SitesBLAST
Comparing PP_0660 PP_0660 S-methyl-L-methionine transporter 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)
41% identity, 94% coverage: 6:457/479 of query aligns to 3:469/489 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 (= W109) 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 (= F220) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E226) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E234) 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 (≠ D434) 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
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, 90% coverage: 10:441/479 of query aligns to 2:429/469 of P46349
- G33 (≠ T41) mutation to D: Lack of activity.
- G42 (= G50) mutation to S: Lack of activity.
- G301 (= G311) mutation to V: Lack of activity.
- G338 (≠ S348) mutation to E: Lack of activity.
- F341 (≠ G351) mutation to S: Lack of activity.
- G414 (≠ L426) mutation to R: Lack of activity.
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
38% identity, 86% coverage: 2:415/479 of query aligns to 5:412/458 of P24207
- R26 (= R23) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P51) 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 (≠ T90) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (= Y92) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ L93) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ G96) mutation to L: No effect on phenylalanine transport activity.
- F101 (≠ Y99) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W103) 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 (≠ W109) 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 (= E226) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (= R252) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P341) 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.
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)
36% identity, 80% coverage: 14:394/479 of query aligns to 9:386/457 of P15993
- Y103 (≠ W109) 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%.
P04817 Arginine permease CAN1; Canavanine resistance protein 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
31% identity, 94% coverage: 17:464/479 of query aligns to 85:551/590 of P04817
- P113 (≠ T45) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
- P148 (= P80) 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 (≠ E81) 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 (= G233) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
- P313 (= P238) 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 (≠ A369) 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 (≠ V379) 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)
31% identity, 82% coverage: 17:408/479 of query aligns to 81:481/587 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, 82% coverage: 17:409/479 of query aligns to 87:491/602 of P19145
- A297 (≠ S223) 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)
28% identity, 85% coverage: 4:409/479 of query aligns to 133:550/663 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)
22% identity, 87% coverage: 8:425/479 of query aligns to 269:761/852 of Q03770
- T382 (≠ I122) 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, 53% coverage: 17:269/479 of query aligns to 19:265/461 of P76037
- Y110 (≠ W109) 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)
23% identity, 86% coverage: 11:424/479 of query aligns to 18:421/458 of 6f34A
- binding arginine: I40 (≠ V33), G42 (= G35), T43 (= T36), G44 (= G37), E115 (≠ T108), Y116 (≠ W109), A119 (= A112), F228 (= F220), A229 (= A221), I231 (≠ S223), V314 (≠ A307)
- binding cholesterol: W201 (≠ G196), Y202 (≠ N197)
- binding : G28 (≠ Q21), F30 (≠ R23), D31 (≠ H24), M34 (= M27), A178 (≠ G183), R179 (≠ G184), A186 (≠ H191), I187 (vs. gap), A190 (vs. gap), L194 (vs. gap), Q296 (≠ I289), V299 (≠ A292)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
23% identity, 86% coverage: 11:424/479 of query aligns to 16:419/456 of 5oqtA
- binding alanine: I38 (≠ V33), G40 (= G35), T41 (= T36), G42 (= G37), F226 (= F220), A227 (= A221), I229 (≠ S223)
- binding : E24 (≠ D19), G26 (≠ Q21), F28 (≠ R23), D29 (≠ H24), M32 (= M27), A176 (≠ G183), R177 (≠ G184), A184 (≠ H191), A188 (vs. gap), L192 (vs. gap), Q294 (≠ I289), V297 (≠ A292)
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)
22% identity, 69% coverage: 30:359/479 of query aligns to 49:381/531 of Q9QXW9
- Y130 (vs. gap) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (≠ W109) 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 (= F220) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
23% identity, 71% coverage: 8:347/479 of query aligns to 2:329/445 of P60061
- I23 (≠ V33) binding ; binding
- S26 (≠ T36) binding
- Y93 (= Y105) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (vs. gap) binding ; binding
- C97 (≠ T108) binding
- N101 (≠ A112) 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 (≠ S115) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (≠ F220) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ A221) binding
- I205 (≠ S223) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (≠ G311) 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.
P60063 Arginine/agmatine antiporter from Escherichia coli O157:H7 (see 3 papers)
23% identity, 71% coverage: 8:347/479 of query aligns to 2:329/445 of P60063
- N22 (≠ G32) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ V33) binding
- GSG 25:27 (≠ GTG 35:37) Helix-breaking GSG motif TM1
- S26 (≠ T36) binding ; mutation to K: 5% Agm antiport.
- G27 (= G37) binding
- Y74 (≠ S86) mutation to A: 50% antiport activity at pH 6.0, 10-fold higher than wild-type antiport activity at pH 7.5, i.e. loss of pH-dependence of substrate transport. No change in binding of Arg or Agm.; mutation Y->C,H,L,M,Q,S: Loss of pH-dependence of substrate transport.; mutation to F: Approximately wild-type antiport.
- Y87 (= Y99) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y105) mutation to A: Reduced binding affinity for Arg, no binding to Agm. 25% Agm antiport.; mutation to K: Almost no binding to both Arg and Agm. 5% Agm antiport.
- A96 (vs. gap) binding
- C97 (≠ T108) binding
- N101 (≠ A112) binding
- W202 (≠ F220) Periplasmic (proximal) gate; binding
- I205 (≠ S223) binding
- GVESA 206:210 (≠ GTELI 224:228) Helix-breaking GVESA motif TM6
- E208 (= E226) mutation E->A,D: 5-10% Agm antiport.
- W293 (≠ G311) binding
Sites not aligning to the query:
- 337 F→A: Severely decreased antiport.
- 357 binding
- 365 Y→A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
24% identity, 67% coverage: 25:347/479 of query aligns to 11:325/437 of 5j4nA
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)
21% identity, 69% coverage: 30:359/479 of query aligns to 50:382/535 of Q9UHI5
- I53 (≠ V33) binding
- Y93 (≠ L72) 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 (≠ W109) 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 (≠ R126) modified: Interchain (with C-210 in SLC3A2)
- W174 (≠ I146) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (= F220) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ S223) 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 (≠ S278) 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
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
21% identity, 69% coverage: 30:359/479 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)
21% identity, 69% coverage: 30:359/479 of query aligns to 10:342/458 of 7cmiB
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
21% identity, 69% coverage: 30:359/479 of query aligns to 10:342/458 of 7cmhB
Sites not aligning to the query:
Query Sequence
>PP_0660 PP_0660 S-methyl-L-methionine transporter
MSVQTTTTRNASAHTFKQDMQTRHIVMLALGGVIGTGLFLTSGYTVNQAGPLGAVIAYIL
GAIMVYLVMMCLGELAVHMPEVGSFSSYATRYLGPGTGYMVAWMYWLTWTVAIGSEFTAA
GILMVRWFPDTPVWMWSALFGAAVFISNIISVRSFAETEFWLSLVKVLAVIAFLVVGGGA
ILGGFEIQQAHSAGLGNFTREGLFPTGFWSIAMTLLAVAFAFSGTELIGIAAGETKDPEK
NVPKAIRTTVLRLALFFIGTIFVLATLLPREQAGVIESPFVMVFAMIGIPYAADIMNFVI
ITALLSAANSGLYAASRMLWTLSDQGNMPRRYATLSRRGTPFNAIVLSMAGGMASLLSSV
FAPDTIYLALVSISGLAVVVVWISIAASQIAFRRHYIASGGKLEDLKFRVRGYPFVPLGA
IFCCVLACVGIAFDPAQRVALYFGLPFIAWCYLAYWLTCKYRSRRTAPLEIVAPGSEAA
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