SitesBLAST
Comparing RR42_RS14635 FitnessBrowser__Cup4G11:RR42_RS14635 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 20 (the maximum) hits to proteins with known functional sites (download)
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
43% identity, 95% coverage: 2:446/466 of query aligns to 13:452/458 of P24207
- R26 (= R15) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P43) 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 (= F76) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y79) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ S81) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (≠ G83) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ L84) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ L87) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F90) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W94) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (= Y96) mutation to L: No effect on phenylalanine transport activity.
- W108 (≠ A97) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ M100) 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 (≠ D107) mutation E->G,L,V,N: Loss of activity.
- K168 (= K157) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (= E219) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (= R245) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P334) 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 (≠ A436) 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)
43% identity, 95% coverage: 2:442/466 of query aligns to 5:440/457 of P15993
- Y103 (≠ M100) 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)
35% identity, 99% coverage: 1:461/466 of query aligns to 1:458/469 of P46349
- G33 (= G33) mutation to D: Lack of activity.
- G42 (= G42) mutation to S: Lack of activity.
- G301 (≠ D304) mutation to V: Lack of activity.
- G338 (≠ M341) mutation to E: Lack of activity.
- F341 (≠ A344) mutation to S: Lack of activity.
- G414 (≠ F417) mutation to R: Lack of activity.
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
38% identity, 89% coverage: 4:418/466 of query aligns to 9:431/489 of P25737
- Y102 (= Y96) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ M100) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K157) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F213) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E219) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E227) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ G267) 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 (≠ G270) 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)
33% identity, 82% coverage: 3:386/466 of query aligns to 75:466/587 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, 90% coverage: 4:424/466 of query aligns to 80:515/590 of P04817
- P113 (≠ A37) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
- P148 (= P71) 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 (= V72) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
- S152 (= S75) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
- Y173 (= Y96) 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 (= G226) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
- P313 (= P231) 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.
- W451 (≠ L362) mutation to C: In CAN1-328; confers citrulline transport activity in GAP1-deleted cells.; mutation to L: In CAN1-316; confers citrulline transport activity in GAP1-deleted cells.; mutation to S: In CAN1-335; confers citrulline transport activity in GAP1-deleted cells.
- F461 (≠ V372) mutation to 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)
31% identity, 82% coverage: 8:390/466 of query aligns to 86:479/602 of P19145
- A297 (≠ G216) 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)
28% identity, 83% coverage: 2:390/466 of query aligns to 138:538/663 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)
27% identity, 85% coverage: 8:405/466 of query aligns to 277:753/852 of Q03770
- T382 (≠ G112) 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.
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
27% identity, 90% coverage: 36:455/466 of query aligns to 52:456/458 of 6f34A
- binding arginine: E115 (= E99), Y116 (≠ M100), A119 (≠ V103), F228 (= F213), A229 (= A214), I231 (≠ G216), V314 (≠ A300)
- binding cholesterol: W201 (≠ V183), Y202 (≠ A184)
- binding : A178 (≠ L149), R179 (≠ E150), A186 (≠ I165), I187 (≠ G166), A190 (≠ V169), L194 (= L173), Q296 (≠ I282), V299 (≠ A285)
Sites not aligning to the query:
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
27% identity, 90% coverage: 36:455/466 of query aligns to 50:454/456 of 5oqtA
Sites not aligning to the query:
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
21% identity, 90% coverage: 1:420/466 of query aligns to 1:405/438 of O34739
- C94 (≠ L92) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ I135) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ A170) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ A300) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
Sites not aligning to the query:
- 415 C→S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
27% identity, 41% coverage: 48:239/466 of query aligns to 58:242/461 of P76037
- Y110 (≠ M100) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
P30825 High affinity cationic amino acid transporter 1; CAT-1; CAT1; Ecotropic retroviral leukemia receptor homolog; Ecotropic retrovirus receptor homolog; Solute carrier family 7 member 1; System Y+ basic amino acid transporter from Homo sapiens (Human) (see paper)
24% identity, 71% coverage: 2:331/466 of query aligns to 23:381/629 of P30825
- N226 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
24% identity, 84% coverage: 22:411/466 of query aligns to 14:391/433 of 6f2wA
3l1lA Structure of arg-bound escherichia coli adic (see paper)
25% identity, 68% coverage: 17:334/466 of query aligns to 9:306/423 of 3l1lA
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
24% identity, 72% coverage: 1:334/466 of query aligns to 1:323/445 of P60061
- I23 (≠ A25) binding ; binding
- S26 (≠ T28) binding
- Y93 (vs. gap) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ L92) binding ; binding
- C97 (≠ G93) binding
- N101 (≠ A97) 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 (= M100) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (≠ F213) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ A214) binding
- I205 (≠ G216) 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.
Sites not aligning to the query:
- 357 binding ; S→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, 72% coverage: 1:334/466 of query aligns to 1:323/445 of P60063
- N22 (≠ S24) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ A25) binding
- GSG 25:27 (≠ GTG 27:29) Helix-breaking GSG motif TM1
- S26 (≠ T28) binding ; mutation to K: 5% Agm antiport.
- G27 (= G29) binding
- Y74 (≠ G77) 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 (≠ F90) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (vs. gap) 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 (≠ L92) binding
- C97 (≠ G93) binding
- N101 (≠ A97) binding
- W202 (≠ F213) Periplasmic (proximal) gate; binding
- I205 (≠ G216) binding
- GVESA 206:210 (≠ GIEII 217:221) Helix-breaking GVESA motif TM6
- E208 (= E219) mutation E->A,D: 5-10% Agm antiport.
- W293 (≠ G309) binding
Sites not aligning to the query:
- 337 F→A: Severely decreased antiport.
- 357 binding
- 365 Y→A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
24% identity, 68% coverage: 17:334/466 of query aligns to 11:319/437 of 5j4nA
P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
26% identity, 36% coverage: 204:372/466 of query aligns to 189:363/444 of P0AAE8
- C196 (≠ V211) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E204 (= E219) mutation to Q: Strong decrease in both cadaverine excretion and cadaverine uptake. 22-fold increase in Km for cadaverine for cadaverine uptake and 6-fold increase in Km for cadaverine for cadaverine excretion.
- Y235 (= Y250) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake. 23-fold increase in Km for cadaverine for cadaverine uptake and 7-fold increase in Km for cadaverine for cadaverine excretion.
- Y246 (= Y261) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C282 (≠ N302) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- R299 (= R319) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
- D303 (vs. gap) mutation to N: Strong decrease in both cadaverine excretion and cadaverine uptake. 24-fold increase in Km for cadaverine for cadaverine uptake and 9-fold increase in Km for cadaverine for cadaverine excretion.
- Y310 (≠ F325) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
Sites not aligning to the query:
- 12 C→S: Does not affect cadaverine excretion and cadaverine uptake.
- 41 W→L: Moderate decrease in cadaverine uptake.
- 43 W→L: Strong decrease in cadaverine uptake.
- 55 Y→L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- 57 Y→L: Strong decrease in cadaverine uptake.
- 73 Y→L: Strong decrease in both cadaverine excretion and cadaverine uptake. 9-fold increase in Km for cadaverine for cadaverine uptake and 10-fold increase in Km for cadaverine for cadaverine excretion.
- 76 E→Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- 89 Y→L: Strong decrease in both cadaverine excretion and cadaverine uptake. 10-fold increase in Km for cadaverine for cadaverine uptake and 5-fold increase in Km for cadaverine for cadaverine excretion.
- 90 Y→L: Strong decrease in both cadaverine excretion and cadaverine uptake.
- 107 Y→L: Strong decrease in cadaverine uptake.
- 125 C→S: Does not affect cadaverine excretion and cadaverine uptake.
- 174 Y→L: Moderate decrease in cadaverine uptake.
- 185 D→N: Moderate decrease in cadaverine uptake.
- 366 Y→L: Strong decrease in cadaverine uptake. 15-fold increase in Km for cadaverine for cadaverine uptake.
- 368 Y→L: Strong decrease in cadaverine uptake.
- 370 C→S: Strong decrease in both cadaverine excretion and cadaverine uptake.
- 377 E→Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- 389 C→S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- 394 C→S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- 397 C→S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- 408 E→Q: Moderate decrease in cadaverine uptake.
- 423 Y→L: Strong decrease in both cadaverine excretion and cadaverine uptake.
Query Sequence
>RR42_RS14635 FitnessBrowser__Cup4G11:RR42_RS14635
MQEQSQGLQRGLSARHIRFMALGSAIGTGLFYGSASAIQTAGPAVLLAYVIGGAAVYMVM
RALGEMAVRNPVAGSFGQYASTGLGPLAGFLLGWTYAFEMIVVCLADVTAFGIYMGFWFP
DVPRWIWVLGIVFLIGGLNLLSVKVFGELEFWLSLLKVGAIVAMIGGGVAIMLFGFGMAD
GGVATGIHNLWTHGGFMPNGIAGVIASFAVVMFAFGGIEIIGITAGEARDPQRVIPRAIN
AVPLRILLFYVLTLAVLMSLYPWHRIGSEGSPFVQIFSRLGIGSAAAVLNIVVISAAVSA
INSDIFGAGRMLYGMAVQRQAPRIFASVSRKGVPWMTVVVMAFALLAGVVLNYVMPEDVF
TLIASIATFATVWVWLMILLSQVALRRRMSRAEVAALKFPVPFWPVAPLAATAFMLFIFG
VLGWFPQTRAALLVGAVWLLLLVVAWWCWGRPRGQEGAPASSFAAD
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