SitesBLAST
Comparing RR42_RS28305 RR42_RS28305 proline-specific permease 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)
45% identity, 96% coverage: 10:462/472 of query aligns to 3:451/457 of P15993
- Y103 (≠ W111) 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)
43% identity, 98% coverage: 1:461/472 of query aligns to 1:458/458 of P24207
- R26 (= R26) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P54) 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 (= F87) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y90) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ E92) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (≠ F94) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ V95) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (= F98) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F101) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W105) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (= Y107) mutation to L: No effect on phenylalanine transport activity.
- W108 (= W108) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ W111) 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 (= E118) mutation E->G,L,V,N: Loss of activity.
- K168 (= K168) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (= E228) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (= R254) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P343) 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 (= P445) 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)
41% identity, 96% coverage: 14:465/472 of query aligns to 3:453/469 of P46349
- G33 (= G44) mutation to D: Lack of activity.
- G42 (= G53) mutation to S: Lack of activity.
- G301 (= G313) mutation to V: Lack of activity.
- G338 (≠ S350) mutation to E: Lack of activity.
- F341 (≠ L353) mutation to S: Lack of activity.
- G414 (≠ A426) 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, 96% coverage: 7:459/472 of query aligns to 1:471/489 of P25737
- M1 (≠ L7) modified: Initiator methionine, Removed
- Y102 (= Y107) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (= W111) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K168) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F222) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E228) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E236) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ E274) 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 (≠ P277) 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.
- E438 (vs. gap) mutation to A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D443 (vs. gap) mutation to A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D446 (= D434) mutation to 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)
34% identity, 86% coverage: 9:415/472 of query aligns to 74:500/590 of P04817
- P113 (≠ A48) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
- P148 (= P82) 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 (= V83) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
- S152 (= S86) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
- Y173 (= Y107) 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 (= G235) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
- P313 (= P240) 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 (= W371) 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 (≠ L381) 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)
34% identity, 83% coverage: 19:411/472 of query aligns to 80:484/587 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)
33% identity, 84% coverage: 16:411/472 of query aligns to 83:493/602 of P19145
- A297 (≠ Q225) 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, 82% coverage: 10:398/472 of query aligns to 136:537/663 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, 88% coverage: 1:415/472 of query aligns to 259:754/852 of Q03770
- T382 (≠ A123) 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)
26% identity, 89% coverage: 6:423/472 of query aligns to 10:420/458 of 6f34A
- binding arginine: I40 (≠ A36), G42 (= G38), T43 (≠ V39), G44 (= G40), E115 (= E93), Y116 (≠ F94), A119 (≠ P97), F228 (= F222), A229 (= A223), I231 (≠ Q225), V314 (≠ S309)
- binding cholesterol: W201 (≠ F185), Y202 (≠ G186)
- binding : G28 (≠ K24), F30 (≠ R26), D31 (≠ H27), M34 (= M30), A178 (≠ F162), R179 (≠ W163), A186 (≠ V170), I187 (≠ T171), A190 (= A174), L194 (≠ I178), Q296 (≠ V291), V299 (≠ A294)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
26% identity, 89% coverage: 6:423/472 of query aligns to 8:418/456 of 5oqtA
- binding alanine: I38 (≠ A36), G40 (= G38), T41 (≠ V39), G42 (= G40), F226 (= F222), A227 (= A223), I229 (≠ Q225)
- binding : E24 (≠ G22), G26 (≠ K24), F28 (≠ R26), D29 (≠ H27), M32 (= M30), A176 (≠ F162), R177 (≠ W163), A184 (≠ V170), A188 (= A174), L192 (≠ I178), Q294 (≠ V291), V297 (≠ A294)
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
25% identity, 74% coverage: 15:361/472 of query aligns to 4:346/438 of O34739
- C94 (≠ T103) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (vs. gap) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ A174) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ S309) 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.
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
27% identity, 68% coverage: 61:381/472 of query aligns to 37:362/445 of P60061
- Y93 (= Y107) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ M110) binding ; binding
- C97 (≠ W111) binding
- N101 (≠ G115) 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 (≠ E118) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (≠ F222) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ A223) binding
- I205 (≠ Q225) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (≠ G313) 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 (= S376) 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)
27% identity, 68% coverage: 61:381/472 of query aligns to 37:362/445 of P60063
- Y74 (≠ F87) 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 (≠ F101) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y107) 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 (≠ M110) binding
- C97 (≠ W111) binding
- N101 (≠ G115) binding
- W202 (≠ F222) Periplasmic (proximal) gate; binding
- I205 (≠ Q225) binding
- GVESA 206:210 (≠ GVELI 226:230) Helix-breaking GVESA motif TM6
- E208 (= E228) mutation E->A,D: 5-10% Agm antiport.
- W293 (≠ G313) binding
- F337 (≠ V358) mutation to A: Severely decreased antiport.
- S357 (= S376) binding
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
- 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)
27% identity, 68% coverage: 61:381/472 of query aligns to 33:358/437 of 5j4nA
Sites not aligning to the query:
3l1lA Structure of arg-bound escherichia coli adic (see paper)
28% identity, 70% coverage: 50:381/472 of query aligns to 16:345/423 of 3l1lA
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
21% identity, 69% coverage: 16:340/472 of query aligns to 15:336/461 of P76037
- Y110 (≠ W111) 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)
30% identity, 34% coverage: 203:362/472 of query aligns to 245:420/629 of P30825
Sites not aligning to the query:
- 226 modified: carbohydrate, N-linked (GlcNAc...) asparagine
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
26% identity, 70% coverage: 31:360/472 of query aligns to 12:337/433 of 6f2wA
P82251 b(0,+)-type amino acid transporter 1; b(0,+)AT1; Glycoprotein-associated amino acid transporter b0,+AT1; Solute carrier family 7 member 9 from Homo sapiens (Human) (see 11 papers)
22% identity, 78% coverage: 2:368/472 of query aligns to 4:371/487 of P82251
- V40 (≠ I33) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ AIGVG 36:40) binding
- I44 (= I37) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (≠ G44) to F: in CSNU; uncertain significance
- P52 (≠ A45) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (≠ Y60) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y90) to H: in CSNU; uncertain significance
- G105 (= G96) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W105) to R: in CSNU; uncertain significance
- I120 (vs. gap) to L: in CSNU; uncertain significance
- T123 (vs. gap) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (= V126) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ Y128) modified: Interchain (with C-114 in SLC3A1)
- V170 (= V154) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ L166) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (= G179) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (= L215) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (≠ T216) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (≠ I219) to D: in CSNU; decreased amino acid transport activity
- W230 (≠ F222) to R: in CSNU; complete loss of amino acid transport activity; mutation to A: Abolishes amino acid transport activity.
- D233 (≠ Q225) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ V227) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ L229) mutation to A: Reduces amino acid transport activity.
- G259 (≠ V251) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ W253) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (≠ G278) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ I314) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ T317) to E: in CSNU; uncertain significance
- V330 (≠ T323) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ L324) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (≠ Q326) to Q: in CSNU; decreased amino acid transport activity; dbSNP:rs769576205; to W: in CSNU; severe loss of amino acid transport activity; dbSNP:rs121908484
- A354 (= A346) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
Sites not aligning to the query:
- 379 S→A: Markedly reduces amino acid transport activity.
- 382 A → T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- 383 W→A: Complete loss of amino acid transport activity.
- 386 Y→A: Loss of amino acid transport activity.
- 401 K → E: in CSNU; uncertain significance; dbSNP:rs760264924
- 426 L → P: in CSNU; uncertain significance
- 482 P → L: in CSNU; severe loss of amino acid transport activity; no effect on localization to the apical membrane; dbSNP:rs146815072; mutation P->A,G,S,V: No effect on amino acid transport activity.; mutation P->F,I,M,W: Decreased amino acid transport activity.
Query Sequence
>RR42_RS28305 RR42_RS28305 proline-specific permease
MTDVRKLLNEERVHEEKDLHRGLKDRHIQMIAIGGAIGVGLFLGAGRAIAIAGPGLMLSY
AIGGVAIFFIMRALGELLLYRPVSGSFATYAEEFVGPFAGFATGWSYWFMWVVTGMAEIT
AVAVYVHYWFPDVPQWIPALATLAVLYLVNCVAVAVFGELEFWFALIKVVTIVAMIVIGL
AIIFFGVTPLGPTASFSNLWTHGGFMPFGTLGVVLTLQIVMFAYQGVELIGVTAGEAQNP
EKVLPHATNGVVWRILIFYVGALIIMMALVPWNELKPGVSPFVYVFERIGVPGAAAIVNL
VVITAAASSCNSGIFSTGRMLYTLAQFGQAPRAFGRVSSKHVPSIAITFSAALMGIGVLL
NYIVPEQVFVWVTSISLVGSLWTWSIIMIAHLGYRKAIAAGRVKAVAFRMPGAPYANWLV
VAFMIAVAVLLSLDPGTRVALYVAPVWFALLGIGYRFTKSRALLEGHVQKSA
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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