SitesBLAST
Comparing Echvi_3555 Echvi_3555 anion transporter to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 7 hits to proteins with known functional sites (download)
7jsjA Structure of the nact-pf2 complex (see paper)
41% identity, 91% coverage: 44:484/485 of query aligns to 33:464/468 of 7jsjA
- binding sodium ion: S124 (= S135), I127 (= I138), S128 (= S139), N129 (= N140), G172 (= G192), T366 (= T384), T369 (= T387), S370 (= S388), N371 (= N389), A413 (= A431), T414 (= T432)
- binding (2R)-2-[2-(4-tert-butylphenyl)ethyl]-2-hydroxybutanedioic acid: N129 (= N140), T130 (= T141), T173 (= T193), G315 (= G333), I316 (= I334), N371 (= N389)
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)
36% identity, 91% coverage: 44:484/485 of query aligns to 45:558/568 of Q86YT5
- T142 (= T141) to M: in DEE25; no loss of localization to plasma membrane; loss of function in citrate transport; dbSNP:rs761917087
- G219 (= G185) 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 (= T193) to M: in DEE25; loss of function in citrate transport; no effect on localization to plasma membrane; dbSNP:rs587777577
- D243 (≠ I209) to N: no effect on localization to plasma membrane; no effect on its function in citrate transport; dbSNP:rs142262032
- G409 (= G333) mutation to Q: No effect on its function in citrate transport.
- I410 (= I334) mutation I->A,F: Significant loss of function in citrate transport.; mutation to V: No effect on its function in citrate transport.
- L420 (= L344) to P: loss of localization to plasma membrane; loss of function in citrate transport; dbSNP:rs150738356
- S427 (≠ T351) to L: in DEE25; loss of localization to plasma membrane; loss of function in citrate transport; dbSNP:rs548065551
- L485 (≠ V409) 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 (≠ Y412) to P: in DEE25; loss of function in citrate transport; loss of localization to plasma membrane; dbSNP:rs587777578
- D524 (≠ A448) 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)
35% identity, 94% coverage: 27:484/485 of query aligns to 32:572/593 of Q28615
- L83 (≠ A82) mutation to C: Decreases cell membrane expression. Decreases succinate transport activity. Decreases Km value for succinate.
- T86 (≠ K85) mutation to C: Does not affect cell membrane localization. Decreases succinate transport activity.
- Y228 (= Y180) mutation to C: Does not affect cell membrane localization. Decreases succinate transport activity.
- Y432 (≠ L342) 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 (= T384) mutation to C: Does not affect cell membrane localization. Abolishes succinate transport activity.
- N525 (= N435) mutation to C: Decreases cell membrane expression. Decreases succinate transport activity.
- M539 (= M449) mutation to C: Does not affect cell membrane localization. Decreases succinate transport activity. Insensitive to inhibition by lithium.
7t9gA Structure of vcindy-na+ (see paper)
35% identity, 95% coverage: 5:465/485 of query aligns to 1:437/445 of 7t9gA
6wtxA Structure of vcindy in complex with terephthalate (see paper)
35% identity, 95% coverage: 5:465/485 of query aligns to 1:437/445 of 6wtxA
- binding sodium ion: S129 (= S135), S133 (= S139), N134 (= N140), G176 (= G186), G182 (= G192), T356 (= T384), A359 (≠ T387), S360 (= S388), N361 (= N389), A403 (= A431)
- binding terephthalic acid: N134 (= N140), S183 (≠ T193), S360 (= S388), N361 (= N389), T362 (≠ V390), T404 (= T432)
6okzB Structure of vcindy bound to fumarate
35% identity, 95% coverage: 7:465/485 of query aligns to 2:436/444 of 6okzB
4f35B Crystal structure of a bacterial dicarboxylate/sodium symporter (see paper)
34% identity, 95% coverage: 7:465/485 of query aligns to 2:406/414 of 4f35B
Query Sequence
>Echvi_3555 Echvi_3555 anion transporter
MNNLLWKRSGLVLGPVAFLLIVLFFNPDGLTYEAQAVLALAVWMAIWWILEAIPIAATAL
LPLVILPLTGALSMDESAAPYADPKVLLYMGGFMIAVTIEKWNLHKRIALSIISLIGTDM
RFIVLGFMLATALLSMWISNTATSLMMLPIAVAVIHQLADGSDEISATRIGQALMLGIAY
SASIGGLATIIGTPTNIVLVGIVKELYGIEIGFAEWMLVGLPISLGLLGICWWYLVSVAY
PFPKNMSLAGGKVEIQRQLAAIGPISKPEIRVLLVFLLVSFSWITRVFLQDLLPFLNDTI
IALVGVLLLFMLPSSRGKKRLLDWKTAEDIPWGILLLFGGGLALAAGFKETGLAAWLGSH
FEALQGVHFLLFILIIVASVNFLTEITSNVATASMLLPILGAVALALGVHPYGLMVAATM
AASCAFMLPVATPPNAVVFGSGYLTIPAMAKAGLWMNILSIFFITLFVYYIMPFLWGIDL
KVYPF
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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