SitesBLAST
Comparing GFF1660 FitnessBrowser__psRCH2:GFF1660 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)
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)
66% identity, 99% coverage: 7:464/464 of query aligns to 7:454/457 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)
61% identity, 97% coverage: 10:458/464 of query aligns to 18:457/458 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 (≠ H84) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (= Y86) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ G87) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ Y90) 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 (= 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 (= P443) 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)
37% identity, 97% coverage: 11:462/464 of query aligns to 8:453/469 of P46349
- G33 (= G36) mutation to D: Lack of activity.
- G42 (= G45) mutation to S: Lack of activity.
- G301 (= G312) mutation to V: Lack of activity.
- G338 (≠ S349) mutation to E: Lack of activity.
- F341 (≠ V352) mutation to S: Lack of activity.
- G414 (= G424) 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)
35% identity, 98% coverage: 1:455/464 of query aligns to 1:469/489 of P25737
- M1 (= M1) modified: Initiator methionine, Removed
- 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 (≠ A271) 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 (= D274) 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 (≠ I428) mutation to A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D446 (≠ W431) 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)
36% identity, 91% coverage: 6:429/464 of query aligns to 79:513/590 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 (≠ AA 271:272) mutation Missing: In CAN1-318; confers citrulline transport activity in GAP1-deleted cells.
- Y356 (≠ G273) 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 (≠ L370) 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 (≠ V380) 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)
33% identity, 88% coverage: 1:408/464 of query aligns to 80:492/602 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)
P48813 High-affinity glutamine permease from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
32% identity, 84% coverage: 10:401/464 of query aligns to 144:541/663 of P48813
Sites not aligning to the query:
- 132 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)
34% identity, 84% coverage: 10:401/464 of query aligns to 79:473/587 of Q9URZ4
Sites not aligning to the query:
- 29 modified: Phosphoserine
- 30 modified: Phosphoserine
- 37 modified: Phosphoserine
Q03770 SPS-sensor component SSY1; Amino-acid permease homolog SSY1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
25% identity, 91% coverage: 11:432/464 of query aligns to 277:770/852 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.
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
22% identity, 79% coverage: 67:432/464 of query aligns to 74:417/461 of P76037
- Y110 (= Y103) 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)
22% identity, 84% coverage: 11:399/464 of query aligns to 28:436/629 of P30825
- N226 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
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: 20:343/464 of query aligns to 11:320/437 of 5j4nA
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
21% identity, 65% coverage: 42:342/464 of query aligns to 55:349/458 of 6f34A
- binding arginine: E115 (≠ L102), Y116 (= Y103), A119 (≠ V106), F228 (= F212), A229 (≠ S213), I231 (≠ G215), V314 (= V308)
- binding cholesterol: W201 (≠ Q183), Y202 (≠ A184)
- binding : A178 (≠ T152), R179 (≠ E153), A186 (≠ K160), I187 (≠ V161), A190 (≠ I164), L194 (≠ I168), Q296 (≠ S290), V299 (≠ A293)
Sites not aligning to the query:
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
22% identity, 70% coverage: 20:343/464 of query aligns to 15:324/445 of P60061
- I23 (≠ A28) binding ; binding
- S26 (≠ T31) binding
- Y93 (= Y99) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ Y103) binding ; binding
- C97 (≠ V104) binding
- N101 (≠ M108) 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 (≠ L111) 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 (≠ 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)
22% identity, 70% coverage: 20:343/464 of query aligns to 15:324/445 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 (≠ Y103) binding
- C97 (≠ V104) binding
- N101 (≠ M108) 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 (≠ G312) 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.
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
22% identity, 65% coverage: 42:342/464 of query aligns to 53:347/456 of 5oqtA
Sites not aligning to the query:
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
23% identity, 91% coverage: 23:445/464 of query aligns to 12:424/433 of 6f2wA
3l1lA Structure of arg-bound escherichia coli adic (see paper)
22% identity, 70% coverage: 20:343/464 of query aligns to 9:307/423 of 3l1lA
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
24% identity, 73% coverage: 23:363/464 of query aligns to 8:345/457 of 7b00A
Sites not aligning to the query:
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
24% identity, 73% coverage: 23:363/464 of query aligns to 8:345/458 of 7cmiB
Query Sequence
>GFF1660 FitnessBrowser__psRCH2:GFF1660
MTAETLHTGSLQRGLKNRHIQLIALGGAIGTGLFLGSAGVLRSAGPSMILGYAIGGFIAF
LIMRQLGEMIVEEPVAGSFSHFAHKYGGGYAGFLSGWNYWVLYVLVGMAELTAVGKYVQF
WWPEVPTWATAAAFFVLINLINLSNVKAFGETEFWFAIVKVAAIVGMILLGLFLLVSGKG
GEQASISNLWSHGGFFPNGFSGMLLALAIIMFSFGGLELVGITAAEAAEPKTVIPKAINQ
VVYRILIFYIGALTVLLALYPWDALLLTLGAAGDPYSGSPFVQIFSLIGSDTAAHLLNFV
VLTAALSVYNSGVYCNSRMLYGLAEQGDAPRSLMKINSRGVPVLAVGVSALVTLLCVAVN
YLFPQGALELLMSLAVAALVINWAMISLAHLKFRRAMQQQGVEPSFKAFWFPLSNYLCLA
FVAGILIIMLWLPGIRMSVFAIPVWVGFLWLCYRLRARLLARAV
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