SitesBLAST
Comparing AO353_24825 FitnessBrowser__pseudo3_N2E3:AO353_24825 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)
44% identity, 94% coverage: 1:441/470 of query aligns to 2:448/489 of P25737
- Y102 (= Y101) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (= W105) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K162) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (≠ Y217) 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 (≠ D431) mutation to A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D443 (≠ P436) mutation to A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D446 (≠ Y439) 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
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
38% identity, 97% coverage: 12:468/470 of query aligns to 8:459/469 of P46349
- G33 (= G37) mutation to D: Lack of activity.
- G42 (= G46) mutation to S: Lack of activity.
- G301 (= G308) mutation to V: Lack of activity.
- G338 (≠ T345) mutation to E: Lack of activity.
- F341 (= F348) mutation to S: Lack of activity.
- G414 (≠ S423) 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, 92% coverage: 6:439/470 of query aligns to 5:431/457 of P15993
- Y103 (≠ W105) 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)
38% identity, 91% coverage: 12:437/470 of query aligns to 19:437/458 of P24207
- R26 (= R19) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P47) 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 (= F81) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ H84) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ T86) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (≠ F88) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ I89) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ A92) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F95) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W99) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (= Y101) mutation to L: No effect on phenylalanine transport activity.
- W108 (= W102) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ W105) 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 (= E112) mutation E->G,L,V,N: Loss of activity.
- K168 (= K162) 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.
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.
P04817 Arginine permease CAN1; Canavanine resistance protein 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
34% identity, 87% coverage: 6:413/470 of query aligns to 78:498/590 of P04817
- P113 (≠ T41) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
- P148 (= P76) 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 (= V77) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
- S152 (= S80) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
- Y173 (= Y101) 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 (≠ V366) 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 (≠ T376) 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, 86% coverage: 7:408/470 of query aligns to 75:484/587 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)
32% identity, 84% coverage: 12:408/470 of query aligns to 86:493/602 of P19145
- A297 (≠ Q220) 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)
29% identity, 86% coverage: 3:407/470 of query aligns to 136:551/663 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)
26% identity, 89% coverage: 8:426/470 of query aligns to 273:767/852 of Q03770
- T382 (≠ M118) 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.
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
24% identity, 98% coverage: 1:460/470 of query aligns to 13:455/458 of 6f34A
- binding arginine: I40 (≠ V29), G42 (= G31), T43 (= T32), G44 (= G33), E115 (≠ S104), Y116 (≠ W105), A119 (≠ G110), F228 (≠ Y217), A229 (= A218), I231 (≠ Q220), V314 (= V304)
- binding cholesterol: W201 (vs. gap), Y202 (vs. gap)
- binding : G28 (≠ K17), F30 (≠ R19), D31 (≠ H20), M34 (= M23), A178 (≠ T184), R179 (≠ S185), A186 (≠ M192), I187 (≠ S193), A190 (≠ I196), L194 (= L200), Q296 (≠ I286), V299 (≠ A289)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
24% identity, 98% coverage: 1:460/470 of query aligns to 11:453/456 of 5oqtA
- binding alanine: I38 (≠ V29), G40 (= G31), T41 (= T32), G42 (= G33), F226 (≠ Y217), A227 (= A218), I229 (≠ Q220)
- binding : E24 (≠ A15), G26 (≠ K17), F28 (≠ R19), D29 (≠ H20), M32 (= M23), A176 (≠ T184), R177 (≠ S185), A184 (≠ M192), A188 (≠ I196), L192 (= L200), Q294 (≠ I286), V297 (≠ A289)
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
24% identity, 84% coverage: 24:419/470 of query aligns to 20:398/438 of O34739
- C94 (≠ I97) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ V138) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ V174) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ V304) 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.
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
21% identity, 92% coverage: 26:458/470 of query aligns to 14:430/433 of 6f2wA
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
24% identity, 50% coverage: 11:243/470 of query aligns to 17:242/461 of P76037
- Y110 (≠ W105) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
23% identity, 70% coverage: 26:356/470 of query aligns to 10:342/457 of 7b00A
Sites not aligning to the query:
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
23% identity, 70% coverage: 26:356/470 of query aligns to 10:342/458 of 7cmiB
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
23% identity, 70% coverage: 26:356/470 of query aligns to 10:342/458 of 7cmhB
Sites not aligning to the query:
Q9UHI5 Large neutral amino acids transporter small subunit 2; L-type amino acid transporter 2; hLAT2; Solute carrier family 7 member 8 from Homo sapiens (Human) (see 3 papers)
23% identity, 70% coverage: 26:356/470 of query aligns to 50:382/535 of Q9UHI5
- I53 (≠ V29) binding
- Y93 (≠ L68) mutation to A: Nearly complete reduction of glycine, L-alanine, and L-glutamine uptake. Minimal effect on the transport of L-isoleucine, L-histidine and L-tryptophan.
- N134 (≠ W105) Important for substrate specificity; binding ; mutation to Q: Reduces L-leucine uptake activity. Abolishes L-tryptophan uptake.; mutation to S: The substrate specificity changed dramatically reducing L-glutamine, glycine and L-alanine uptake activity thus mimicking the selectivity of SLC7A5.
- C154 (≠ V127) modified: Interchain (with C-210 in SLC3A2)
- W174 (≠ G142) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (≠ Y217) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ Q220) Important for substrate specificity; binding ; mutation to S: Strong decrease in the uptake of large substrates L-tryptophan, L-glutamine, and L-histidine but increases the uptake of small neutral amino acids glycine and L-alanine.
- V302 (= V284) to I: found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity
Sites not aligning to the query:
- 395 binding ; N→Q: Strongly reduces L-leucine uptake activity. Strongly reduces L-tryptophan uptake activity.
- 396 Y→A: Strongly reduces L-leucine uptake activity.
- 402 T → M: found in a patient with age-related hearing loss; strongly decreased L-alanine transport activity. Decreases L-tyrosine transport activity
- 418 R → C: found in a patient with age-related hearing loss; decreases L-alanine transport activity. Decreases L-tyrosine transport activity
- 460 V → E: found in a patient with age-related hearing loss; strongly decreases L-alanine transport activity. Decreases L-tyrosine transport activity. Decreases cell membrane localization
7epzB Overall structure of erastin-bound xct-4f2hc complex (see paper)
24% identity, 65% coverage: 38:342/470 of query aligns to 23:325/453 of 7epzB
Sites not aligning to the query:
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
24% identity, 65% coverage: 38:342/470 of query aligns to 23:325/455 of 7p9uB
Query Sequence
>AO353_24825 FitnessBrowser__pseudo3_N2E3:AO353_24825
MSESIERKGIHLTRALKSRHIFMLSLGGVIGTGLFMGSGVTINQGGPVGAILAYLIAGFL
MYLVMVCLGELSVQMPVSGSFQTHATKFIGPATGFMIGWVYWMSWASTVGLEFTAAGMLM
VRWFPTVPIWYWSALFVVVLFGLNALATRAFGEAEYWFSGIKVAAILGFIVVGVLVIFGA
IPLTSGAPAPMMSNLIGDSLFPNGLPAVFAVMMTVVYAFQGCEIMGVAAGETDQPEKSIP
RAVRNVVFRVLIFYVLAIVVLSAIVPWQQAGLMESPFVQVFDMVGIPYAADLMNFVILTA
ILSVGNSGLYASTRILWAMSKTGMAPKSLSPLSKRGVPLRALSITLCFALVSLMTSFIAA
DTLFMVLMAVSGMSGTVTWIVIALAQYKFRRAYIRDGGKLSDLKYRAPWFPLLPILCIAL
CCSLFVFLAMDETQRPSLYWGFGFMALCYGAYFLIQRKRQAVLAPSLPTV
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