SitesBLAST
Comparing H281DRAFT_01668 FitnessBrowser__Burk376:H281DRAFT_01668 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)
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
42% identity, 97% coverage: 6:449/459 of query aligns to 8:452/469 of P46349
- G33 (= G31) mutation to D: Lack of activity.
- G42 (= G40) mutation to S: Lack of activity.
- G301 (≠ F299) mutation to V: Lack of activity.
- G338 (≠ C336) mutation to E: Lack of activity.
- F341 (≠ V339) mutation to S: Lack of activity.
- G414 (≠ A412) 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)
38% identity, 89% coverage: 5:414/459 of query aligns to 10:417/457 of P15993
- Y103 (≠ S98) 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%.
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
37% identity, 90% coverage: 6:417/459 of query aligns to 13:436/489 of P25737
- Y102 (= Y94) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ S98) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K155) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F208) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E214) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E222) 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.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 438 E→A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 443 D→A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 446 D→A: Retains 13% of wild-type lysine uptake activity. Is unable to inhibit CadC.
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
36% identity, 90% coverage: 2:414/459 of query aligns to 15:427/458 of P24207
- R26 (= R13) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P41) 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 (= F74) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y77) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ N79) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (= Y81) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ L82) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ W85) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F88) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W92) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (= Y94) mutation to L: No effect on phenylalanine transport activity.
- W108 (= W95) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ S98) 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 (= E105) mutation E->G,L,V,N: Loss of activity.
- K168 (= K155) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (= E214) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (= R240) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P329) 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)
31% identity, 92% coverage: 1:422/459 of query aligns to 79:521/590 of P04817
- P113 (≠ I35) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
- P148 (= P69) 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 (≠ D70) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
- S152 (= S73) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
- Y173 (= Y94) 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 (= G221) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
- P313 (= P226) 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 (≠ M357) 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 (≠ M367) 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, 73% coverage: 5:338/459 of query aligns to 79:418/587 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)
31% identity, 89% coverage: 6:414/459 of query aligns to 86:507/602 of P19145
- A297 (≠ G211) 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)
27% identity, 85% coverage: 1:389/459 of query aligns to 140:542/663 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)
24% identity, 90% coverage: 2:413/459 of query aligns to 273:763/852 of Q03770
- T382 (≠ I107) 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)
24% identity, 84% coverage: 6:390/459 of query aligns to 18:397/461 of P76037
- Y110 (= Y94) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
25% identity, 88% coverage: 5:408/459 of query aligns to 22:419/458 of 6f34A
- binding arginine: I40 (≠ V23), G42 (= G25), T43 (≠ A26), G44 (= G27), E115 (vs. gap), Y116 (vs. gap), A119 (vs. gap), F228 (= F208), A229 (≠ S209), I231 (≠ G211), V314 (= V287)
- binding cholesterol: W201 (≠ L170), Y202 (≠ F171)
- binding : G28 (≠ K11), F30 (≠ R13), D31 (≠ H14), M34 (= M17), A178 (= A147), R179 (≠ E148), A186 (≠ K155), I187 (≠ V156), A190 (≠ I159), L194 (≠ M163), Q296 (≠ L271), V299 (≠ M274)
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, 68% coverage: 2:314/459 of query aligns to 24:369/629 of P30825
- N226 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
25% identity, 88% coverage: 5:408/459 of query aligns to 20:417/456 of 5oqtA
- binding alanine: I38 (≠ V23), G40 (= G25), T41 (≠ A26), G42 (= G27), F226 (= F208), A227 (≠ S209), I229 (≠ G211)
- binding : E24 (≠ S9), G26 (≠ K11), F28 (≠ R13), D29 (≠ H14), M32 (= M17), A176 (= A147), R177 (≠ E148), A184 (≠ K155), A188 (≠ I159), L192 (≠ M163), Q294 (≠ L271), V297 (≠ M274)
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
23% identity, 94% coverage: 18:449/459 of query aligns to 12:433/433 of 6f2wA
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
23% identity, 98% coverage: 2:449/459 of query aligns to 4:438/438 of O34739
- C94 (≠ V90) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ S140) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ A167) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ V295) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
- C415 (≠ F425) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.
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)
23% identity, 74% coverage: 5:344/459 of query aligns to 34:375/531 of Q9QXW9
- Y130 (≠ T101) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (≠ V104) 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 (= F208) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
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, 74% coverage: 5:344/459 of query aligns to 35:376/535 of Q9UHI5
- I53 (≠ V23) binding
- Y93 (≠ L61) 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 (≠ V104) 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 (≠ W119) modified: Interchain (with C-210 in SLC3A2)
- W174 (vs. gap) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (= F208) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (= G211) 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 (= V269) 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
P39277 L-methionine/branched-chain amino acid exporter YjeH from Escherichia coli (strain K12) (see paper)
27% identity, 42% coverage: 178:368/459 of query aligns to 176:354/418 of P39277
- W195 (≠ F208) 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.
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
21% identity, 70% coverage: 15:335/459 of query aligns to 11:325/437 of 5j4nA
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
21% identity, 70% coverage: 15:335/459 of query aligns to 15:329/445 of P60061
- I23 (≠ V23) binding ; binding
- S26 (≠ A26) binding
- Y93 (= Y94) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ K97) binding ; binding
- C97 (≠ S98) binding
- N101 (≠ I102) 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 (≠ E105) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (≠ F208) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (= S209) binding
- I205 (≠ G211) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (≠ F299) 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.
Query Sequence
>H281DRAFT_01668 FitnessBrowser__Burk376:H281DRAFT_01668
MQDYSLKKSLKQRHITMIALGGVIGAGLFVGSGSIIATAGPAAILSYLIGGVMVTLVMFM
LGEMASRNPDSGSFSTYANSYLGEWAGFAVGWLYWFKSMITITVEAILLGAILHDFLPWL
PVPAGALFMLIALMATNAYSVRAFGEAEYWLSFAKVATIIVFMVLGASILFGLQPGIPAP
GLLNLTDHGGFMPNGISPVISGVMVVIFSLGGSEIAAVAAGESENPSKNVIRAIKSVILR
VMVFYVGSVSILILCMPWTDKANLKSPYVSLFSMAGFTGAAVAMKIVLFVSFMSVMNSFL
FSNSRMLFSLSQRGHAPAMFGRTNAKGVPMNALVLCLVVCVSILGIHFLSGGDLFLMLAK
SSGAFVMIVWIFIIVAHFAMRRQTKHEQRDPASFRAWFYPVSNWVALLALVAVLGSQAFN
PESRFQFWFAVSTALAIVAWYYVRRRHPSFGQTSGAKVR
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