SitesBLAST
Comparing GFF2849 FitnessBrowser__WCS417:GFF2849 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 17 hits to proteins with known functional sites (download)
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
36% identity, 96% coverage: 10:456/465 of query aligns to 15:456/458 of P24207
- R26 (= R21) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (≠ T49) mutation to A: 50% of wild-type phenylalanine transport activity.; mutation to G: No change in phenylalanine transport activity.; mutation to L: 26% of wild-type phenylalanine transport activity.
- F87 (= F82) mutation to L: No effect on phenylalanine transport activity.
- F90 (= F85) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ G87) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (= Y89) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ L90) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ R93) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F96) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W100) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (= Y102) mutation to L: No effect on phenylalanine transport activity.
- W108 (= W103) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ W106) mutation to L: 60% of wild-type phenylalanine transport activity.; mutation to Y: Enables the transport of tryptophan to almost the same steady-state level as that of phenylalanine.
- E118 (≠ D113) mutation E->G,L,V,N: Loss of activity.
- K168 (= K163) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (= E224) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (= R250) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P339) mutation to A: 5% of wild-type phenylalanine transport activity.; mutation P->G,Q,K,R: Loss of activity.; mutation to S: 3% of wild-type phenylalanine transport activity.; mutation to T: 17% of wild-type phenylalanine transport activity.
- P442 (= P442) mutation to A: 46% of wild-type phenylalanine transport activity.; mutation to G: 52% of wild-type phenylalanine transport activity.; mutation to L: 43% of wild-type phenylalanine transport activity.
P15993 Aromatic amino acid transport protein AroP; Aromatic amino acid:H(+) symporter AroP; General aromatic amino acid permease; General aromatic transport system from Escherichia coli (strain K12) (see paper)
36% identity, 97% coverage: 6:456/465 of query aligns to 3:448/457 of P15993
- Y103 (≠ W106) Key residue for tryptophan transport; mutation to F: Decreases tryptophan transport to less than 50% of wild-type levels and reduces the ability of tryptophan to inhibit phenylalanine transport from 95 to 62%.
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
34% identity, 85% coverage: 11:404/465 of query aligns to 5:394/469 of P46349
- G33 (= G39) mutation to D: Lack of activity.
- G42 (= G48) mutation to S: Lack of activity.
- G301 (= G309) mutation to V: Lack of activity.
- G338 (≠ T346) mutation to E: Lack of activity.
- F341 (≠ L349) mutation to S: Lack of activity.
Sites not aligning to the query:
- 414 G→R: Lack of activity.
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
36% identity, 86% coverage: 10:408/465 of query aligns to 9:411/489 of P25737
- Y102 (= Y102) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (= W106) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K163) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F218) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E224) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E232) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (vs. gap) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-278.
- D278 (vs. gap) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-275.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 438 E→A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 443 D→A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 446 D→A: Retains 13% of wild-type lysine uptake activity. Is unable to inhibit CadC.
Q9URZ4 Cationic amino acid transporter 1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
31% identity, 83% coverage: 10:393/465 of query aligns to 76:466/587 of Q9URZ4
Sites not aligning to the query:
- 29 modified: Phosphoserine
- 30 modified: Phosphoserine
- 37 modified: Phosphoserine
P04817 Arginine permease CAN1; Canavanine resistance protein 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
32% identity, 73% coverage: 3:343/465 of query aligns to 73:427/590 of P04817
- P113 (≠ I43) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
- P148 (≠ L77) mutation to L: In CAN1-337; confers citrulline transport activity in GAP1-deleted cells and leads to sensitivity to L-glutamic acid alpha-hydroxamate, alpha-aminoisobutyrate, 3-chloro-L-alanine, L-ethionine, L-allylglycine, and D-histidine, but not sensitivity to L-aspartic acid alpha-hydroxamate or p-fluoro-L-phenylalanine.
- V149 (≠ N78) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
- S152 (= S81) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
- Y173 (= Y102) mutation to D: In CAN1-306; confers citrulline transport activity in GAP1-deleted cells.; mutation to H: In CAN1-327; confers citrulline transport activity in GAP1-deleted cells.
- G308 (≠ A231) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
- P313 (= P236) mutation to S: In CAN1-329; confers citrulline transport activity in GAP1-deleted cells and leads to sensitivity to L-glutamic acid alpha-hydroxamate, alpha-aminoisobutyrate, 3-chloro-L-alanine, L-ethionine, L-allylglycine, and D-histidine, L-aspartic acid alpha-hydroxamate and p-fluoro-L-phenylalanine.
- TS 354:355 (vs. gap) mutation Missing: In CAN1-318; confers citrulline transport activity in GAP1-deleted cells.
- Y356 (vs. gap) mutation to H: In CAN1-340; confers citrulline transport activity in GAP1-deleted cells.; mutation to N: In CAN1-339; confers citrulline transport activity in GAP1-deleted cells.
Sites not aligning to the query:
- 451 W→C: In CAN1-328; confers citrulline transport activity in GAP1-deleted cells.; W→L: In CAN1-316; confers citrulline transport activity in GAP1-deleted cells.; W→S: In CAN1-335; confers citrulline transport activity in GAP1-deleted cells.
- 461 F→S: In CAN1-307; confers citrulline transport activity in GAP1-deleted cells.
P19145 General amino-acid permease GAP1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
30% identity, 82% coverage: 14:394/465 of query aligns to 86:476/602 of P19145
- A297 (= A221) mutation to V: Impairs basic amino-acids transport and regulation by these amino-acids.
Sites not aligning to the query:
- 76 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
P48813 High-affinity glutamine permease from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
26% identity, 90% coverage: 10:429/465 of query aligns to 141:571/663 of P48813
Sites not aligning to the query:
- 132 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Q03770 SPS-sensor component SSY1; Amino-acid permease homolog SSY1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
22% identity, 86% coverage: 10:408/465 of query aligns to 273:746/852 of Q03770
- T382 (≠ G119) mutation T->H,L: Constitutively active, up-regulates amino acid permease transcription in response to subthreshold concentrations of amino acids.; mutation to K: In SSY1-102; constitutively active, up-regulates amino acid permease transcription in the absence of amino-acids.; mutation to R: Constitutively active, up-regulates amino acid permease transcription in the absence of amino acids.
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
24% identity, 81% coverage: 23:397/465 of query aligns to 15:385/445 of P60061
- I23 (≠ A31) binding ; binding
- S26 (≠ T34) binding
- Y93 (= Y102) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ S105) binding ; binding
- C97 (≠ W106) binding
- N101 (≠ V110) binding ; mutation to A: Vmax for Arg-Agm exchange 1% of wild-type, KM increases 3-fold.; mutation to D: Nearly wild-type Arg-Agm exchange.
- M104 (≠ D113) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (≠ F218) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (= S219) binding
- I205 (≠ A221) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (≠ G309) binding ; mutation W->C,H,L: Loss of Arg-Agm exchange.; mutation W->F,Y: Less than 20% Arg-Agm exchange activity. Vmax 15% of wild-type rate.
- S357 (= S374) binding ; mutation to A: 20% decreased affinity for Arg, 40% decrease affinity for Agm.
P60063 Arginine/agmatine antiporter from Escherichia coli O157:H7 (see 3 papers)
24% identity, 81% coverage: 23:397/465 of query aligns to 15:385/445 of P60063
- N22 (≠ G30) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ A31) binding
- GSG 25:27 (≠ GTG 33:35) Helix-breaking GSG motif TM1
- S26 (≠ T34) binding ; mutation to K: 5% Agm antiport.
- G27 (= G35) binding
- Y74 (= Y89) mutation to A: 50% antiport activity at pH 6.0, 10-fold higher than wild-type antiport activity at pH 7.5, i.e. loss of pH-dependence of substrate transport. No change in binding of Arg or Agm.; mutation Y->C,H,L,M,Q,S: Loss of pH-dependence of substrate transport.; mutation to F: Approximately wild-type antiport.
- Y87 (≠ W100) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y102) mutation to A: Reduced binding affinity for Arg, no binding to Agm. 25% Agm antiport.; mutation to K: Almost no binding to both Arg and Agm. 5% Agm antiport.
- A96 (≠ S105) binding
- C97 (≠ W106) binding
- N101 (≠ V110) binding
- W202 (≠ F218) Periplasmic (proximal) gate; binding
- I205 (≠ A221) binding
- GVESA 206:210 (≠ GTELI 222:226) Helix-breaking GVESA motif TM6
- E208 (= E224) mutation E->A,D: 5-10% Agm antiport.
- W293 (≠ G309) binding
- F337 (≠ L354) mutation to A: Severely decreased antiport.
- S357 (= S374) binding
- Y365 (≠ W382) mutation to A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.
3l1lA Structure of arg-bound escherichia coli adic (see paper)
23% identity, 81% coverage: 23:397/465 of query aligns to 9:368/423 of 3l1lA