SitesBLAST
Comparing 14258 b0112 aromatic amino acid transporter (NCBI) to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
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)
100% identity, 100% coverage: 1:457/457 of query aligns to 1:457/457 of P15993
- Y103 (= Y103) 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%.
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
65% identity, 94% coverage: 11:440/457 of query aligns to 19:448/458 of P24207
- R26 (= R18) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P46) 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 (= F79) mutation to L: No effect on phenylalanine transport activity.
- F90 (= F82) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (= Y84) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (= Y86) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (= W87) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (= F90) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F93) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W97) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (= Y99) mutation to L: No effect on phenylalanine transport activity.
- W108 (= W100) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ Y103) 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 (= E110) mutation E->G,L,V,N: Loss of activity.
- K168 (= K160) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (= E218) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (= R244) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P333) 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 (= P434) 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.
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
36% identity, 99% coverage: 5:456/457 of query aligns to 2:455/469 of P46349
- G33 (= G36) mutation to D: Lack of activity.
- G42 (= G45) mutation to S: Lack of activity.
- G301 (≠ C303) mutation to V: Lack of activity.
- G338 (≠ S340) mutation to E: Lack of activity.
- F341 (≠ V343) mutation to S: Lack of activity.
- G414 (≠ A415) 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)
36% identity, 84% coverage: 11:392/457 of query aligns to 13:404/489 of P25737
- Y102 (= Y99) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ Y103) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K160) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F212) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E218) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E226) 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.
P04817 Arginine permease CAN1; Canavanine resistance protein 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
36% identity, 92% coverage: 3:423/457 of query aligns to 76:516/590 of P04817
- P113 (≠ V40) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
- P148 (= P74) 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 (= V75) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
- S152 (= S78) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
- Y173 (= Y99) 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 (≠ A225) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
- P313 (= P230) 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 (≠ TA 266:267) 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 (≠ L361) 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 (≠ V371) mutation to S: In CAN1-307; confers citrulline transport activity in GAP1-deleted cells.
Q9URZ4 Cationic amino acid transporter 1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
33% identity, 91% coverage: 6:420/457 of query aligns to 75:502/587 of Q9URZ4
Sites not aligning to the query:
- 29 modified: Phosphoserine
- 30 modified: Phosphoserine
- 37 modified: Phosphoserine
P48813 High-affinity glutamine permease from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
33% identity, 86% coverage: 2:392/457 of query aligns to 136:541/663 of P48813
Sites not aligning to the query:
- 132 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
P19145 General amino-acid permease GAP1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
35% identity, 89% coverage: 11:419/457 of query aligns to 86:511/602 of P19145
- A297 (≠ G215) 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)
Q03770 SPS-sensor component SSY1; Amino-acid permease homolog SSY1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
26% identity, 85% coverage: 10:396/457 of query aligns to 276:740/852 of Q03770
- T382 (≠ G115) 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.
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)
22% identity, 76% coverage: 1:346/457 of query aligns to 18:398/629 of P30825
- N226 (= N179) modified: carbohydrate, N-linked (GlcNAc...) asparagine
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
22% identity, 87% coverage: 1:398/457 of query aligns to 13:408/458 of 6f34A
- binding arginine: I40 (≠ A28), G42 (= G30), T43 (= T31), G44 (= G32), E115 (≠ L102), Y116 (= Y103), A119 (≠ V106), F228 (= F212), A229 (≠ S213), I231 (≠ G215), V314 (= V299)
- binding cholesterol: W201 (= W173), Y202 (≠ L174)
- binding : G28 (≠ K16), F30 (≠ R18), D31 (≠ H19), M34 (≠ L22), A178 (≠ M152), R179 (≠ E153), A186 (≠ K160), I187 (≠ V161), A190 (≠ V164), L194 (≠ I168), Q296 (≠ D281), V299 (= V284)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
22% identity, 87% coverage: 1:398/457 of query aligns to 11:406/456 of 5oqtA
- binding alanine: I38 (≠ A28), G40 (= G30), T41 (= T31), G42 (= G32), F226 (= F212), A227 (≠ S213), I229 (≠ G215)
- binding : E24 (≠ G14), G26 (≠ K16), F28 (≠ R18), D29 (≠ H19), M32 (≠ L22), A176 (≠ M152), R177 (≠ E153), A184 (≠ K160), A188 (≠ V164), L192 (≠ I168), Q294 (≠ D281), V297 (= V284)
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
26% identity, 37% coverage: 67:237/457 of query aligns to 74:241/461 of P76037
- Y110 (= Y103) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
22% identity, 84% coverage: 20:402/457 of query aligns to 11:393/437 of 5j4nA
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
23% identity, 84% coverage: 20:402/457 of query aligns to 15:397/445 of P60061
- I23 (≠ A28) binding ; binding
- S26 (≠ T31) binding
- Y93 (= Y99) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ L102) binding ; binding
- C97 (≠ Y103) binding
- N101 (≠ A107) 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 (≠ E110) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (≠ F212) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (= S213) binding
- I205 (≠ G215) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (vs. gap) 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 (vs. gap) 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)
23% identity, 84% coverage: 20:402/457 of query aligns to 15:397/445 of P60063
- N22 (≠ G27) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ A28) binding
- GSG 25:27 (≠ GTG 30:32) Helix-breaking GSG motif TM1
- S26 (≠ T31) binding ; mutation to K: 5% Agm antiport.
- G27 (= G32) binding
- Y74 (≠ S80) 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 (≠ F93) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y99) 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 (≠ L102) binding
- C97 (≠ Y103) binding
- N101 (≠ A107) binding
- W202 (≠ F212) Periplasmic (proximal) gate; binding
- I205 (≠ G215) binding
- GVESA 206:210 (≠ GLELV 216:220) Helix-breaking GVESA motif TM6
- E208 (= E218) mutation E->A,D: 5-10% Agm antiport.
- W293 (vs. gap) binding
- F337 (≠ C347) mutation to A: Severely decreased antiport.
- S357 (vs. gap) binding
- Y365 (≠ A369) 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, 84% coverage: 20:402/457 of query aligns to 9:380/423 of 3l1lA
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
22% identity, 82% coverage: 23:396/457 of query aligns to 12:377/433 of 6f2wA
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
23% identity, 72% coverage: 23:353/457 of query aligns to 8:351/458 of 7cmiB
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
23% identity, 72% coverage: 23:353/457 of query aligns to 8:351/458 of 7cmhB
Sites not aligning to the query:
Query Sequence
>14258 b0112 aromatic amino acid transporter (NCBI)
MMEGQQHGEQLKRGLKNRHIQLIALGGAIGTGLFLGSASVIQSAGPGIILGYAIAGFIAF
LIMRQLGEMVVEEPVAGSFSHFAYKYWGSFAGFASGWNYWVLYVLVAMAELTAVGKYIQF
WYPEIPTWVSAAVFFVVINAINLTNVKVFGEMEFWFAIIKVIAVVAMIIFGGWLLFSGNG
GPQATVSNLWDQGGFLPHGFTGLVMMMAIIMFSFGGLELVGITAAEADNPEQSIPKATNQ
VIYRILIFYIGSLAVLLSLMPWTRVTADTSPFVLIFHELGDTFVANALNIVVLTAALSVY
NSCVYCNSRMLFGLAQQGNAPKALASVDKRGVPVNTILVSALVTALCVLINYLAPESAFG
LLMALVVSALVINWAMISLAHMKFRRAKQEQGVVTRFPALLYPLGNWICLLFMAAVLVIM
LMTPGMAISVYLIPVWLIVLGIGYLFKEKTAKAVKAH
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