SitesBLAST
Comparing WP_017178492.1 NCBI__GCF_000295095.1:WP_017178492.1 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)
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
56% identity, 95% coverage: 10:477/493 of query aligns to 1:470/489 of P25737
- M1 (≠ V10) modified: Initiator methionine, Removed
- Y102 (= Y111) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (= W115) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K172) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (≠ Y224) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E230) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E238) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ A283) 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 (≠ N286) 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 (≠ G446) mutation to A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D443 (≠ G451) mutation to A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D446 (≠ S453) mutation to A: Retains 13% of wild-type lysine uptake activity. Is unable to inhibit CadC.
Q9URZ4 Cationic amino acid transporter 1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
38% identity, 97% coverage: 9:484/493 of query aligns to 69:550/587 of Q9URZ4
Sites not aligning to the query:
- 29 modified: Phosphoserine
- 30 modified: Phosphoserine
- 37 modified: Phosphoserine
P04817 Arginine permease CAN1; Canavanine resistance protein 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
38% identity, 99% coverage: 2:491/493 of query aligns to 64:569/590 of P04817
- P113 (≠ T51) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
- P148 (= P86) 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 (= V87) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
- S152 (= S90) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
- Y173 (= Y111) 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 (= G237) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
- P313 (= P242) 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.
- T-S 354:355 (≠ AED 283:285) mutation Missing: In CAN1-318; confers citrulline transport activity in GAP1-deleted cells.
- Y356 (≠ N286) 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 (≠ F381) 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 (= F391) 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)
34% identity, 96% coverage: 5:479/493 of query aligns to 60:552/602 of P19145
- K76 (≠ E21) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
- A297 (≠ Q227) mutation to V: Impairs basic amino-acids transport and regulation by these amino-acids.
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
39% identity, 88% coverage: 5:440/493 of query aligns to 2:421/458 of P24207
- R26 (= R29) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P57) 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 (= F91) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y94) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ T96) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (≠ F98) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ V99) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ S102) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F105) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W109) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (= Y111) mutation to L: No effect on phenylalanine transport activity.
- W108 (= W112) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ W115) 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 (= E122) mutation E->G,L,V,N: Loss of activity.
- K168 (= K172) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (= E230) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (= R256) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P353) 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)
39% identity, 86% coverage: 22:445/493 of query aligns to 8:421/469 of P46349
- G33 (≠ A47) mutation to D: Lack of activity.
- G42 (= G56) mutation to S: Lack of activity.
- G301 (= G323) mutation to V: Lack of activity.
- G338 (≠ T360) mutation to E: Lack of activity.
- F341 (≠ V363) mutation to S: Lack of activity.
- G414 (≠ A438) mutation to R: Lack of 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)
37% identity, 86% coverage: 16:441/493 of query aligns to 5:418/457 of P15993
- Y103 (≠ W115) 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%.
P48813 High-affinity glutamine permease from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
30% identity, 96% coverage: 4:476/493 of query aligns to 120:610/663 of P48813
- K132 (≠ Q16) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Q88CZ8 L-histidine transporter HutT from Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) (see paper)
30% identity, 97% coverage: 17:492/493 of query aligns to 2:467/467 of Q88CZ8
- T27 (= T42) mutation T->A,S: Retains 60% of wild-type activity.; mutation to N: Retains 20% of wild-type activity.
- E98 (≠ N114) mutation to A: Retains 80% of wild-type activity.
- K156 (= K172) mutation K->A,Q: Retains less than 10% of wild-type activity.; mutation to R: Retains 40% of wild-type activity.
- F212 (≠ Y224) mutation F->A,Q: Loss of activity.; mutation to Y: No change in activity.
- E218 (= E230) mutation E->A,Q: Loss of activity.; mutation to D: Retains 70% of wild-type activity.
Q03770 SPS-sensor component SSY1; Amino-acid permease homolog SSY1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
26% identity, 92% coverage: 21:475/493 of query aligns to 276:783/852 of Q03770
- T382 (≠ A127) 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)
25% identity, 48% coverage: 16:250/493 of query aligns to 12:242/461 of P76037
- Y110 (≠ W115) 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)
23% identity, 70% coverage: 18:360/493 of query aligns to 24:392/629 of P30825
- N226 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
27% identity, 84% coverage: 21:436/493 of query aligns to 22:421/458 of 6f34A
- binding arginine: I40 (≠ A39), G42 (= G41), T43 (= T42), G44 (= G43), E115 (= E93), Y116 (= Y94), A119 (≠ R97), F228 (≠ Y224), A229 (≠ S225), I231 (≠ Q227), V314 (≠ I311)
- binding cholesterol: W201 (≠ A185), Y202 (≠ M186)
- binding : G28 (≠ L27), F30 (≠ R29), D31 (≠ H30), M34 (= M33), A178 (≠ G162), R179 (≠ E163), A186 (≠ S170), I187 (= I171), A190 (≠ V174), L194 (≠ V178), Q296 (≠ F292), V299 (= V295)
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
24% identity, 88% coverage: 34:467/493 of query aligns to 12:424/433 of 6f2wA
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
27% identity, 84% coverage: 21:436/493 of query aligns to 20:419/456 of 5oqtA
- binding alanine: I38 (≠ A39), G40 (= G41), T41 (= T42), G42 (= G43), F226 (≠ Y224), A227 (≠ S225), I229 (≠ Q227)
- binding : E24 (≠ S25), G26 (≠ L27), F28 (≠ R29), D29 (≠ H30), M32 (= M33), A176 (≠ G162), R177 (≠ E163), A184 (≠ S170), A188 (≠ V174), L192 (≠ V178), Q294 (≠ F292), V297 (= V295)
Q9QXW9 Large neutral amino acids transporter small subunit 2; L-type amino acid transporter 2; mLAT2; Solute carrier family 7 member 8 from Mus musculus (Mouse) (see paper)
24% identity, 90% coverage: 34:475/493 of query aligns to 47:471/531 of Q9QXW9
- Y130 (≠ V119) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (≠ E122) mutation to S: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake. Increases the export of both L-leucine and L-phenylalanine.
- F242 (≠ Y224) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
Q22397 Amino acid transporter protein 6 from Caenorhabditis elegans (see paper)
22% identity, 82% coverage: 36:441/493 of query aligns to 30:421/523 of Q22397
Sites not aligning to the query:
- 521:523 PDZ-binding motif; mutation Missing: Abolishes the interaction with nrfl-1.
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
24% identity, 69% coverage: 16:353/493 of query aligns to 2:323/438 of O34739
- C94 (≠ I107) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ V148) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ V178) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ A319) 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.
6li9B Heteromeric amino acid transporter b0,+at-rbat complex bound with arginine (see paper)
22% identity, 69% coverage: 34:374/493 of query aligns to 9:347/458 of 6li9B
Q9FFL1 Polyamine transporter RMV1; Protein RESISTANT TO METHYL VIOLOGEN 1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
21% identity, 78% coverage: 51:437/493 of query aligns to 76:433/490 of Q9FFL1
- I377 (≠ L362) mutation to F: Loss of sensitivity to paraquat.
Query Sequence
>WP_017178492.1 NCBI__GCF_000295095.1:WP_017178492.1
MTDSTQAGPVAADGEQSEPQELRRSLLSRHLTMISIGGAIGTGLFVASGATISQAGPGGA
LVAYAAVGIMVWLIMQSLGEMAAYLPVAGSFGEYGTRFVSPSFGFAIGWNYWFNWAITVA
AELVAAALVMKYWLPDVPSLVWSALFLVILFTINALSARAYGESEFLFASIKVVAVIVFL
ILGVAMIAGILGGPSPGTENWTTGEAPFVGGGEGILLVLLVAGYSFQGTELIGTAAGEAE
NPERTIPRAIRTIFWRILLFYIGAIAVIGFLIPYTDPNLLNSAEDNVSVSPFTLVFERAG
ILGAASVINAIILTSVLSAGTSGLYSSTRMLFALAERGHAPRFLTRLSSHQVPMNALVAT
TLVGLAGFITSLVGDGAAYEFLLTLSALAGFITWAGISWCHWRFRMALKAQGQPLTDLPY
RARFFPAGAIVALIACIAIIIGQAYGPVTSGKSLGEILMPYIGIPVFLALWWGHKLVTRA
PTVDPATADLERK
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