SitesBLAST
Comparing WP_011842723.1 NCBI__GCF_000015985.1:WP_011842723.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
24% identity, 76% coverage: 64:499/576 of query aligns to 28:443/502 of P07117
- R257 (= R308) mutation to C: Sodium-independent binding affinity for proline.
- C281 (≠ F332) mutation to S: Does not affect proline uptake activity. Confers resistance to N-ethylmaleimide. Na(+)-dependent proline binding activity is similar to wild-type carrier.
- C344 (≠ G398) mutation to S: Small decrease in proline uptake activity. Confers resistance to N-ethylmaleimide. Exhibits low Na(+)-dependent proline binding.
- C349 (≠ G403) 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 (≠ F432) mutation R->E,Q: No change in activity.; mutation to K: Loss of activity.
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)
24% identity, 32% coverage: 45:226/576 of query aligns to 18:201/643 of Q92911
- A102 (≠ T126) natural variant: A -> P
Sites not aligning to the query:
- 226 mutation H->A,D,E,K: Significant loss of iodide transport activity but no effect on its localization to the cell membrane.
- 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)
21% identity, 70% coverage: 27:432/576 of query aligns to 9:428/672 of P31639
- V95 (vs. gap) mutation to A: Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.
- F98 (= F109) mutation to A: Slightly decreases D-glucose transporter activity. Abolishes the binding to inhibitor, empagliflozin.
- V157 (vs. gap) mutation to A: Decreases D-glucose transporter activity.
- L283 (≠ T299) mutation to M: Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.
Sites not aligning to the query:
- 453 F→A: Slightly decreases D-glucose transporter activity. Greatly reduces the binding to inhibitor, empagliflozin.
B4EZY7 Sodium/sialic acid symporter SiaT; Na(+)-coupled sialic acid symporter; Sialic acid transporter from Proteus mirabilis (strain HI4320) (see paper)
19% identity, 55% coverage: 40:354/576 of query aligns to 10:306/496 of B4EZY7
- A56 (≠ G89) binding Na(+)
- T58 (≠ Y91) mutation to A: 2-fold increase in Neu5Ac transport.
- L59 (≠ M92) binding Na(+)
- S60 (= S93) mutation to A: Abolishes Neu5Ac transport.
- T63 (≠ S96) mutation to A: Abolishes Neu5Ac transport.
- Q82 (≠ S115) mutation to D: Abolishes Neu5Ac transport.
- R135 (≠ Q173) mutation to E: Abolishes Neu5Ac transport.
- D182 (≠ Q216) binding Na(+); mutation to A: Abolishes Neu5Ac transport.
Sites not aligning to the query:
- 339 binding Na(+)
- 342 binding Na(+); binding Na(+); S→A: Abolishes Neu5Ac transport.
- 343 binding Na(+); S→A: Abolishes Neu5Ac transport.
- 345 binding Na(+); S→A: Reduces Neu5Ac transport.
- 346 binding Na(+); S→A: Slightly increases Neu5Ac transport.
5nv9A Substrate-bound outward-open state of a na+-coupled sialic acid symporter reveals a novel na+-site (see paper)
19% identity, 55% coverage: 40:354/576 of query aligns to 6:302/480 of 5nv9A
- binding sodium ion: A52 (≠ G89), T53 (≠ D90), L55 (≠ M92), S56 (= S93), V174 (≠ T212), D178 (≠ Q216)
- binding N-acetyl-beta-neuraminic acid: T54 (≠ Y91), S56 (= S93), I58 (≠ A95), T59 (≠ S96), G77 (≠ Y114), Q78 (≠ S115), R131 (≠ Q173), F239 (= F291)
Sites not aligning to the query:
8hg7A Structure of human sglt2-map17 complex with sotagliflozin (see paper)
21% identity, 68% coverage: 40:432/576 of query aligns to 2:408/590 of 8hg7A
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-methylsulfanyl-oxane-3,4,5-triol: N55 (≠ Y91), G59 (≠ A95), H60 (≠ S96), G63 (= G99), L64 (≠ I100), E79 (≠ D110), V266 (≠ L306), S267 (≠ M307), Y270 (≠ F310), W271 (≠ T311), K301 (≠ A343)
- binding sodium ion: A53 (≠ G89), S54 (≠ D90), I56 (≠ M92), G57 (≠ S93), A369 (≠ T391), S372 (≠ A394), S373 (≠ V395)
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: 433, 437
- binding : 579, 583, 584, 587, 588
8hezA Structure of human sglt2-map17 complex with dapagliflozin (see paper)
21% identity, 68% coverage: 40:432/576 of query aligns to 2:408/582 of 8hezA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (≠ Y91), G59 (≠ A95), H60 (≠ S96), G63 (= G99), L64 (≠ I100), T67 (≠ A103), F78 (= F109), E79 (≠ D110), V266 (≠ L306), S267 (≠ M307), W271 (≠ T311), K301 (≠ A343)
- binding sodium ion: A53 (≠ G89), I56 (≠ M92), G57 (≠ S93), A369 (≠ T391), S372 (≠ A394), S373 (≠ V395)
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: 433, 437
- binding : 568, 571, 572, 575, 576, 579, 580
8hdhA Structure of human sglt2-map17 complex with canagliflozin (see paper)
21% identity, 68% coverage: 40:432/576 of query aligns to 2:408/586 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 (≠ Y91), G59 (≠ A95), H60 (≠ S96), G63 (= G99), L64 (≠ I100), F78 (= F109), E79 (≠ D110), S267 (≠ M307), W271 (≠ T311)
- binding sodium ion: A53 (≠ G89), S54 (≠ D90), I56 (≠ M92), G57 (≠ S93), A369 (≠ T391), S372 (≠ A394), S373 (≠ V395)
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: 433, 434, 437, 506
- binding : 575, 579, 580, 583, 584
8hb0A Structure of human sglt2-map17 complex with ta1887 (see paper)
21% identity, 68% coverage: 40:432/576 of query aligns to 2:408/586 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 (≠ Y91), H60 (≠ S96), G63 (= G99), L64 (≠ I100), T67 (≠ A103), V75 (vs. gap), F78 (= F109), E79 (≠ D110), V137 (vs. gap), V266 (≠ L306), S267 (≠ M307), W271 (≠ T311)
- binding sodium ion: A53 (≠ G89), I56 (≠ M92), G57 (≠ S93), A369 (≠ T391), S372 (≠ A394), S373 (≠ V395)
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: 433, 437
- binding : 575, 576, 579, 580, 583, 584
7vsiA Structure of human sglt2-map17 complex bound with empagliflozin (see paper)
21% identity, 68% coverage: 40:432/576 of query aligns to 2:408/586 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 (≠ Y91), H60 (≠ S96), G63 (= G99), L64 (≠ I100), V75 (vs. gap), F78 (= F109), E79 (≠ D110), V266 (≠ L306), S267 (≠ M307), Y270 (≠ F310)
Sites not aligning to the query:
Query Sequence
>WP_011842723.1 NCBI__GCF_000015985.1:WP_011842723.1
MSRLTSSRRLAVVMAALILLPTLALAAGPDLGEVQKQATNYTAIGMFAAFVVFTLFITKW
AAAKTKSAADFYTAGGGITGFQNGLAIAGDYMSAASFLGISAAVMASGFDGLIYSIGFLV
GWPILTFLMAERLRNLGQFTFADVAAFRFAQTPVRVFAASSTLVVVAFYLIAQMVGAGQL
IKLLFGLEYWVAVVIVGGLMMIYVLFGGMTATTWVQIIKACLLLGGATFMAVMVMMQYGF
SLERFFAAAVEVKAQIAAQTPGTTPEDAAAAGQSIMGPGKFITDPISAISFGMALMFGTA
GLPHILMRFFTVPDAKEARKSVMWATTWIGYFYLLTFIIGFGAITFVLTNPGFLDETGAL
VGGSNMAAIHLAKAVGGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDIYATVIKKNK
AGSAAELKVSRFTVLALGVLAVALGIVFEKQNIAFMVSLAFAIAASANFPVLFLSVLWKG
CTTRGVVIGGFIGLVVSVVLTVLSPSVWEATLGYDKGSAPFPYTSPALFSMTAGFVGIWL
FSTLDRSLRGRQDRAGFVAQQVRSETGIGAAAASAH
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