SitesBLAST
Comparing BPHYT_RS07280 BPHYT_RS07280 amino acid permease to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 18 hits to proteins with known functional sites (download)
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
38% identity, 97% coverage: 13:464/466 of query aligns to 3:458/469 of P46349
- G33 (= G43) mutation to D: Lack of activity.
- G42 (= G52) mutation to S: Lack of activity.
- G301 (≠ Q310) mutation to V: Lack of activity.
- G338 (≠ S347) mutation to E: Lack of activity.
- F341 (≠ G350) mutation to S: Lack of activity.
- G414 (≠ S420) mutation to R: Lack of activity.
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
37% identity, 96% coverage: 9:455/466 of query aligns to 10:458/458 of P24207
- R26 (≠ G25) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P53) 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 (= F86) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y89) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ E91) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (= Y93) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ I94) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ W97) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F100) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (≠ Y104) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (= Y106) mutation to L: No effect on phenylalanine transport activity.
- W108 (= W107) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ I110) 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 (= E117) mutation E->G,L,V,N: Loss of activity.
- K168 (= K167) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (= E225) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (= R251) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P340) 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 (≠ V439) 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)
35% identity, 85% coverage: 13:408/466 of query aligns to 6:403/457 of P15993
- Y103 (≠ I110) 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%.
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
33% identity, 86% coverage: 9:408/466 of query aligns to 4:418/489 of P25737
- Y102 (= Y106) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ I110) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K167) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F219) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E225) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E233) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ N270) 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 (≠ G273) 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)
28% identity, 90% coverage: 9:428/466 of query aligns to 69:516/590 of P04817
- P113 (≠ A47) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
- P148 (= P81) 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 (≠ T82) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
- S152 (= S85) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
- Y173 (= Y106) 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 (= G232) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
- P313 (= P237) 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 (≠ L368) 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 (≠ M378) 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)
30% identity, 85% coverage: 13:407/466 of query aligns to 75:474/587 of Q9URZ4
Sites not aligning to the query:
- 29 modified: Phosphoserine
- 30 modified: Phosphoserine
- 37 modified: Phosphoserine
P19145 General amino-acid permease GAP1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
30% identity, 82% coverage: 11:393/466 of query aligns to 79:476/602 of P19145
- A297 (≠ L222) 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, 85% coverage: 3:400/466 of query aligns to 136:544/663 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)
26% identity, 50% coverage: 14:248/466 of query aligns to 273:541/852 of Q03770
- T382 (≠ A122) 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.
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
23% identity, 86% coverage: 9:408/466 of query aligns to 5:390/438 of O34739
- C94 (≠ V102) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ I146) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ G173) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ A306) 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)
25% identity, 49% coverage: 15:244/466 of query aligns to 15:241/461 of P76037
- Y110 (≠ I110) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
3l1lA Structure of arg-bound escherichia coli adic (see paper)
22% identity, 70% coverage: 74:397/466 of query aligns to 55:364/423 of 3l1lA
Sites not aligning to the query:
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
22% identity, 55% coverage: 202:457/466 of query aligns to 211:455/458 of 6f34A
Sites not aligning to the query:
- binding arginine: 40, 42, 43, 44, 115, 116, 119
- binding cholesterol: 201, 202
- binding : 28, 30, 31, 34, 178, 179, 186, 187, 190, 194
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
22% identity, 55% coverage: 202:457/466 of query aligns to 209:453/456 of 5oqtA
Sites not aligning to the query:
- binding alanine: 38, 40, 41, 42
- binding : 24, 26, 28, 29, 32, 176, 177, 184, 188, 192
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
22% identity, 70% coverage: 74:397/466 of query aligns to 57:377/437 of 5j4nA
Sites not aligning to the query:
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
22% identity, 70% coverage: 74:397/466 of query aligns to 61:381/445 of P60061
- Y93 (= Y106) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ S109) binding ; binding
- C97 (≠ I110) binding
- N101 (≠ V114) 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 (≠ E117) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (≠ F219) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (= S220) binding
- I205 (≠ L222) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (≠ Q310) 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 (= S373) binding ; mutation to A: 20% decreased affinity for Arg, 40% decrease affinity for Agm.
Sites not aligning to the query:
- 23 binding ; binding
- 26 binding
P60063 Arginine/agmatine antiporter from Escherichia coli O157:H7 (see 3 papers)
22% identity, 70% coverage: 74:397/466 of query aligns to 61:381/445 of P60063
- Y74 (≠ G87) 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 (≠ F100) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y106) 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 (≠ S109) binding
- C97 (≠ I110) binding
- N101 (≠ V114) binding
- W202 (≠ F219) Periplasmic (proximal) gate; binding
- I205 (≠ L222) binding
- GVESA 206:210 (≠ SIEMI 223:227) Helix-breaking GVESA motif TM6
- E208 (= E225) mutation E->A,D: 5-10% Agm antiport.
- W293 (≠ Q310) binding
- F337 (vs. gap) mutation to A: Severely decreased antiport.
- S357 (= S373) binding
- Y365 (≠ W381) mutation to A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.
Sites not aligning to the query:
- 22 N→A: No change in antiport activity, 6-fold higher affinity for Arg.
- 23 binding
- 25:27 Helix-breaking GSG motif TM1
- 26 binding ; S→K: 5% Agm antiport.
- 27 binding
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)
21% identity, 86% coverage: 5:404/466 of query aligns to 15:443/629 of P30825
- N226 (≠ A185) modified: carbohydrate, N-linked (GlcNAc...) asparagine
Query Sequence
>BPHYT_RS07280 BPHYT_RS07280 amino acid permease
MTQEQRGFDTIVEREKGLQRGLSTGQLSMIAIGGAIGTGLFLGSGFAIGFAGPSVLVSYA
IGALIALLLMGCLAEMTVAHPTSGSFGAYAEHYIAPWAGFLVRYAYWSSIVFAVGTEVTA
IAVYMKYWFPAVPGWYWIVGFSAALIGINSVSVKVFGAVEYVFSMLKIVAIVGFILLGAY
VVFGAPADSTIGFANYTSHGGFFPKGVWGMWVAVIVSIFSYLSIEMIAVAAGEARDPQKA
ITRAFRATMFRLVFFYLLTLALMLAIVPWNAAGTDESPFVRVMAATHVPGAAGVINFVIL
VAALSAMNSQLYITTRMMFSLSRAGYAPRKLGALNGKGVPVAALWLSTIGIALATVLNVV
YPDASFVLMMSVSMFGAMFTWLMIFVTHFFFRHRHQGAPLAFRMWGYPGTSALGAGLMVS
ALVTTWFTREFRMTLVIGVPFIVSLLVVYFVWYRKRAVEGAAAELA
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