Mouse) (see paper)
24% identity, 80% coverage: 26:486/574 of query aligns to 72:563/704 of P58735
- T190 (= T103) mutation to M: Decreased sulfate-hydrogencarbonate exchange activity. Loss of localization to plasma membrane.
- S363 (≠ A285) 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)
20% identity, 91% coverage: 26:550/574 of query aligns to 71:651/680 of 7lguA
Query Sequence
>WP_043765232.1 NCBI__GCF_000733765.1:WP_043765232.1
MSFPPLFTALRASLKAGYGIATLRRDVLAGITVGTVAIPLSMALAIATGVPPQHGLYTAI
VAGAVAALTGGARFNVTGPTAAFVVILFPIVAEYGIGGLLVATLMAGLILVALGASGMGR
LVQFIPYPVVLGFTAGIALVIAVLQVPQFLGIADGEGAGHFLSGLASIGRSLPELEPLTL
ATGVITLATLLLWPRLQLPVPAPLAGLAVGAVAAWFFNAMQAGDAPVATIASQFEWTAEG
RSGSGIPPLAPGFVLPWRLPGADGAPLVVDFALIRDLAGPAFAIAMLAAIESLLCSVVAD
GMTRTRHDSNGELIGQGLSNLAAPFFGGITATAAIARTATGIRSGAQSPIAAIVHSLVVL
LAMLLLAPLLGLVPMSALAALLFVVAWNMSEARHFLHTLRSAPPGDVLVLVTCFGLTVLF
DMVLAVAVGIGLAAALFIRRMALLTSADRVRQEGAATTTRVPDSVALYDVNGPLFFAAAE
KALSTLRMVDPEVRTAIVDMHDVPSMDATAIVTLRSIIDEMQQHGVALIFVGLPTRIIAK
LRRAGIRKQPGRLGYCSSLDTALATIRRWEARGT
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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