SitesBLAST
Comparing WP_011385006.1 NCBI__GCF_000009985.1:WP_011385006.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 5 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)
27% identity, 83% coverage: 32:489/554 of query aligns to 3:450/502 of P07117
- R257 (= R285) mutation to C: Sodium-independent binding affinity for proline.
- C281 (= C314) 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 (≠ G378) mutation to S: Small decrease in proline uptake activity. Confers resistance to N-ethylmaleimide. Exhibits low Na(+)-dependent proline binding.
- C349 (≠ G383) 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 (≠ K411) 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, 69% coverage: 38:419/554 of query aligns to 8:382/480 of 5nv9A
- binding sodium ion: A52 (≠ G82), T53 (≠ D83), L55 (≠ M85), S56 (= S86), V174 (≠ T205), D178 (≠ Q209), A335 (≠ T371), S338 (≠ A374), S338 (≠ A374), S339 (≠ V375), S341 (= S377), S342 (≠ G378)
- binding N-acetyl-beta-neuraminic acid: T54 (≠ Y84), S56 (= S86), I58 (≠ A88), T59 (= T89), G77 (≠ Y107), Q78 (≠ T108), R131 (≠ S155), F239 (≠ L268)
Q9NY91 Probable glucose sensor protein SLC5A4; Solute carrier family 5 member 4 from Homo sapiens (Human) (see paper)
19% identity, 83% coverage: 16:474/554 of query aligns to 11:493/659 of Q9NY91
- E457 (≠ F441) mutation to Q: Confers sugar transport activity not found in the wild-type protein. Increased sensitivity to inhibitor phlorizin.
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)
20% identity, 84% coverage: 15:479/554 of query aligns to 10:498/662 of P11170
- C255 (≠ I252) modified: Disulfide link with 608
- Q457 (≠ F441) mutation to W: Drasticly decreased affinity for glucose and phlorizin.
- T460 (≠ A444) mutation to W: Decreased affinity for glucose and phlorizin.
Sites not aligning to the query:
- 608 modified: Disulfide link with 255
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)
22% identity, 31% coverage: 49:219/554 of query aligns to 29:201/643 of Q92911
- A102 (≠ L119) 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
>WP_011385006.1 NCBI__GCF_000009985.1:WP_011385006.1
MKRILPILLALAVPTAALAGPGDLGGSEKQPINVTAIAMFFAFVMGTLGITYWASKRTKS
ASDFYTAGGGITGFQNGLAIAGDYMSAATLLGLSSMVFATGFDGFIYTISFFVGWPIILF
LLAERLRNLGRYTFADIASYRLDQSKVRTFAAMGSLTVVCFYLIVQMVGAGQLIKLLFGL
DYAVAVIIVGVLMVVYVTFGGMIATTWVQIIKACLLLGGGVLLCALALSKFGFSLENVAA
KAVESHKAGVKIMGPGTMLADPVSAVSLSLGLVFGTAALPHILMRFFTVPNAKEARKSVF
VASGFIGFFFLIVCILGLAAVSIVGTDPQFFEGGKVGGKLLGGGNMPVMHLAKALGGDIF
LGFLSAVAFATILAVVSGLALAGASAIAHDIYARVIRKGHATEAEEMRVSKLSSLVLGVV
AVILGIMFEKQNVAFLVGLTFGIAASANFPVLFLSMYWRGLTTKGALWGGIAGLVSAVTC
VVLSKAVWVVVLNNPAPIFPYEHPALFSMTLAFLVTIVVSKLDGSETAKAEKALFDDQYV
RAQTGIGAASASNH
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