SitesBLAST
Comparing 7023217 FitnessBrowser__ANA3:7023217 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)
7t9gA Structure of vcindy-na+ (see paper)
61% identity, 95% coverage: 22:465/466 of query aligns to 2:445/445 of 7t9gA
6wtxA Structure of vcindy in complex with terephthalate (see paper)
61% identity, 95% coverage: 22:465/466 of query aligns to 2:445/445 of 6wtxA
- binding sodium ion: S129 (= S149), S133 (= S153), N134 (= N154), G176 (= G196), G182 (= G202), T356 (= T376), A359 (= A379), S360 (= S380), N361 (= N381), A403 (= A423)
- binding terephthalic acid: N134 (= N154), S183 (= S203), S360 (= S380), N361 (= N381), T362 (= T382), T404 (= T424)
6okzB Structure of vcindy bound to fumarate
61% identity, 95% coverage: 22:465/466 of query aligns to 1:444/444 of 6okzB
4f35B Crystal structure of a bacterial dicarboxylate/sodium symporter (see paper)
59% identity, 95% coverage: 22:465/466 of query aligns to 1:414/414 of 4f35B
7jsjA Structure of the nact-pf2 complex (see paper)
31% identity, 88% coverage: 54:463/466 of query aligns to 29:453/468 of 7jsjA
- binding sodium ion: S124 (= S149), I127 (= I152), S128 (= S153), N129 (= N154), G172 (= G202), T366 (= T376), T369 (≠ A379), S370 (= S380), N371 (= N381), A413 (= A423), T414 (= T424)
- binding (2R)-2-[2-(4-tert-butylphenyl)ethyl]-2-hydroxybutanedioic acid: N129 (= N154), T130 (= T155), T173 (≠ S203), G315 (= G324), I316 (≠ V325), N371 (= N381)
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, 88% coverage: 54:463/466 of query aligns to 41:547/568 of Q86YT5
- T142 (= T155) to M: in DEE25; no loss of localization to plasma membrane; loss of function in citrate transport; dbSNP:rs761917087
- G219 (= G195) 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 (≠ S203) 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 (= G324) mutation to Q: No effect on its function in citrate transport.
- I410 (≠ V325) mutation I->A,F: Significant loss of function in citrate transport.; mutation to V: No effect on its function in citrate transport.
- L420 (= L335) to P: loss of localization to plasma membrane; loss of function in citrate transport; dbSNP:rs150738356
- S427 (≠ T342) to L: in DEE25; loss of localization to plasma membrane; loss of function in citrate transport; dbSNP:rs548065551
- L485 (≠ V401) 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 (≠ V404) to P: in DEE25; loss of function in citrate transport; loss of localization to plasma membrane; dbSNP:rs587777578
- D524 (≠ E440) 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)
26% identity, 86% coverage: 55:456/466 of query aligns to 42:554/593 of Q28615
- L83 (≠ A96) mutation to C: Decreases cell membrane expression. Decreases succinate transport activity. Decreases Km value for succinate.
- T86 (≠ I99) mutation to C: Does not affect cell membrane localization. Decreases succinate transport activity.
- Y228 (= Y190) mutation to C: Does not affect cell membrane localization. Decreases succinate transport activity.
- Y432 (≠ L333) 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 (= T376) mutation to C: Does not affect cell membrane localization. Abolishes succinate transport activity.
- N525 (= N427) mutation to C: Decreases cell membrane expression. Decreases succinate transport activity.
- M539 (= M441) 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)
26% identity, 40% coverage: 73:260/466 of query aligns to 40:221/472 of Q10SY9
- S115 (= S149) mutation to N: In lsi2; impairs silicon uptake. Reduced growth. Grain discoloration. Reduces grain yield 2.5-fold.
Query Sequence
>7023217 FitnessBrowser__ANA3:7023217
MSLEQSKSVPPNHSSANVGLEKKKMLILVADIFLLFALYYGLPFDQGVNTGLAILVFAAI
LWLTEAIHISITAILVPILAVFFGVFETKEAMSNFANPIIYLFFGGFVLAAALHHQKIDT
LIAQKLLLASKGKLSIACLMLFGVTALLSMWISNTATTAMMLPLALGILQQLDRKLYHST
YVFLLLGIAYSANIGGIGTLVGSPPNAIAAAQVGLSFSDWLKFGIPTVILMLPMMLLALY
WYFKPDLSAKCELAVEDQKLTFQGKLTLVIFLATVCCWIFSVPLAKALGGITQFDTVVAL
GAVVLLAGLGLVGWKKIESTTDWGVLILFGGGLTLSAVLKSTGTSVFLAHWMTDIFGSTH
MSLFVFAVIAFVVMLTEFASNTASAALLVPVFAAIAEALGVSPVMLSVLIGIAASCAFML
PVATPPNAIVYGSGHIKQSEMVRVGMIINFLSMIVLGIIAHTFWEV
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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