SitesBLAST
Comparing H281DRAFT_04042 FitnessBrowser__Burk376:H281DRAFT_04042 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 17 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)
71% identity, 88% coverage: 51:497/506 of query aligns to 5:453/457 of P15993
- Y103 (= Y147) 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)
62% identity, 88% coverage: 51:494/506 of query aligns to 15:458/458 of P24207
- R26 (= R62) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P90) 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 (= F123) mutation to L: No effect on phenylalanine transport activity.
- F90 (= F126) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (= Y128) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (= Y130) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (= W131) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (= F134) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F137) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W141) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (= Y143) mutation to L: No effect on phenylalanine transport activity.
- W108 (= W144) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ Y147) 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 (= E154) mutation E->G,L,V,N: Loss of activity.
- K168 (= K204) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (= E262) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (= R288) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P377) 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 (= P478) 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)
36% identity, 90% coverage: 51:506/506 of query aligns to 4:462/469 of P46349
- G33 (= G80) mutation to D: Lack of activity.
- G42 (= G89) mutation to S: Lack of activity.
- G301 (= G347) mutation to V: Lack of activity.
- G338 (≠ S384) mutation to E: Lack of activity.
- F341 (≠ A387) mutation to S: Lack of activity.
- G414 (≠ L459) 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, 87% coverage: 51:492/506 of query aligns to 9:471/489 of P25737
- Y102 (= Y143) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ Y147) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K204) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F256) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E262) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E270) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ E308) 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 (≠ A311) 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 (vs. gap) mutation to A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D446 (vs. gap) 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
P19145 General amino-acid permease GAP1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
33% identity, 92% coverage: 15:477/506 of query aligns to 43:521/602 of P19145
- K76 (≠ Q51) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
- A297 (≠ G259) mutation to V: Impairs basic amino-acids transport and regulation by these amino-acids.
P04817 Arginine permease CAN1; Canavanine resistance protein 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
33% identity, 84% coverage: 42:467/506 of query aligns to 71:516/590 of P04817
- P113 (≠ V84) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
- P148 (= P118) 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 (= V119) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
- S152 (= S122) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
- Y173 (= Y143) 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 (≠ A269) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
- P313 (= P274) 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 (≠ L405) 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 (≠ V415) 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)
35% identity, 83% coverage: 48:466/506 of query aligns to 71:504/587 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)
30% identity, 78% coverage: 47:439/506 of query aligns to 137:544/663 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)
25% identity, 78% coverage: 45:438/506 of query aligns to 267:743/852 of Q03770
- T382 (≠ G159) 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.
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)
24% identity, 66% coverage: 46:380/506 of query aligns to 19:388/629 of P30825
- N226 (≠ H223) 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, 65% coverage: 86:414/506 of query aligns to 55:389/458 of 6f34A
- binding arginine: E115 (≠ L146), Y116 (= Y147), A119 (≠ V150), F228 (= F256), A229 (≠ S257), I231 (≠ G259), V314 (= V343)
- binding cholesterol: W201 (vs. gap), Y202 (vs. gap)
- binding : A178 (≠ S229), R179 (≠ I230), A186 (vs. gap), I187 (vs. gap), A190 (vs. gap), L194 (vs. gap), Q296 (≠ S325), V299 (≠ T328)
Sites not aligning to the query:
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
24% identity, 88% coverage: 51:496/506 of query aligns to 4:438/438 of O34739
- C94 (≠ S139) 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 (≠ G210) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ V343) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
- C415 (≠ P468) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
23% identity, 65% coverage: 86:414/506 of query aligns to 53:387/456 of 5oqtA
Sites not aligning to the query:
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
27% identity, 34% coverage: 111:282/506 of query aligns to 74:242/461 of P76037
- Y110 (= Y147) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
22% identity, 59% coverage: 67:365/506 of query aligns to 12:308/433 of 6f2wA
P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
25% identity, 28% coverage: 245:386/506 of query aligns to 187:328/444 of P0AAE8
- C196 (≠ I254) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E204 (= E262) 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 (= Y293) 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 (= Y304) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C282 (≠ A340) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- R299 (≠ G357) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
- D303 (≠ Q361) 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 (≠ L368) 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.
- 73 Y→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.
- 76 E→Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- 89 Y→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.
- 90 Y→L: Strong decrease in both cadaverine excretion and cadaverine uptake.
- 107 Y→L: Strong decrease in cadaverine uptake.
- 125 C→S: Does not affect cadaverine excretion and cadaverine uptake.
- 174 Y→L: Moderate decrease in cadaverine uptake.
- 185 D→N: Moderate 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.
P39277 L-methionine/branched-chain amino acid exporter YjeH from Escherichia coli (strain K12) (see paper)
26% identity, 30% coverage: 246:398/506 of query aligns to 185:332/418 of P39277
- W195 (≠ F256) mutation to A: Strong decrease in methionine efflux.
Sites not aligning to the query:
- 24 T→Y: Strong decrease in methionine efflux.
- 25 G→F: Strong decrease in methionine efflux.
Query Sequence
>H281DRAFT_04042 FitnessBrowser__Burk376:H281DRAFT_04042
VPVRCKKSAGWYQYLGNIGRGKIFGSAGADHKSGRAIEIHTLGRNLDNALQQDGLKRGLK
NRHIQLIALGGAIGTGLFLGSASVLQAAGPSMILGYAIGGVIAFMIMRQLGEMVAQEPVA
GSFSHFAYKYWGDFPGFLSGWNYWVLYVLVSMAELTAVGTYVHYWWPGVPTWVSALVCFA
GINAINLANVKAYGETEFWFAIIKVVAVIGMILFGGYLLVSGHGGPQASISNLWSHGGFF
PHGFHGLFTMLAVIMFSFGGLELIGITAAEADEPQKSIPKAVNQVIYRILIFYICSLAVL
LSLYPWNEVAAGGSPFVMIFSQIGSTLTANVLNVVVLTAALSVYNSGVYANSRMLYGLAE
QGNAPRALMKVDRRGVPYMAIGLSALATFTCVIVNYLIPAEALGLLMALVVAALVLNWAL
ISLTHLKSRRAMVAAGETLVFKSFWFPVSNWICLAFMALILVILAMTPGLSVSVLLVPVW
LVVMWAGYAFKRRRAAAHVAARVVGR
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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