SitesBLAST
Comparing AO353_05930 FitnessBrowser__pseudo3_N2E3:AO353_05930 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 18 hits to proteins with known functional sites (download)
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
36% identity, 97% coverage: 3:456/470 of query aligns to 5:458/458 of P24207
- R26 (≠ G24) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P52) 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 (= F85) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y88) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ E90) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (= Y92) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ I93) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ L96) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F99) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (≠ Y103) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (= Y105) mutation to L: No effect on phenylalanine transport activity.
- W108 (= W106) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ I109) 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 (= E116) mutation E->G,L,V,N: Loss of activity.
- K168 (= K166) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (= E223) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (= R249) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P338) 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 (≠ V440) 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)
37% identity, 96% coverage: 10:461/470 of query aligns to 2:453/457 of P15993
- Y103 (≠ I109) 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)
35% identity, 95% coverage: 10:456/470 of query aligns to 1:449/469 of P46349
- G33 (= G42) mutation to D: Lack of activity.
- G42 (= G51) mutation to S: Lack of activity.
- G301 (≠ Q308) mutation to V: Lack of activity.
- G338 (≠ S345) mutation to E: Lack of activity.
- F341 (≠ G348) mutation to S: Lack of activity.
- G414 (≠ A421) 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)
33% identity, 94% coverage: 8:450/470 of query aligns to 4:467/489 of P25737
- Y102 (= Y105) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ I109) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K166) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F217) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E223) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E231) 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.
- E438 (≠ T429) mutation to A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D443 (≠ M434) mutation to A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D446 (≠ V437) 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)
29% identity, 91% coverage: 1:429/470 of query aligns to 67:516/590 of P04817
- P113 (≠ A46) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
- P148 (≠ S80) 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 (≠ T81) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
- S152 (= S84) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
- Y173 (= Y105) 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 (= G230) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
- P313 (= P235) 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 (≠ L366) 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 (≠ I376) 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)
29% identity, 89% coverage: 17:434/470 of query aligns to 80:512/587 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, 83% coverage: 8:398/470 of query aligns to 136:542/663 of P48813
Sites not aligning to the query:
- 132 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
P19145 General amino-acid permease GAP1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
28% identity, 89% coverage: 17:432/470 of query aligns to 86:519/602 of P19145
- A297 (≠ L220) 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)
Q03770 SPS-sensor component SSY1; Amino-acid permease homolog SSY1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
21% identity, 85% coverage: 13:412/470 of query aligns to 273:749/852 of Q03770
- T382 (≠ A121) 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)
27% identity, 49% coverage: 17:248/470 of query aligns to 18:247/461 of P76037
- Y110 (≠ I109) 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, 69% coverage: 9:334/470 of query aligns to 20:373/629 of P30825
- N226 (≠ S184) modified: carbohydrate, N-linked (GlcNAc...) asparagine
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
23% identity, 94% coverage: 17:460/470 of query aligns to 23:457/458 of 6f34A
- binding arginine: I40 (≠ A34), G42 (= G36), T43 (= T37), G44 (= G38), E115 (≠ A112), Y116 (≠ V113), A119 (≠ E116), F228 (= F217), A229 (≠ S218), I231 (≠ L220), V314 (≠ A304)
- binding cholesterol: W201 (≠ Y179), Y202 (≠ V180)
- binding : G28 (≠ T22), F30 (≠ G24), D31 (≠ Q25), M34 (= M28), A178 (≠ G156), R179 (≠ T157), A186 (≠ T164), I187 (= I165), A190 (≠ G168), L194 (≠ G172), Q296 (≠ I286), V299 (≠ A289)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
23% identity, 94% coverage: 17:460/470 of query aligns to 21:455/456 of 5oqtA
- binding alanine: I38 (≠ A34), G40 (= G36), T41 (= T37), G42 (= G38), F226 (= F217), A227 (≠ S218), I229 (≠ L220)
- binding : E24 (≠ Q20), G26 (≠ T22), F28 (≠ G24), D29 (≠ Q25), M32 (= M28), A176 (≠ G156), R177 (≠ T157), A184 (≠ T164), A188 (≠ G168), L192 (≠ G172), Q294 (≠ I286), V297 (≠ A289)
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
22% identity, 95% coverage: 12:456/470 of query aligns to 3:436/438 of O34739
- C94 (≠ V101) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ I145) 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 (≠ A304) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
- C415 (≠ F432) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.
P0AAF1 Putrescine transporter PotE; Putrescine-proton symporter / putrescine-ornithine antiporter from Escherichia coli (strain K12) (see 2 papers)
21% identity, 70% coverage: 25:354/470 of query aligns to 13:341/439 of P0AAF1
- C62 (≠ M75) mutation C->A,T: Strong decrease in both uptake and excretion activities.; mutation to S: Moderate decrease in both uptake and excretion activities.
- K68 (≠ T81) mutation to A: Slight decrease in both uptake and excretion activities.
- E77 (= E90) mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
- Y78 (≠ F91) mutation to L: Uptake activity decreases more than excretion activity.
- K82 (≠ P95) mutation to A: Slight decrease in both uptake and excretion activities.
- Y90 (= Y103) mutation to L: Uptake activity decreases more than excretion activity.
- Y92 (= Y105) mutation to L: Moderate decrease in both uptake and excretion activities.
- W201 (≠ F217) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- E207 (= E223) mutation E->A,D,N,Q: Lack of both uptake and excretion activities.
- C210 (≠ A226) mutation to A: Moderate decrease in both uptake and excretion activities.
- C285 (≠ A301) mutation to A: Moderate decrease in both uptake and excretion activities.
- C286 (≠ L302) mutation to A: Moderate decrease in both uptake and excretion activities.
- W292 (≠ Q308) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- K301 (≠ F317) mutation to A: Excretion activity decreases more than uptake activity.
- Y308 (= Y324) mutation to L: Excretion activity decreases more than uptake activity.
Sites not aligning to the query:
- 422 W→L: Uptake activity decreases more than excretion activity.
- 425 Y→F: Moderate decrease in both uptake and excretion activities.; Y→L: Strong decrease in both uptake and excretion activities.
- 433 mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
22% identity, 83% coverage: 29:417/470 of query aligns to 12:393/433 of 6f2wA
P63235 Glutamate/gamma-aminobutyrate antiporter; Glu/GABA antiporter; Extreme acid sensitivity protein from Escherichia coli (strain K12) (see 2 papers)
24% identity, 56% coverage: 144:405/470 of query aligns to 135:405/511 of P63235
- L212 (≠ F217) mutation to A: 70% decrease in substrate transport.
- E218 (= E223) mutation to A: At least 90% decrease in substrate transport.
- E304 (≠ A304) mutation to A: At least 90% decrease in substrate transport.
- W308 (≠ Q308) mutation to A: At least 90% decrease in substrate transport.
- Y378 (≠ A375) mutation to A: At least 90% decrease in substrate transport.
- Y382 (≠ W379) mutation to A: At least 90% decrease in substrate transport.
Sites not aligning to the query:
- 25 M→A: 25% decrease in substrate transport.
- 30 Y→A: At least 90% decrease in substrate transport.
- 471:511 mutation Missing: Shifts the pH-dependent substrate transport towards higher pH values. Transports Gln, but not Glu, at pH 7.0 or higher.
- 491 H→A: Allows substrate transport at pH 6.5.
- 497 R→A: Allows substrate transport at pH 6.5.
- 499 R→A: Allows substrate transport at pH 6.5.
- 502 H→A: Allows substrate transport at pH 6.5.
- 503 Y→A: Allows substrate transport at pH 6.5.
3l1lA Structure of arg-bound escherichia coli adic (see paper)
20% identity, 58% coverage: 73:344/470 of query aligns to 55:312/423 of 3l1lA
Sites not aligning to the query:
Query Sequence
>AO353_05930 FitnessBrowser__pseudo3_N2E3:AO353_05930
MTDTLGFETISNREHGLRRQLTSGQMSMIAIGGAIGTGLFMGSAYAIGYAGPSVLLSYAI
GAVITLLLMGCLAEMTVAHSTSGSFGAYAEFYISPLAGFLVRYAYWAAIVLAVGTEVTAV
AMYMKYWFANVPEWIWIVSFSSILIVLNAISVKTFGTFEYWFSTIKIGAIVGFIILAVYV
VFGSGNPEYGVHHYTSHGGFFPNGLQGMWVAVIVSIFSYLSVEMIAVAAGEAEDPERAVK
KAFRATIVRLVVFYLLTLALMLAIVPWVQAGHAQSPFVTVMQTIGIPGATGVMNFVILIA
ALSAMNSQLYITTRMMFSLSRGGYAPKAMGALSKSGIPLNALLLSSSGIALATLLNVMYP
ESSFTLMMAISMFGAIFTWFMIFLTHYCFRRYHQRHGERKLSFRMRLFPYTTLLGLVLMG
AVMITTYFTEAFKMTLVFGVPFLLILSLVYGVFFRKTRALAGTLDNAPAP
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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