SitesBLAST
Comparing WP_012332766.1 NCBI__GCF_000019365.1:WP_012332766.1 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)
26% identity, 79% coverage: 44:487/563 of query aligns to 11:442/502 of P07117
- R257 (= R289) mutation to C: Sodium-independent binding affinity for proline.
- C281 (≠ T317) 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 (≠ G387) mutation to S: Small decrease in proline uptake activity. Confers resistance to N-ethylmaleimide. Exhibits low Na(+)-dependent proline binding.
- C349 (≠ G392) 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 (≠ K420) 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)
27% identity, 32% coverage: 42:223/563 of query aligns to 18:201/643 of Q92911
- A102 (≠ L123) 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
B4EZY7 Sodium/sialic acid symporter SiaT; Na(+)-coupled sialic acid symporter; Sialic acid transporter from Proteus mirabilis (strain HI4320) (see paper)
19% identity, 50% coverage: 59:338/563 of query aligns to 29:309/496 of B4EZY7
- A56 (≠ G86) binding Na(+)
- T58 (≠ Y88) mutation to A: 2-fold increase in Neu5Ac transport.
- L59 (≠ M89) binding Na(+)
- S60 (= S90) mutation to A: Abolishes Neu5Ac transport.
- T63 (≠ S93) mutation to A: Abolishes Neu5Ac transport.
- Q82 (≠ S112) mutation to D: Abolishes Neu5Ac transport.
- R135 (≠ T159) mutation to E: Abolishes Neu5Ac transport.
- D182 (≠ Q213) binding Na(+); mutation to A: Abolishes Neu5Ac transport.
Sites not aligning to the query:
- 339 binding Na(+)
- 342 binding Na(+); binding Na(+); S→A: Abolishes Neu5Ac transport.
- 343 binding Na(+); S→A: Abolishes Neu5Ac transport.
- 345 binding Na(+); S→A: Reduces Neu5Ac transport.
- 346 binding Na(+); S→A: Slightly increases Neu5Ac transport.
5nv9A Substrate-bound outward-open state of a na+-coupled sialic acid symporter reveals a novel na+-site (see paper)
19% identity, 50% coverage: 59:340/563 of query aligns to 25:307/480 of 5nv9A
- binding sodium ion: A52 (≠ G86), T53 (≠ D87), L55 (≠ M89), S56 (= S90), V174 (≠ T209), D178 (≠ Q213)
- binding N-acetyl-beta-neuraminic acid: T54 (≠ Y88), S56 (= S90), I58 (≠ A92), T59 (≠ S93), G77 (≠ Y111), Q78 (≠ S112), R131 (≠ T159), F239 (≠ L276)
Sites not aligning to the query:
Query Sequence
>WP_012332766.1 NCBI__GCF_000019365.1:WP_012332766.1
MIRLRLPALAALALLAAATAASAAGPDLGAVQKQNLNWSAIGMFLLFVLGTLGITYRAAA
QTRSAADFYAAGGGISAGQNALAIAGDYMSAASFLGISGLVFSSGFDGLIYSIGFLVGWP
IVLFLIAERLRNLGKFTFADVASFRLDQTQIRVLSATGTLVVVAFYLIAQMVGAGKLIQL
LFGLDYLYAVVLVGILMIVYVAFGGMKATTWVQIIKACLLLAGATFMALAVLWRYGFNPE
ALFAAAVKEHPKHDAIMAPGGLVSDPISAISLGIGLMFGTAGLPHILMRFFTVSDAQAAR
KSVFYATGLIAYFYILTFIIGFGAITFLMNDPSYFKAGADGAYDRIAGLIGGTNMAAVHL
ANATGGALFLGFISAVAFATILAVVAGLTLAGASAVSHDLYAQVIARGRTSEQKEVRLSK
LSAVVIGVVAIVLGYVFENQNVAFMVGLAFAVAASCNFPVLAMSILWKGTTTTGALVGGL
VGLITAVAMVVLSKAVWVSTLGYSTALFPYDNPALFSMPIAFLVIWAVSKADASARARRE
RDSFEAQYVRSETGIGAATAHAH
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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