SitesBLAST
Comparing WP_011383956.1 AMB_RS07815 cation acetate symporter to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 4 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)
25% identity, 90% coverage: 44:546/561 of query aligns to 8:489/502 of P07117
- R257 (= R292) mutation to C: Sodium-independent binding affinity for proline.
- C281 (≠ T320) 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 (≠ G385) mutation to S: Small decrease in proline uptake activity. Confers resistance to N-ethylmaleimide. Exhibits low Na(+)-dependent proline binding.
- C349 (≠ G390) 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 (≠ K418) 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)
22% identity, 53% coverage: 50:344/561 of query aligns to 13:308/480 of 5nv9A
- binding sodium ion: A52 (≠ G89), T53 (≠ D90), L55 (≠ M92), S56 (= S93), V174 (≠ T212), D178 (≠ Q216)
- binding N-acetyl-beta-neuraminic acid: T54 (≠ Y91), S56 (= S93), I58 (≠ A95), T59 (≠ S96), G77 (≠ F114), Q78 (≠ S115), R131 (≠ Q173), F239 (≠ L275)
Sites not aligning to the query:
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)
26% identity, 34% coverage: 46:235/561 of query aligns to 19:211/643 of Q92911
- A102 (≠ L126) 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
Q9NY91 Probable glucose sensor protein SLC5A4; Solute carrier family 5 member 4 from Homo sapiens (Human) (see paper)
21% identity, 84% coverage: 20:489/561 of query aligns to 5:501/659 of Q9NY91
- E457 (≠ F448) mutation to Q: Confers sugar transport activity not found in the wild-type protein. Increased sensitivity to inhibitor phlorizin.
Query Sequence
>WP_011383956.1 AMB_RS07815 cation acetate symporter
MKTTKTAIASALAFGGTALLASAALAAGADMGGAEKQATNWHAIIMFVIFVGATLGITYW
AAGRTKTAADFYAAGGGITGFQNGLAIAGDYMSAASFLGISALVYGSGYDGLIFSVGWLV
GWPIILFLIAERLRNLGKYTFADVCGYRLARTPIRTFAATGSLIVVIFYLIGQMVGAGQL
IKLLFGMDYVYAVMIVGALMMVYVTFGGMVATTWVQIIKACLLLGGATFIAFGVMSQFGF
SFEKLFVKAIEVHPKKVAIMAPGALVTNPVDAISLGMALMFGTAGLPHILMRFFTVPDAR
EARKSVFYATGFIGYFYILTFIIGFGAITMVATNPEYLTKGLGSLDLKGGNNMAAVWLAH
AIGGNLFLGFISAVAFATILAVVSGLTLAGASAISHDLYASVIMHGQATEGKEVTVSKIA
SICLGVIAVLLGLVFEKQNVAFIVALTFSVAASANFPVLVLSMFWGGLTTRGAVLGGMIG
LLMSVIMVVLSKAVWVQSFGFKAEIFPFAYPALFSVPAAFFFSWLFSIMDNSPSAQAERA
AYEAQSIRSETGLGAEGAASH
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