SitesBLAST
Comparing Ga0059261_3091 FitnessBrowser__Korea:Ga0059261_3091 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 11 hits to proteins with known functional sites (download)
A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
31% identity, 27% coverage: 77:190/430 of query aligns to 63:162/446 of A0A0H2VG78
- R102 (= R124) mutation to A: Loss of transport activity.
- I105 (≠ Q127) mutation to S: Affects symport activity. May function as an uniporter.
- E122 (= E144) mutation to A: Loss of transport activity.
- Q137 (≠ Y159) mutation to A: Loss of transport activity.
Sites not aligning to the query:
- 22 D→N: Affects symport activity. May function as an uniporter.
- 250 Q→A: Loss of transport activity.
- 251 Q→A: Loss of transport activity.
- 256 N→A: Loss of transport activity.
- 357 W→A: Loss of transport activity.
Q9Y7Q9 Probable metabolite transporter C2H8.02 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
31% identity, 35% coverage: 71:221/430 of query aligns to 98:255/583 of Q9Y7Q9
Sites not aligning to the query:
- 267 modified: Phosphoserine
- 269 modified: Phosphoserine
- 289 modified: Phosphoserine
- 290 modified: Phosphoserine
- 292 modified: Phosphoserine
- 330 modified: Phosphoserine
P77589 3-(3-hydroxy-phenyl)propionate transporter; 3HPP transporter; 3-(3-hydroxy-phenyl)propionate:H(+) symporter; 3HPP:H(+) symporter from Escherichia coli (strain K12) (see paper)
31% identity, 40% coverage: 61:230/430 of query aligns to 55:208/403 of P77589
- D75 (= D81) mutation D->A,E: Lack of 3HPP transport activity.
Sites not aligning to the query:
- 27 E→A: Lack of 3HPP transport activity.; E→D: Slight decrease in 3HPP transport activity.
- 272 A→H: 30% increase in 3HPP transport activity.
- 276 K→D: Lack of 3HPP transport activity.
4gc0A The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to 6-bromo-6-deoxy-d-glucose (see paper)
22% identity, 91% coverage: 38:430/430 of query aligns to 36:469/475 of 4gc0A
4gbzA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-glucose (see paper)
22% identity, 91% coverage: 38:430/430 of query aligns to 36:469/475 of 4gbzA
4gbyA The structure of the mfs (major facilitator superfamily) proton:xylose symporter xyle bound to d-xylose (see paper)
22% identity, 91% coverage: 38:430/430 of query aligns to 36:469/475 of 4gbyA
P0AGF4 D-xylose-proton symporter; D-xylose transporter from Escherichia coli (strain K12) (see paper)
22% identity, 91% coverage: 38:430/430 of query aligns to 40:473/491 of P0AGF4
- G83 (= G84) mutation to A: Abolishes xylose transport.
- R133 (= R124) mutation R->C,H,L: Abolishes xylose transport.
- E153 (= E144) mutation to A: Abolishes xylose transport.
- R160 (= R151) mutation to A: Abolishes xylose transport.
- Q168 (≠ Y159) binding ; mutation to A: Abolishes xylose transport.
- Q288 (≠ G250) mutation to A: Abolishes xylose transport.
- QQ 288:289 (≠ GT 250:251) binding
- Q289 (≠ T251) mutation to A: Strongly decreases xylose transport.
- N294 (≠ A256) binding ; mutation to A: Abolishes xylose transport.
- Y298 (= Y260) mutation to A: Abolishes xylose transport.
- N325 (≠ F287) mutation to A: No effect on xylose transport.
- G340 (= G302) mutation to A: Abolishes xylose transport.
- R341 (= R303) mutation R->A,W: Abolishes xylose transport.
- W392 (≠ A353) binding ; mutation to A: Abolishes xylose transport.
- E397 (= E358) mutation to A: Abolishes xylose transport.
- R404 (= R365) mutation to A: Strongly decreases xylose transport.
- Q415 (≠ A378) binding
- W416 (≠ I379) mutation to A: Strongly decreases xylose transport.
Sites not aligning to the query:
- 24 F→A: Decreases xylose transport.
O42885 Putative inorganic phosphate transporter C8E4.01c from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
28% identity, 37% coverage: 72:230/430 of query aligns to 109:278/572 of O42885
Sites not aligning to the query:
- 12 modified: Phosphoserine
- 14 modified: Phosphoserine
- 292 modified: Phosphoserine
- 296 modified: Phosphoserine
6rw3A The molecular basis for sugar import in malaria parasites. (see paper)
21% identity, 67% coverage: 79:365/430 of query aligns to 66:378/437 of 6rw3A
P25297 Inorganic phosphate transporter PHO84 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
26% identity, 49% coverage: 12:223/430 of query aligns to 61:285/587 of P25297
Sites not aligning to the query:
- 6 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
- 298 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
O15244 Solute carrier family 22 member 2; Organic cation transporter 2; hOCT2 from Homo sapiens (Human) (see 8 papers)
25% identity, 73% coverage: 64:377/430 of query aligns to 158:475/555 of O15244
- M165 (≠ W74) to I: lower Vmax for MPP(+) transport; no change in transport efficiency (Vmax/Km) and clearance of cyclo(his-pro) and salsolinol; dbSNP:rs8177507
- Y169 (≠ V78) mutation to F: No change in TEA uptake.
- T201 (≠ E110) to M: in dbSNP:rs145450955
- Y241 (≠ Q158) mutation to F: Slight decrease in TEA uptake. No change in tyrosine phosphorylation. Strong decrease in TEA uptake; when associated with F-362. Strong decrease in TEA and metformin uptake and YES1-mediated tyrosine phosphorylation; when associated with F-362 and F-377.
- Y257 (≠ A183) mutation to F: No change in TEA uptake.
- S270 (≠ F195) to A: decreased Ki value for TBA inhibition of MPP(+); no change in transport efficiency (Vmax/Km) and clearance of cyclo(his-pro) and salsolinol; dbSNP:rs316019
- Y279 (≠ V204) mutation to F: No change in TEA uptake.
- Y280 (≠ F205) mutation to F: No change in TEA uptake.
- P284 (vs. gap) mutation to A: Decreased TEA and metformin uptake. Decreased tyrosine phosphorylation.
- PESPR 284:288 (≠ ----R 208) Proline-rich sequence
- S286 (vs. gap) mutation to A: No change in TEA and metformin uptake. No change in tyrosine phosphorylation.
- P287 (vs. gap) mutation to A: Decreased TEA and metformin uptake. Decreased tyrosine phosphorylation.
- Y362 (≠ D272) mutation to F: Decreased TEA uptake and YES1-mediated tyrosine phosphorylation. Strong decrease in TEA uptake; when associated with F-241. Strong decrease in TEA uptake; when associated with F-377. Strong decrease in TEA and metformin uptake and YES1-mediated tyrosine phosphorylation; when associated with F-241 and F-377.
- Y377 (≠ A282) mutation to F: Slight decrease in TEA uptake. No change in tyrosine phosphorylation. Strong decrease in TEA uptake; when associated with F-362. Strong decrease in TEA and metformin uptake and YES1-mediated tyrosine phosphorylation; when associated with F-241 and F-362.
- R400 (= R300) to C: lower Vmax and reduced Ki value for TBA inhibition of MPP(+); lower transport efficiency (Vmax/Km) and clearance of cyclo(his-pro); no change in transport efficiency (Vmax/Km) and clearance of salsolinol; dbSNP:rs8177516
- K432 (≠ A334) to Q: lower Km value for MPP(+) and reduced Ki value for TBA inhibition of MPP; no change in transport efficiency (Vmax/Km) and clearance of cyclo(his-pro) and salsolinol; dbSNP:rs8177517
- Y458 (≠ F360) mutation to F: No change in TEA uptake.
Sites not aligning to the query:
- 54 P → S: in dbSNP:rs8177504
- 73 Y→F: No change in TEA uptake.
- 92 Y→F: No change in TEA uptake.
- 128 Y→F: No change in TEA uptake.
- 544 Y→F: No change in TEA uptake.
Query Sequence
>Ga0059261_3091 FitnessBrowser__Korea:Ga0059261_3091
MNESSGEAGTRQRLKSILGGSAGNLVEWYDWYAYAAFTLYFAPHFFPKGDQTTQLLNTAA
VFAVGFLMRPIGGWLMGVYADKYGRKAGLTLSVSLMCAGSLLIAVTPGYETIGALAPALL
VFARLMQGLSIGGEYGASATYLSEMAGRKRRGFFSSFQYVTLISGQLIALGVLLILQASM
SEAALESWGWRIPFFIGGALAVIVFWLRRGLSETQSFENAKAEGRKTGALALLREHPGEF
LLVMALTAGGTLAFYAYSIYLQKFLVNTSGFDRETASEINAAALFVFMCIQPLAGALSDR
IGRKPLMIGFGVLGVLCTYPIFTALEQVSSAWAAFGLMLGALVIVTGYTSINAVVKAELF
PAHIRTLGVALPYALANAIFGGTAEYVALWFKDQGMERGFYWYVTGMIGISLIVYLRMRD
TRTHSKILED
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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