SitesBLAST
Comparing AO353_24335 FitnessBrowser__pseudo3_N2E3:AO353_24335 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 19 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)
38% identity, 88% coverage: 26:462/494 of query aligns to 5:435/457 of P15993
- Y103 (≠ W124) 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)
39% identity, 85% coverage: 26:447/494 of query aligns to 13:429/458 of P24207
- R26 (= R39) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P67) 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 (= F100) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y103) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ R105) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (≠ F107) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ M108) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ R111) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F114) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W118) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (= Y120) mutation to L: No effect on phenylalanine transport activity.
- W108 (≠ F121) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ W124) 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 (≠ D131) mutation E->G,L,V,N: Loss of activity.
- K168 (= K183) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (= E243) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (= R269) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P358) 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.
Sites not aligning to the query:
- 442 P→A: 46% of wild-type phenylalanine transport activity.; P→G: 52% of wild-type phenylalanine transport activity.; P→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)
37% identity, 94% coverage: 25:489/494 of query aligns to 1:459/469 of P46349
- G33 (= G57) mutation to D: Lack of activity.
- G42 (= G66) mutation to S: Lack of activity.
- G301 (= G328) mutation to V: Lack of activity.
- G338 (≠ T365) mutation to E: Lack of activity.
- F341 (≠ I368) mutation to S: Lack of activity.
- G414 (≠ V441) 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)
34% identity, 86% coverage: 27:450/494 of query aligns to 8:437/489 of P25737
- Y102 (= Y120) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (= W124) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K183) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F237) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E243) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E251) 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)
31% identity, 84% coverage: 33:448/494 of query aligns to 85:515/590 of P04817
- P113 (≠ R61) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
- P148 (= P95) 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 (≠ S96) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
- S152 (= S99) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
- Y173 (= Y120) 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 (= G250) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
- P313 (≠ A255) 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 288:289) mutation Missing: In CAN1-318; confers citrulline transport activity in GAP1-deleted cells.
- Y356 (= Y290) 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 (≠ L386) 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 (≠ I396) 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)
32% identity, 88% coverage: 29:463/494 of query aligns to 83:540/602 of P19145
- A297 (= A240) 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)
Q9URZ4 Cationic amino acid transporter 1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
32% identity, 77% coverage: 34:415/494 of query aligns to 82:471/587 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)
28% identity, 82% coverage: 10:414/494 of query aligns to 111:538/663 of P48813
- K132 (vs. gap) 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)
22% identity, 90% coverage: 8:452/494 of query aligns to 249:774/852 of Q03770
- T382 (≠ A136) 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.
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
26% identity, 47% coverage: 34:263/494 of query aligns to 20:242/461 of P76037
- Y110 (≠ W124) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
23% identity, 53% coverage: 25:285/494 of query aligns to 1:251/438 of O34739
- C94 (≠ A116) 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 (≠ I189) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
Sites not aligning to the query:
- 291 C→S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
- 415 C→S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.
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, 76% coverage: 28:402/494 of query aligns to 24:423/629 of P30825
- N226 (≠ H207) 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, 76% coverage: 65:438/494 of query aligns to 57:420/458 of 6f34A
- binding arginine: E115 (≠ V123), Y116 (≠ W124), A119 (vs. gap), F228 (= F237), A229 (= A238), I231 (≠ A240), V314 (≠ S324)
- binding cholesterol: W201 (≠ F196), Y202 (≠ F197)
- binding : A178 (≠ G173), R179 (≠ E174), A186 (≠ V181), I187 (= I182), A190 (= A185), L194 (≠ I189), Q296 (≠ V306), V299 (≠ I309)
Sites not aligning to the query:
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
23% identity, 76% coverage: 65:438/494 of query aligns to 55:418/456 of 5oqtA
Sites not aligning to the query:
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
24% identity, 69% coverage: 26:364/494 of query aligns to 6:329/445 of P60061
- I23 (≠ A49) binding ; binding
- S26 (≠ T52) binding
- Y93 (= Y120) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ L126) binding ; binding
- C97 (≠ T127) binding
- N101 (≠ D131) 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 (≠ A134) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (≠ F237) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ A238) binding
- I205 (≠ A240) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (≠ G328) 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, 69% coverage: 26:364/494 of query aligns to 6:329/445 of P60063
- N22 (≠ G48) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ A49) binding
- GSG 25:27 (≠ GTG 51:53) Helix-breaking GSG motif TM1
- S26 (≠ T52) binding ; mutation to K: 5% Agm antiport.
- G27 (= G53) binding
- Y74 (≠ V101) 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 (≠ F114) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y120) 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 (≠ L126) binding
- C97 (≠ T127) binding
- N101 (≠ D131) binding
- W202 (≠ F237) Periplasmic (proximal) gate; binding
- I205 (≠ A240) binding
- GVESA 206:210 (≠ SIELV 241:245) Helix-breaking GVESA motif TM6
- E208 (= E243) mutation E->A,D: 5-10% Agm antiport.
- W293 (≠ G328) 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, 69% coverage: 26:364/494 of query aligns to 2:325/437 of 5j4nA
P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
20% identity, 56% coverage: 89:364/494 of query aligns to 59:325/444 of P0AAE8
- Y73 (= Y103) 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 (= E106) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y89 (= Y120) 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 (≠ F121) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
- Y107 (≠ I137) mutation to L: Strong decrease in cadaverine uptake.
- C125 (≠ A154) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- Y174 (≠ H207) mutation to L: Moderate decrease in cadaverine uptake.
- D185 (≠ G218) mutation to N: Moderate decrease in cadaverine uptake.
- C196 (≠ V232) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E204 (= E243) 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 (= Y274) 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 (≠ L285) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C282 (≠ A321) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- R299 (≠ S338) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
- D303 (≠ G342) 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 (≠ F349) 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.
3l1lA Structure of arg-bound escherichia coli adic (see paper)
22% identity, 66% coverage: 41:364/494 of query aligns to 9:312/423 of 3l1lA
Query Sequence
>AO353_24335 FitnessBrowser__pseudo3_N2E3:AO353_24335
MKKQKIQSLSAVQCGSELKDRSNWLDSHESGYSKHLKKRHVQMMALGGAIGTGLFLGAGA
RLQIAGPALAVIYLVCGIFAFFILRALGELVMHRPSSGSFVSYTREFMGERASFVAGWMY
FVVWALTGVVDITAIAIYMKYWSVFSDVPQWVFALSALGVVTLMNMVGVKWFGEMEFWFA
VIKVAAISIFLVIGSFFFATGHEVAGHIPGLHLITDNGGIFPHGLLPAIIIVQGVIFAYA
SIELVGTAAGETADARKVIPKAINGVIWRISLFYVGSVFLLVTVLPWTAYSANVSPFVTF
FEALGVPGIGSVMNIVVMTAALSSLNSGLYATGRVLRSLAMGGSAPKMFKRMSSQGVPYM
GILVTMGINVFGVVLNFLIPAQLFELLLNLVSLGIISTWAFIVLSQINYRRAVKRGEVEM
VSFRMPGAPFTSWLTLVFLLVVLVLLAFDYPNGTYTVLSIPLVAGALMLGWSKAVRSKAK
GSEEIKSDPSHVGA
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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