SitesBLAST
Comparing RR42_RS13875 RR42_RS13875 sodium:solute symporter 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)
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, 25% coverage: 68:237/683 of query aligns to 45:207/643 of Q92911
- A102 (= A125) 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
P07117 Sodium/proline symporter; Proline carrier; Proline permease; Propionate transporter from Escherichia coli (strain K12) (see 4 papers)
25% identity, 28% coverage: 48:235/683 of query aligns to 7:201/502 of P07117
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.
- 344 C→S: Small decrease in proline uptake activity. Confers resistance to N-ethylmaleimide. Exhibits low Na(+)-dependent proline binding.
- 349 C→S: Does not affect proline uptake activity. Sensitive to N-ethylmaleimide. Na(+)-dependent proline binding activity is similar to wild-type carrier.
- 376 mutation R->E,Q: No change in activity.; R→K: Loss of activity.
Q9NY91 Probable glucose sensor protein SLC5A4; Solute carrier family 5 member 4 from Homo sapiens (Human) (see paper)
26% identity, 24% coverage: 70:234/683 of query aligns to 58:218/659 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.
Query Sequence
>RR42_RS13875 RR42_RS13875 sodium:solute symporter
MPDEQSRFRRRLLLYYGLFTIGLFVFIGMMGLLEHSSGDALWLGYVFLFVTIAIYACIGL
ICRTSDLNEYYVAGRRVPALFNGMAIAADWMSAASFIGLAGILFASGYEGLAYVMGWTGG
YCLVAFLLAPYLRKYGGYTIPDFLAARYGNGKPGGNMPVRAIAVMAASLCSFVYLVAQIQ
GVGLIVTRFIGVEFAVGVFFGLAGILVCSFLGGMRAVTWTQVAQYIMLIAAFLVTVSMIA
WKHHHEALPQLSYGTLLQQLDTRERSIERDPAEQAVREYYRQQAIQMQDRISRLPQSFDE
ERNALSARLQELRLRNAPLREIKTVERERVEFPRDIAAAQQQWNQQREEALARSQPSTPS
TEPYPSPSEAERKTKRLNFVLLVFCLMLGTASLPHILTRLYTTPSVKESRNSVAWAVFFI
ALLYVSAPALAALVKYEFFQHLVGTPYAELPQWVVQWRKVDPPVFGIRDVNGDGIVQWAE
ILIQPDMIVLAAPEIAGLPYVISGLVAAGALAAALSTADGLLLTIANALSHDVFYHMGDR
TASHQRRVTTAKIVLLGVALFASYVTSLRPGNILFLVGAAFSLAASSFFPVLVLAIFWRR
TTAAGAVAGMVAGLGVAVYYIFVNYPFFTRMTGIFGNRWFGVDPIASGAFGVPAGFAVAI
LVSLLTPRNAPVIDRLVTYLRRG
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