SitesBLAST
Comparing WP_086508553.1 NCBI__GCF_002151265.1:WP_086508553.1 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 10 hits to proteins with known functional sites (download)
P07117 Sodium/proline symporter; Proline carrier; Proline permease; Propionate transporter from Escherichia coli (strain K12) (see 4 papers)
26% identity, 32% coverage: 390:581/598 of query aligns to 320:501/502 of P07117
- C344 (≠ G421) mutation to S: Small decrease in proline uptake activity. Confers resistance to N-ethylmaleimide. Exhibits low Na(+)-dependent proline binding.
- C349 (≠ I426) mutation to S: Does not affect proline uptake activity. Sensitive to N-ethylmaleimide. Na(+)-dependent proline binding activity is similar to wild-type carrier.
- R376 (= R453) mutation R->E,Q: No change in activity.; mutation to K: Loss of activity.
Sites not aligning to the query:
- 257 R→C: Sodium-independent binding affinity for proline.
- 281 C→S: Does not affect proline uptake activity. Confers resistance to N-ethylmaleimide. Na(+)-dependent proline binding activity is similar to wild-type carrier.
Q92911 Sodium/iodide cotransporter; Na(+)/I(-) cotransporter; Natrium iodide transporter; Sodium-iodide symporter; Na(+)/I(-) symporter; Solute carrier family 5 member 5 from Homo sapiens (Human) (see 3 papers)
25% identity, 34% coverage: 13:216/598 of query aligns to 18:228/643 of Q92911
- A102 (= A88) natural variant: A -> P
- H226 (= H214) mutation H->A,D,E,K: Significant loss of iodide transport activity but no effect on its localization to the cell membrane.
Sites not aligning to the query:
- 237 D→A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization.
- 242 Required for homodimerization; Y→A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization; when associated with A-471. Loss of iodide transport activity; when associated with F-535.
- 243 Required for homodimerization; T→A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Reduced homodimerization; when associated with A-471.
- 471 Required for homodimerization; Q→A: No effect on localization to the cell membrane, iodide transport activity and homodimerization. Significant loss of homodimerization; when associated with A-242 or A243.
- 525 A→F: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization. Loss of iodide transport activity; when associated with A-242.
- 536 T → Q: requires 2 nucleotide substitutions
- 556 S → Q: requires 2 nucleotide substitutions
P31639 Sodium/glucose cotransporter 2; Na(+)/glucose cotransporter 2; Low affinity sodium-glucose cotransporter; Solute carrier family 5 member 2 from Homo sapiens (Human) (see paper)
25% identity, 30% coverage: 7:186/598 of query aligns to 25:209/672 of P31639
- V95 (≠ N73) mutation to A: Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.
- F98 (= F76) mutation to A: Slightly decreases D-glucose transporter activity. Abolishes the binding to inhibitor, empagliflozin.
- V157 (≠ G134) mutation to A: Decreases D-glucose transporter activity.
Sites not aligning to the query:
- 283 L→M: Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.
- 453 F→A: Slightly decreases D-glucose transporter activity. Greatly reduces the binding to inhibitor, empagliflozin.
8hdhA Structure of human sglt2-map17 complex with canagliflozin (see paper)
25% identity, 30% coverage: 7:186/598 of query aligns to 5:189/586 of 8hdhA
- binding (2~{S},3~{R},4~{R},5~{S},6~{R})-2-[3-[[5-(4-fluorophenyl)thiophen-2-yl]methyl]-4-methyl-phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (≠ W53), G59 (≠ A57), H60 (≠ S58), G63 (≠ S61), L64 (≠ M62), F78 (= F76), E79 (≠ G79)
- binding sodium ion: A53 (= A51), S54 (≠ D52), I56 (≠ M54), G57 (≠ S55)
Sites not aligning to the query:
- binding (2~{S},3~{R},4~{R},5~{S},6~{R})-2-[3-[[5-(4-fluorophenyl)thiophen-2-yl]methyl]-4-methyl-phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: 267, 271, 433, 434, 437, 506
- binding sodium ion: 369, 372, 373
- binding : 575, 579, 580, 583, 584
8hb0A Structure of human sglt2-map17 complex with ta1887 (see paper)
25% identity, 30% coverage: 7:186/598 of query aligns to 5:189/586 of 8hb0A
- binding (2R,3R,4S,5S,6R)-2-[3-[(4-cyclopropylphenyl)methyl]-4-fluoranyl-indol-1-yl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (≠ W53), H60 (≠ S58), G63 (≠ S61), L64 (≠ M62), T67 (≠ L65), V75 (≠ N73), F78 (= F76), E79 (≠ G79), V137 (≠ G134)
- binding sodium ion: A53 (= A51), I56 (≠ M54), G57 (≠ S55)
Sites not aligning to the query:
- binding (2R,3R,4S,5S,6R)-2-[3-[(4-cyclopropylphenyl)methyl]-4-fluoranyl-indol-1-yl]-6-(hydroxymethyl)oxane-3,4,5-triol: 266, 267, 271, 433, 437
- binding sodium ion: 369, 372, 373
- binding : 575, 576, 579, 580, 583, 584
7vsiA Structure of human sglt2-map17 complex bound with empagliflozin (see paper)
25% identity, 30% coverage: 7:186/598 of query aligns to 5:189/586 of 7vsiA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[[4-[(3S)-oxolan-3-yl]oxyphenyl]methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (≠ W53), H60 (≠ S58), G63 (≠ S61), L64 (≠ M62), V75 (≠ N73), F78 (= F76), E79 (≠ G79)
Sites not aligning to the query:
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[[4-[(3S)-oxolan-3-yl]oxyphenyl]methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: 266, 267, 270, 433, 434, 437
8hg7A Structure of human sglt2-map17 complex with sotagliflozin (see paper)
25% identity, 30% coverage: 7:186/598 of query aligns to 5:189/590 of 8hg7A
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-methylsulfanyl-oxane-3,4,5-triol: N55 (≠ W53), G59 (≠ A57), H60 (≠ S58), G63 (≠ S61), L64 (≠ M62), E79 (≠ G79)
- binding sodium ion: A53 (= A51), S54 (≠ D52), I56 (≠ M54), G57 (≠ S55)
Sites not aligning to the query:
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-methylsulfanyl-oxane-3,4,5-triol: 266, 267, 270, 271, 301, 433, 437
- binding sodium ion: 369, 372, 373
- binding : 579, 583, 584, 587, 588
8hezA Structure of human sglt2-map17 complex with dapagliflozin (see paper)
25% identity, 30% coverage: 7:186/598 of query aligns to 5:189/582 of 8hezA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (≠ W53), G59 (≠ A57), H60 (≠ S58), G63 (≠ S61), L64 (≠ M62), T67 (≠ L65), F78 (= F76), E79 (≠ G79)
- binding sodium ion: A53 (= A51), I56 (≠ M54), G57 (≠ S55)
Sites not aligning to the query:
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: 266, 267, 271, 301, 433, 437
- binding sodium ion: 369, 372, 373
- binding : 568, 571, 572, 575, 576, 579, 580
Q9NY91 Probable glucose sensor protein SLC5A4; Solute carrier family 5 member 4 from Homo sapiens (Human) (see paper)
23% identity, 38% coverage: 15:240/598 of query aligns to 36:261/659 of Q9NY91
Sites not aligning to the query:
- 457 E→Q: Confers sugar transport activity not found in the wild-type protein. Increased sensitivity to inhibitor phlorizin.
8hinA Structure of human sglt2-map17 complex with phlorizin (see paper)
24% identity, 30% coverage: 7:186/598 of query aligns to 12:185/588 of 8hinA
- binding 1-[2-[(2S,3R,4S,5S,6R)-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-4,6-bis(oxidanyl)phenyl]-3-(4-hydroxyphenyl)propan-1-one: S46 (≠ G39), A49 (≠ P42), S50 (≠ V43), G53 (= G46), D177 (≠ Q178), T181 (≠ Y182)
Sites not aligning to the query:
- binding 1-[2-[(2S,3R,4S,5S,6R)-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-4,6-bis(oxidanyl)phenyl]-3-(4-hydroxyphenyl)propan-1-one: 276, 369
- binding : 574, 578, 581, 582, 585, 586
Query Sequence
>WP_086508553.1 NCBI__GCF_002151265.1:WP_086508553.1
MSQFAINLLFVGGSFALYIGIAIWARAGSTKDFYVAGGGVHPVTNGMATAADWMSAASFI
SMAGLLASGGYANSTFLMGWTGGYVILAMLLAPYLRKFGKFTVPDFIGDRFYSKTARVVA
VICLIVASVTYVIGQMTGAGVAFSRFLEVPSSTGIWIAAGIVFLYAVFGGMKGITYTQVA
QYIVLIIAYTIPAVFIAMQLTGNPIPMFGMFSTHTESGVPLLAKLDEVVTALGFRDYTAD
VDNKLNMVLFTLSLMIGTAGLPHVIIRFFTVPKVADARWSAGWALVFIALLYLTAPAVGS
MARLNLATTIFPEMAGQVEDYQEALANPILYEERPDWIRTWEDTGLITFTDRNNDGRIQM
YNDANPGFQPIASELGWEGNELTVNNDILVLANPEIANLPGWVIGLIAAGGIAAALSTAA
GLLLAISSAISHDLIKNTINPSISEKGEMLAARISMAGAILLATYLGLNPPGFAAQVVAL
AFGIAAASLFPVLMMGIFSTRMNSKGAICGMLAGLISTLLYIFTYLGWFFIPGTNMLANV
EANWLLGISPLSFGAVGAMINFAVAYAVSSATEEPPQEIQELVESVRYPKGAGAATGH
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