SitesBLAST
Comparing Pf1N1B4_801 D-serine/D-alanine/glycine transporter 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)
44% identity, 95% coverage: 12:460/473 of query aligns to 13:458/458 of P24207
- R26 (= R25) 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 (≠ Q91) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (= Y93) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ L94) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ L97) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F100) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W104) 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 (≠ W110) 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 (= E227) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (= R253) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P342) 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 (= P444) 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: 14:463/473 of query aligns to 7:452/457 of P15993
- Y103 (≠ W110) 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)
39% identity, 96% coverage: 13:468/473 of query aligns to 4:455/469 of P46349
- G33 (= G43) mutation to D: Lack of activity.
- G42 (= G52) mutation to S: Lack of activity.
- G301 (= G312) mutation to V: Lack of activity.
- G338 (≠ S349) mutation to E: Lack of activity.
- F341 (≠ A352) mutation to S: Lack of activity.
- G414 (≠ L425) 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)
37% identity, 93% coverage: 11:449/473 of query aligns to 6:463/489 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 (= W110) 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 (= F221) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E227) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E235) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ E273) 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 (≠ T276) 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 (≠ M430) mutation to A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D443 (= D435) mutation to A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D446 (vs. gap) mutation to A: Retains 13% of wild-type lysine uptake activity. Is unable to inhibit CadC.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P04817 Arginine permease CAN1; Canavanine resistance protein 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
34% identity, 89% coverage: 14:434/473 of query aligns to 80:520/590 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 (= V82) 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 (= G234) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
- P313 (= P239) 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 (= W370) 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 (≠ I380) 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, 82% coverage: 14:401/473 of query aligns to 76:478/587 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)
31% identity, 83% coverage: 12:402/473 of query aligns to 81:483/602 of P19145
- A297 (≠ L224) 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, 90% coverage: 8:433/473 of query aligns to 135:573/663 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: 18:432/473 of query aligns to 277:772/852 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.
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)
26% identity, 66% coverage: 18:327/473 of query aligns to 28:369/629 of P30825
- N226 (= N188) modified: carbohydrate, N-linked (GlcNAc...) asparagine
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
26% identity, 87% coverage: 13:422/473 of query aligns to 18:420/458 of 6f34A
- binding arginine: I40 (≠ C35), G42 (= G37), T43 (≠ V38), G44 (= G39), E115 (≠ V112), Y116 (≠ T113), A119 (= A116), F228 (= F221), A229 (= A222), I231 (≠ L224), V314 (≠ S308)
- binding cholesterol: W201 (≠ A192), Y202 (≠ L193)
- binding : G28 (= G23), F30 (≠ R25), D31 (≠ H26), M34 (≠ L29), A178 (≠ V169), R179 (≠ T170), A186 (≠ G177), I187 (≠ G178), A190 (≠ V181), L194 (≠ G185), Q296 (≠ I290), V299 (≠ A293)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
26% identity, 87% coverage: 13:422/473 of query aligns to 16:418/456 of 5oqtA
- binding alanine: I38 (≠ C35), G40 (= G37), T41 (≠ V38), G42 (= G39), F226 (= F221), A227 (= A222), I229 (≠ L224)
- binding : E24 (= E21), G26 (= G23), F28 (≠ R25), D29 (≠ H26), M32 (≠ L29), A176 (≠ V169), R177 (≠ T170), A184 (≠ G177), A188 (≠ V181), L192 (≠ G185), Q294 (≠ I290), V297 (≠ A293)
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
24% identity, 87% coverage: 18:428/473 of query aligns to 8:405/438 of O34739
- C94 (≠ T102) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ G146) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ G180) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ S308) 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)
23% identity, 51% coverage: 8:247/473 of query aligns to 6:242/461 of P76037
- Y110 (≠ W110) 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)
24% identity, 73% coverage: 20:365/473 of query aligns to 2:328/423 of 3l1lA
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
24% identity, 73% coverage: 20:365/473 of query aligns to 4:341/437 of 5j4nA
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
24% identity, 73% coverage: 20:365/473 of query aligns to 8:345/445 of P60061
- I23 (≠ C35) binding ; binding
- S26 (≠ V38) binding
- Y93 (= Y106) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ L109) binding ; binding
- C97 (≠ W110) binding
- N101 (≠ C114) 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 (≠ F221) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ A222) binding
- I205 (≠ L224) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (≠ G312) 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, 73% coverage: 20:365/473 of query aligns to 8:345/445 of P60063
- N22 (≠ A34) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ C35) binding
- GSG 25:27 (≠ GVG 37:39) Helix-breaking GSG motif TM1
- S26 (≠ V38) binding ; mutation to K: 5% Agm antiport.
- G27 (= G39) binding
- Y74 (≠ S87) 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 (≠ L109) binding
- C97 (≠ W110) binding
- N101 (≠ C114) binding
- W202 (≠ F221) Periplasmic (proximal) gate; binding
- I205 (≠ L224) binding
- GVESA 206:210 (≠ GVEMI 225:229) Helix-breaking GVESA motif TM6
- E208 (= E227) mutation E->A,D: 5-10% Agm antiport.
- W293 (≠ G312) binding
- F337 (≠ V357) mutation to A: Severely decreased antiport.
Sites not aligning to the query:
- 357 binding
- 365 Y→A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.
P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
24% identity, 58% coverage: 75:349/473 of query aligns to 59:326/444 of P0AAE8
- Y73 (= Y89) mutation to 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.
- E76 (≠ D92) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y89 (= Y106) mutation to 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.
- Y90 (≠ W107) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
- Y107 (= Y124) mutation to L: Strong decrease in cadaverine uptake.
- C125 (≠ A138) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- Y174 (≠ G194) mutation to L: Moderate decrease in cadaverine uptake.
- D185 (≠ P206) mutation to N: Moderate decrease in cadaverine uptake.
- C196 (≠ V219) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E204 (= E227) 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 (= Y258) 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 (= Y269) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C282 (≠ A305) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- R299 (≠ S322) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
- D303 (≠ N326) 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 (≠ F333) 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.
- 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.
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
24% identity, 85% coverage: 20:420/473 of query aligns to 2:392/433 of 6f2wA
Query Sequence
>Pf1N1B4_801 D-serine/D-alanine/glycine transporter
MPVGNHLPHGETAQGGPLKRELGERHIRLMALGACIGVGLFLGSAKAIEMAGPAIMLSYI
IGGLAILVIMRALGEMAVHNPVAGSFSRYAQDYLGPLAGFLTGWNYWFLWLVTCVAEITA
VAVYMGVWFPDVPRWIWALAALISMGSINLIAVKAFGEFEFWFALIKIVTIIAMVVGGIG
VIAFGFGNDGVALGISNLWAHGGFMPNGVQGVLMSLQMVMFAYLGVEMIGLTAGEAKNPQ
KTIPNAIGSVFWRILLFYVGALFVILSIYPWNEIGTQGSPFVMTFERLGIKTAAGIINFV
VITAALSSCNGGIFSTGRMLYSLAQNGQAPAGFAKTSNNGVPRRALLLSIGALLLGVLLN
YLVPEKVFVWVTAIATFGAIWTWVMILLAQLKFRQGLSASERAGLKYRMWLYPVSSYLAL
AFLVLVVGLMAYFPDTRVALYVGPAFLVLLTVLFYVFKLQPSNVSQGAVRSAS
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