SitesBLAST
Comparing 5210043 Shew_2490 anion transporter (RefSeq) to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 8 hits to proteins with known functional sites (download)
6okzB Structure of vcindy bound to fumarate
62% identity, 96% coverage: 19:461/463 of query aligns to 1:443/444 of 6okzB
7t9gA Structure of vcindy-na+ (see paper)
62% identity, 96% coverage: 19:461/463 of query aligns to 2:444/445 of 7t9gA
6wtxA Structure of vcindy in complex with terephthalate (see paper)
62% identity, 96% coverage: 19:461/463 of query aligns to 2:444/445 of 6wtxA
- binding sodium ion: S129 (= S146), S133 (= S150), N134 (= N151), G176 (= G193), G182 (= G199), T356 (= T373), A359 (= A376), S360 (= S377), N361 (= N378), A403 (= A420)
- binding terephthalic acid: N134 (= N151), S183 (= S200), S360 (= S377), N361 (= N378), T362 (= T379), T404 (= T421)
4f35B Crystal structure of a bacterial dicarboxylate/sodium symporter (see paper)
60% identity, 96% coverage: 19:461/463 of query aligns to 1:413/414 of 4f35B
7jsjA Structure of the nact-pf2 complex (see paper)
29% identity, 87% coverage: 51:455/463 of query aligns to 29:448/468 of 7jsjA
- binding sodium ion: S124 (= S146), I127 (= I149), S128 (= S150), N129 (= N151), G172 (= G199), T366 (= T373), T369 (≠ A376), S370 (= S377), N371 (= N378), A413 (= A420), T414 (= T421)
- binding (2R)-2-[2-(4-tert-butylphenyl)ethyl]-2-hydroxybutanedioic acid: N129 (= N151), T130 (= T152), T173 (≠ S200), G315 (= G321), I316 (≠ V322), N371 (= N378)
Q86YT5 Na(+)/citrate cotransporter; NaCT; Sodium-coupled citrate transporter; Sodium-dependent citrate transporter; Solute carrier family 13 member 5 from Homo sapiens (Human) (see 5 papers)
27% identity, 87% coverage: 51:455/463 of query aligns to 41:542/568 of Q86YT5
- T142 (= T152) to M: in DEE25; no loss of localization to plasma membrane; loss of function in citrate transport; dbSNP:rs761917087
- G219 (= G192) to E: loss of localization to plasma membrane; loss of function in citrate transport; dbSNP:rs150024888; to R: in DEE25; loss of function in citrate transport; loss of localization to plasma membrane; dbSNP:rs144332569
- T227 (≠ S200) to M: in DEE25; loss of function in citrate transport; no effect on localization to plasma membrane; dbSNP:rs587777577
- D243 (vs. gap) to N: no effect on localization to plasma membrane; no effect on its function in citrate transport; dbSNP:rs142262032
- G409 (= G321) mutation to Q: No effect on its function in citrate transport.
- I410 (≠ V322) mutation I->A,F: Significant loss of function in citrate transport.; mutation to V: No effect on its function in citrate transport.
- L420 (= L332) to P: loss of localization to plasma membrane; loss of function in citrate transport; dbSNP:rs150738356
- S427 (≠ T339) to L: in DEE25; loss of localization to plasma membrane; loss of function in citrate transport; dbSNP:rs548065551
- L485 (= L398) to R: no effect on localization to plasma membrane; reduced function in citrate transport; increased Km and Vmax values compared with that of wild type with citrate as substrate; dbSNP:rs148049520
- L488 (≠ V401) to P: in DEE25; loss of function in citrate transport; loss of localization to plasma membrane; dbSNP:rs587777578
- D524 (≠ E437) to H: in DEE25; loss of function in citrate transport; no effect on localization to plasma membrane; dbSNP:rs863225448
Sites not aligning to the query:
- 341:568 natural variant: Missing (in DEE25; loss of localization to plasma membrane; loss of function in citrate transport)
- 562 modified: carbohydrate, N-linked (GlcNAc...) asparagine
Q28615 Solute carrier family 13 member 2; Na(+)/dicarboxylate cotransporter 1; NaDC-1; Renal sodium/dicarboxylate cotransporter from Oryctolagus cuniculus (Rabbit) (see paper)
27% identity, 87% coverage: 52:453/463 of query aligns to 42:554/593 of Q28615
- L83 (≠ A93) mutation to C: Decreases cell membrane expression. Decreases succinate transport activity. Decreases Km value for succinate.
- T86 (≠ I96) mutation to C: Does not affect cell membrane localization. Decreases succinate transport activity.
- Y228 (= Y187) mutation to C: Does not affect cell membrane localization. Decreases succinate transport activity.
- Y432 (≠ L330) mutation to C: Does not affect cell membrane localization. Decreases succinate transport activity. Decreases Km value for succinate. More sensitive to inhibition by lithium.
- T474 (= T373) mutation to C: Does not affect cell membrane localization. Abolishes succinate transport activity.
- N525 (= N424) mutation to C: Decreases cell membrane expression. Decreases succinate transport activity.
- M539 (= M438) mutation to C: Does not affect cell membrane localization. Decreases succinate transport activity. Insensitive to inhibition by lithium.
Q10SY9 Silicon efflux transporter LSI2; Low silicon protein 2 from Oryza sativa subsp. japonica (Rice) (see paper)
25% identity, 37% coverage: 70:240/463 of query aligns to 40:197/472 of Q10SY9
- S115 (= S146) mutation to N: In lsi2; impairs silicon uptake. Reduced growth. Grain discoloration. Reduces grain yield 2.5-fold.
Query Sequence
>5210043 Shew_2490 anion transporter (RefSeq)
MSLDTTQEAIAAPPKQAAQTNLPILFGDIVLFALLYNFLPFEPGVNTGIAILVFAAVLWL
TEAIHISVTAILIPIMGVLLGVFETKAAMSNFANPIIYLFFGGFVLAAALNHQGIDRRIA
QKVLTASKGKLSIACMLLFGITALLSMWISNTATAAMMLPLALGILRQLDFKEHRSTYLF
MLLGIAYSANIGGIGTLVGSPPNAIAAAQVGLSFADWLEFGLLTVALMLPSMLIALYIYL
KPNLNVVCEIPKSNEQLALQGKLTLLIFLTTVCCWIFSKPISNALGGIKQFDTIVALGSV
VMLAGLGLVDWKKIEKTTDWGVLILFGGGLTLSAILKTTGTSVFLAHWVTDIFGNTHMAL
FTFAVIFFVVMLTEFASNTASAALLVPVFAAIAEALGLSPVMLSVLIGIAASCAFMLPVA
TPPNAIVYGSGFIKQSEMMRAGVIINFISMLALYVIAHLFWTI
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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