SitesBLAST
Comparing WP_015817849.1 NCBI__GCF_000023025.1:WP_015817849.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
Q8N695 Sodium-coupled monocarboxylate transporter 1; Apical iodide transporter; Electrogenic sodium monocarboxylate cotransporter; Sodium iodide-related cotransporter; Solute carrier family 5 member 8 from Homo sapiens (Human) (see 3 papers)
28% identity, 88% coverage: 32:499/530 of query aligns to 39:552/610 of Q8N695
- V193 (≠ M189) to I: in dbSNP:rs1709189
- F251 (= F249) to V: in dbSNP:rs11834933
Sites not aligning to the query:
- 608 T→A: Loss of interaction with PDZK1.
- 608:610 PDZ-binding
- 610 L→A: Loss of interaction with PDZK1.
Q9Y289 Sodium-dependent multivitamin transporter; Na(+)-dependent multivitamin transporter; hSMVT; Solute carrier family 5 member 6 from Homo sapiens (Human) (see 10 papers)
32% identity, 85% coverage: 3:454/530 of query aligns to 21:465/635 of Q9Y289
- C68 (≠ A47) mutation to A: No effect on biotin transport.
- T78 (= T57) mutation to A: Reduced membrane localization. Decrease in biotin transport.
- C104 (≠ L82) mutation to A: No effect on biotin transport.
- R123 (≠ A105) to L: in SMVTD; reduced membrane localization; impaired biotin transport
- S128 (= S110) mutation to A: No effect on biotin transport.
- N138 (≠ D120) mutation to A: Reduced protein levels. Decrease in biotin transport.
- C144 (≠ V126) mutation to A: No effect on biotin transport.
- Y162 (= Y144) to C: in COMNB; no effect on membrane localization
- C187 (≠ T169) mutation to A: No effect on biotin transport.
- S242 (≠ Q223) mutation to A: No effect on biotin transport.
- S283 (≠ C267) mutation to A: No effect on protein levels or membrane localization.
- T286 (≠ S274) mutation to A: Resistant to phorbol 12-myristate 13-acetate (PMA)-induced inhibition of biotin transport. No effect on protein levels or membrane localization.
- C294 (≠ G282) mutation to A: Reduced membrane localization. Decrease in biotin transport (decreased Vmax, no change in Km).; mutation C->S,M: Decrease in biotin transport.
- C309 (= C293) mutation to A: No effect on biotin transport.
- C358 (≠ A345) mutation to A: No effect on biotin transport.
- T366 (≠ S353) mutation to A: No effect on biotin transport.
- R400 (= R388) to T: in SMVTD; impaired biotin transport; dbSNP:rs370950187
- C410 (≠ A398) mutation to A: No effect on biotin transport.
- S429 (≠ K418) to G: in COMNB; no effect on membrane localization
- C443 (≠ V432) mutation to A: No effect on biotin transport.
- C450 (≠ R439) mutation to A: No effect on biotin transport.
Sites not aligning to the query:
- 94:635 natural variant: Missing (in SMVTD and COMNB; reduced membrane localization; impaired biotin transport; dbSNP:rs994218778)
- 481 S → F: in dbSNP:rs1395
- 489 N→A: Slight decrease in protein levels. Decrease in biotin transport.
- 498 N→A: No effect on biotin transport.
- 534 N→A: No effect on biotin transport.
- 567:635 mutation Missing: Loss of biotin transport. Loss of membrane localization.
- 570:635 mutation Missing: Loss of biotin transport. Loss of membrane localization.
- 575:635 mutation Missing: Partial loss (75%) of biotine transport. Apical membrane localization and intracellular structure localization in polarized cells.
- 577 C→A: No effect on biotin transport.
- 583 C→A: No effect on biotin transport.
- 584:635 mutation Missing: Partial loss (75%) of biotine transport. Apical membrane localization and intracellular structure localization in polarized cells.
- 600:635 mutation Missing: Partial loss (75%) of biotine transport. Apical membrane localization and intracellular structure localization in polarized cells.
- 612:635 mutation Missing: Partial loss (75%) of biotine transport. Apical membrane localization and intracellular structure localization in polarized cells.
- 616:635 mutation Missing: Loss of apical membrane localization in polarized cells. Basolateral localization in polarized cells.
- 620:635 mutation Missing: Partial loss (25%) of biotine transport. No change in apical membrane localization in polarized cells.
- 624:635 mutation Missing: Partial loss (25%) of biotine transport. No change in apical membrane localization in polarized cells.
- 627 T→A: No effect on biotin transport.
- 628 mutation C->A,S: Decrease in biotin transport.
- 632:635 mutation Missing: Partial loss (25%) of biotine transport. No change in apical membrane localization in polarized cells.
7sl9A Cryoem structure of smct1 (see paper)
31% identity, 77% coverage: 44:453/530 of query aligns to 30:429/497 of 7sl9A
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)
30% identity, 78% coverage: 32:444/530 of query aligns to 41:444/643 of Q92911
- A102 (≠ M96) natural variant: A -> P
- H226 (≠ Q219) mutation H->A,D,E,K: Significant loss of iodide transport activity but no effect on its localization to the cell membrane.
- D237 (≠ H230) mutation to A: Loss of localization to the cell membrane, significant loss of iodide transport activity but no effect on homodimerization.
- Y242 (≠ F238) Required for homodimerization; mutation to 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.
- T243 (≠ A239) Required for homodimerization; mutation to 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.
Sites not aligning to the query:
- 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
B4EZY7 Sodium/sialic acid symporter SiaT; Na(+)-coupled sialic acid symporter; Sialic acid transporter from Proteus mirabilis (strain HI4320) (see paper)
28% identity, 92% coverage: 9:494/530 of query aligns to 9:485/496 of B4EZY7
- A56 (= A56) binding Na(+)
- T58 (≠ Q58) mutation to A: 2-fold increase in Neu5Ac transport.
- L59 (≠ C59) binding Na(+)
- S60 (= S60) mutation to A: Abolishes Neu5Ac transport.
- T63 (≠ S63) mutation to A: Abolishes Neu5Ac transport.
- Q82 (= Q83) mutation to D: Abolishes Neu5Ac transport.
- R135 (≠ A138) mutation to E: Abolishes Neu5Ac transport.
- D182 (= D185) binding Na(+); mutation to A: Abolishes Neu5Ac transport.
- A339 (= A349) binding Na(+)
- S342 (= S352) binding Na(+); binding Na(+); mutation to A: Abolishes Neu5Ac transport.
- S343 (= S353) binding Na(+); mutation to A: Abolishes Neu5Ac transport.
- S345 (≠ D355) binding Na(+); mutation to A: Reduces Neu5Ac transport.
- S346 (= S356) binding Na(+); mutation to 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)
28% identity, 92% coverage: 9:494/530 of query aligns to 5:477/480 of 5nv9A
- binding sodium ion: A52 (= A56), T53 (= T57), L55 (≠ C59), S56 (= S60), V174 (= V181), D178 (= D185), A335 (= A349), S338 (= S352), S338 (= S352), S339 (= S353), S341 (≠ D355), S342 (= S356)
- binding N-acetyl-beta-neuraminic acid: T54 (≠ Q58), S56 (= S60), I58 (≠ N62), T59 (≠ S63), G77 (≠ L82), Q78 (= Q83), R131 (≠ A138), F239 (= F248)
7uuzA Structure of the sodium/iodide symporter (nis) in complex with perrhenate and sodium (see paper)
28% identity, 86% coverage: 42:495/530 of query aligns to 26:491/501 of 7uuzA
P11170 Sodium/glucose cotransporter 1; Na(+)/glucose cotransporter 1; High affinity sodium-glucose cotransporter; Solute carrier family 5 member 1 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
28% identity, 81% coverage: 28:457/530 of query aligns to 48:497/662 of P11170
- C255 (≠ R221) modified: Disulfide link with 608
- Q457 (≠ N417) mutation to W: Drasticly decreased affinity for glucose and phlorizin.
- T460 (≠ G420) mutation to W: Decreased affinity for glucose and phlorizin.
Sites not aligning to the query:
- 608 modified: Disulfide link with 255
8hezA Structure of human sglt2-map17 complex with dapagliflozin (see paper)
27% identity, 83% coverage: 7:445/530 of query aligns to 2:465/582 of 8hezA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: N55 (≠ Q58), G59 (≠ N62), H60 (≠ S63), G63 (= G66), L64 (≠ F70), T67 (≠ F73), F78 (≠ Y84), E79 (= E85), V266 (≠ Y251), S267 (≠ V252), W271 (≠ G256), K301 (≠ R285), F433 (≠ A409), Q437 (≠ N417)
- binding sodium ion: A53 (= A56), I56 (≠ C59), G57 (≠ S60), A369 (= A349), S372 (= S352), S373 (= S353)
Sites not aligning to the query:
8hdhA Structure of human sglt2-map17 complex with canagliflozin (see paper)
27% identity, 83% coverage: 7:445/530 of query aligns to 2:465/586 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 (≠ Q58), G59 (≠ N62), H60 (≠ S63), G63 (= G66), L64 (≠ F70), F78 (≠ Y84), E79 (= E85), S267 (≠ V252), W271 (≠ G256), F433 (≠ A409), D434 (= D410), Q437 (≠ N417)
- binding sodium ion: A53 (= A56), S54 (≠ T57), I56 (≠ C59), G57 (≠ S60), A369 (= A349), S372 (= S352), S373 (= S353)
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: 506
- binding : 575, 579, 580, 583, 584
8hb0A Structure of human sglt2-map17 complex with ta1887 (see paper)
27% identity, 83% coverage: 7:445/530 of query aligns to 2:465/586 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 (≠ Q58), H60 (≠ S63), G63 (= G66), L64 (≠ F70), T67 (≠ F73), V75 (≠ W81), F78 (≠ Y84), E79 (= E85), V137 (= V141), V266 (≠ Y251), S267 (≠ V252), W271 (≠ G256), F433 (≠ A409), Q437 (≠ N417)
- binding sodium ion: A53 (= A56), I56 (≠ C59), G57 (≠ S60), A369 (= A349), S372 (= S352), S373 (= S353)
Sites not aligning to the query:
8hg7A Structure of human sglt2-map17 complex with sotagliflozin (see paper)
27% identity, 83% coverage: 7:445/530 of query aligns to 2:465/590 of 8hg7A
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[(4-ethoxyphenyl)methyl]phenyl]-6-methylsulfanyl-oxane-3,4,5-triol: N55 (≠ Q58), G59 (≠ N62), H60 (≠ S63), G63 (= G66), L64 (≠ F70), E79 (= E85), V266 (≠ Y251), S267 (≠ V252), Y270 (= Y255), W271 (≠ G256), K301 (≠ R285), F433 (≠ A409), Q437 (≠ N417)
- binding sodium ion: A53 (= A56), S54 (≠ T57), I56 (≠ C59), G57 (≠ S60), A369 (= A349), S372 (= S352), S373 (= S353)
Sites not aligning to the query:
7vsiA Structure of human sglt2-map17 complex bound with empagliflozin (see paper)
27% identity, 83% coverage: 7:445/530 of query aligns to 2:465/586 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 (≠ Q58), H60 (≠ S63), G63 (= G66), L64 (≠ F70), V75 (≠ W81), F78 (≠ Y84), E79 (= E85), V266 (≠ Y251), S267 (≠ V252), Y270 (= Y255), F433 (≠ A409), D434 (= D410), Q437 (≠ N417)
7sl8A Cryoem structure of sglt1 at 3.4 a resolution (see paper)
29% identity, 76% coverage: 43:445/530 of query aligns to 31:453/582 of 7sl8A
Sites not aligning to the query:
7slaA Cryoem structure of sglt1 at 3.15 angstrom resolution (see paper)
29% identity, 76% coverage: 43:445/530 of query aligns to 32:454/585 of 7slaA
Sites not aligning to the query:
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)
27% identity, 83% coverage: 7:445/530 of query aligns to 22:485/672 of P31639
- V95 (≠ W81) mutation to A: Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.
- F98 (≠ Y84) mutation to A: Slightly decreases D-glucose transporter activity. Abolishes the binding to inhibitor, empagliflozin.
- V157 (= V141) mutation to A: Decreases D-glucose transporter activity.
- L283 (≠ F248) mutation to M: Strong reduction in D-glucose transporter activity. Confers partial resistance to empagliflozin inhibition.
- F453 (≠ A409) mutation to A: Slightly decreases D-glucose transporter activity. Greatly reduces the binding to inhibitor, empagliflozin.
Q9NY91 Probable glucose sensor protein SLC5A4; Solute carrier family 5 member 4 from Homo sapiens (Human) (see paper)
27% identity, 78% coverage: 38:452/530 of query aligns to 58:492/659 of Q9NY91
- E457 (≠ K418) mutation to 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)
27% identity, 83% coverage: 7:445/530 of query aligns to 9:461/588 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 (= S53), A49 (= A56), S50 (≠ T57), G53 (≠ S60), D177 (= D185), T181 (≠ M189), R276 (= R264), S369 (= S353)
Sites not aligning to the query:
3dh4A Crystal structure of sodium/sugar symporter with bound galactose from vibrio parahaemolyticus (see paper)
27% identity, 77% coverage: 42:450/530 of query aligns to 19:426/512 of 3dh4A
7wmvA Structure of human sglt1-map17 complex bound with lx2761 (see paper)
29% identity, 79% coverage: 28:445/530 of query aligns to 31:468/602 of 7wmvA
- binding N-[2-(dimethylamino)ethyl]-2-methyl-2-[4-[4-[[2-methyl-5-[(2S,3R,4R,5S,6R)-6-methylsulfanyl-3,4,5-tris(oxidanyl)oxan-2-yl]phenyl]methyl]phenyl]butanoylamino]propanamide: N61 (≠ Q58), H66 (≠ S63), L70 (≠ A67), I81 (≠ G76), F84 (≠ L79), L257 (≠ F240), M266 (≠ F248), L269 (≠ Y251), T270 (≠ V252), Y273 (= Y255), W274 (≠ G256), F436 (≠ A409), D437 (= D410), Q440 (≠ N417)
Sites not aligning to the query:
Query Sequence
>WP_015817849.1 NCBI__GCF_000023025.1:WP_015817849.1
MAIATISPLDWLVIGFYLFGLISFSLYLSRKQHSRADYYVGGRSIGAWPIAISTMATQCS
TNSILGAPAFVAFSAGGGLIWLQYELAVPLAMLAIMIFLLPVFRAMNLVSVYEYLERRFD
LKTRLVLSGLFQFLRAFATSVTIYSIALVVELITGTTFLISVLILGAITLVYDVFGGVKG
VVYSDVLQMGILVVVLLMLFVILVGELGGLTGIFNGIPQERLQTLDFSHHGLGDGETFAF
WPMLIGGFFLYVSYYGCDQSQVQRELCAANIHESKKSLFLNGLLRFPLVLLYCLIGVGLG
SYAASHPEFIQQLPAEGGTPNYNVAVPLYMLQVLPMGLVGLALVALFAAAMSSLDSVINS
LSASTMEDFVRRLSSNAWSDETELWISRVVTLCWGSLAVVFSFYVGDIADSVLVAINKIG
SLINGPVLGVFVLGVFTRRCNGLGAVCGLCLGFVTNVLCWLYLPNVSWLWWNVIGLIVCM
LGGYLISIFAGCRQQRGEPFTVQLDWLNWRGRYGILVLYTLGIVGVLALL
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