SitesBLAST
Comparing RR42_RS06400 FitnessBrowser__Cup4G11:RR42_RS06400 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 3 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)
29% identity, 80% coverage: 39:475/546 of query aligns to 11:443/502 of P07117
- R257 (= R284) mutation to C: Sodium-independent binding affinity for proline.
- C281 (≠ G308) 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 (≠ G374) mutation to S: Small decrease in proline uptake activity. Confers resistance to N-ethylmaleimide. Exhibits low Na(+)-dependent proline binding.
- C349 (≠ G379) 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 (= R407) mutation R->E,Q: No change in activity.; mutation to K: Loss of activity.
5nv9A Substrate-bound outward-open state of a na+-coupled sialic acid symporter reveals a novel na+-site (see paper)
19% identity, 71% coverage: 34:422/546 of query aligns to 5:389/480 of 5nv9A
- binding sodium ion: A52 (≠ G81), T53 (≠ D82), L55 (≠ M84), S56 (= S85), V174 (≠ T204), D178 (≠ Q208), A335 (≠ T367), S338 (≠ A370), S338 (≠ A370), S339 (≠ V371), S341 (≠ A373), S342 (≠ G374)
- binding N-acetyl-beta-neuraminic acid: T54 (≠ Y83), S56 (= S85), I58 (≠ A87), T59 (≠ S88), G77 (≠ Y106), Q78 (≠ S107), R131 (≠ Q165), F239 (vs. gap)
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)
23% identity, 30% coverage: 57:218/546 of query aligns to 41:201/643 of Q92911
- A102 (≠ L118) 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
Query Sequence
>RR42_RS06400 FitnessBrowser__Cup4G11:RR42_RS06400
MKQANLCAIGAALLLTALPAFAAPGSVGQGMNVIAIAMFLMFVAATLVVTRWAARSNHSV
ADHYAAGGKITALQNGWAIAGDYMSAASLLGISALVFTSGYDGLIYSIGFLASWPIILFL
IAEPLRNLGRFTLADVVSYRLRQRPIRAFSASSSIVIVLLYLVSQMVGAGKLVELLFGFS
YTAAVVLVGVLMVVYVFFGGMLATTWIQIIKAVLLLAGAAFMAFMVMSRFGFSLNALFAQ
AIEAHGKHAAIMRPGGLVSDPVSAVSLGLALIFGTAGLPHILMRFFTVGDVKAARKSILY
ATGIVGIGYALIIIIGFGTIALVASDPAYHTPAGAVIGGVNMVAVHLAHAVGGNLFLGFI
CAVAFSTILAVVAGLTLAGSSAISHDLYAKVLRQGNATDKEEMRVSRMTTLVLGVLSILL
GILFEKQTIAFIVSLTFSIAASSNFPVLLLSIYWRGLTTRGAVVGGSLGLLSAVVLTVLS
PTVWVQVLGHARAIYPYEYPALFSMLVAFAGIYVFSVTDRSARGARERGAFNNQLVDCEL
GLVKPQ
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