SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing PP_1743 PP_1743 acetate permease 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 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, 80% coverage: 42:484/554 of query aligns to 7:462/502 of P07117

query
sites
P07117

M

M

F

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A

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C

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R257 (= R288) mutation to C: Sodium-independent binding affinity for proline.
C281 (≠ T316) 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)
22% identity, 50% coverage: 58:336/554 of query aligns to 25:304/480 of 5nv9A

query
sites
5nv9A

S

S

K

K

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R

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Q

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A

binding sodium ion: A52 (≠ G85), T53 (≠ D86), L55 (≠ M88), S56 (= S89), V174 (≠ T208), D178 (≠ Q212)
binding N-acetyl-beta-neuraminic acid: T54 (≠ Y87), L55 (≠ M88), S56 (= S89), I58 (≠ A91), T59 (≠ S92), G77 (≠ Y110), Q78 (≠ S111), R131 (≠ L166), F239 (vs. gap), V277 (≠ I309)

Sites not aligning to the query:

binding sodium ion: 335, 338, 338, 339, 341, 342

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)
25% identity, 33% coverage: 42:222/554 of query aligns to 19:201/643 of Q92911

query
sites
Q92911

M

V

F

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A102 (≠ L122) 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

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)
19% identity, 82% coverage: 29:482/554 of query aligns to 18:501/662 of P11170

query
sites
P11170

E

E

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C255 (≠ L261) 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

Query Sequence

>PP_1743 PP_1743 acetate permease
MIRQVKALAVLACGAFAPAVWAADALTGEVQKQPLNVSAIAMFVAFVAFTLGITYWASKR
NKSASDYYAAGGKITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSIGFLVGWPI
ILFLIAERLRNLGKYTFADVASYRLGQKEIRTLSASGSLVVVAFYLIAQMVGAGKLIELL
FGLDYHVAVILVGILMCLYVLFGGMLATTWVQIIKAVLLLSGASFMALMVMKHVGFDFNT
LFSEAIKVHAKGEAIMSPGGLVKDPISAFSLGLALMFGTAGLPHILMRFFTVSDAKEARK
SVLYATGFIGYFYILTFIIGFGAILLVSTNPEFKDAAGALLGGNNMAAVHLANAVGGSVF
LGFISAVAFATILAVVAGLTLAGASAVSHDLYASVWRKGKANDKDEIRVSKITTVALGVL
AIGLGILFEKQNIAFMVGLAFSIAASCNFPVLLLSMYWKKLTTRGAMIGGWLGLVSAVTL
MILGPTIWVQILGHEKPIYPYEYPALFSMAIAFVSIWFFSVTDKSKAAEDERALFFPQFV
RSQTGLGASGAVSH

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