SitesBLAST
Comparing Dsui_0290 FitnessBrowser__PS:Dsui_0290 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)
23% identity, 91% coverage: 39:570/582 of query aligns to 8:493/502 of P07117
- R257 (= R316) mutation to C: Sodium-independent binding affinity for proline.
- C281 (≠ F340) 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 (≠ G406) mutation to S: Small decrease in proline uptake activity. Confers resistance to N-ethylmaleimide. Exhibits low Na(+)-dependent proline binding.
- C349 (≠ G411) 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 (≠ M440) 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)
28% identity, 30% coverage: 50:221/582 of query aligns to 32:201/643 of Q92911
- A102 (≠ M121) 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
5nv9A Substrate-bound outward-open state of a na+-coupled sialic acid symporter reveals a novel na+-site (see paper)
22% identity, 33% coverage: 40:231/582 of query aligns to 9:197/480 of 5nv9A
- binding sodium ion: A52 (≠ G84), T53 (≠ D85), L55 (≠ M87), S56 (= S88), V174 (≠ T207), D178 (≠ Q211)
- binding N-acetyl-beta-neuraminic acid: T54 (≠ Y86), S56 (= S88), I58 (≠ A90), T59 (≠ S91), G77 (≠ Y109), Q78 (≠ S110), R131 (≠ L165)
Sites not aligning to the query:
Query Sequence
>Dsui_0290 FitnessBrowser__PS:Dsui_0290
MKKLTNTLALAGLGLLSSPVFAAALEGQAEKQATNWTAIIMFGAFVLATLWITKWAASKT
KTAADFYTAGGGITGFQNGLAIAGDYMSAASFLGISAAVFANGYDGLIYSIGFLVGWPII
MFLMAERLRNLGKFTFADVAAYRFQATPIRALAASGTLVVVAFYLIAQMVGAGQLIKLLF
GLDYWMAVVLVGILMMVYVLFGGMTATTWVQIIKAVLLLSGASFMVFMVLAKYGFSPEAL
FADAVRIKTDLAAKGLLAKALETDPSATAETVAAAAAAKGQSIMGPGSFIKDPISAISFG
MALMFGTAGLPHILMRFFTVPDGKEARKSVFWATTWIGYFYILTFIIGFGAIVLVGTNPE
FLDAKGVLKGGGNMAAIHLANAVGGNVFLGFISAVAFATILAVVAGLTLSGASAVSHDLY
ASVFRHGNVDSATEMRVSKMTTVALGIIAVVLGIAFEKQNIAFMVSLAFAIAASANFPVL
FMSVLWKDCTTKGAFYGGFLGLITAVVLTVLSKSIWVDILGNKTEIFPYASPALFSMAAG
FIGIWLFSLMDRSEQAAKERVAYLDQEIRSETGIGAAAASSH
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