SitesBLAST
Comparing PfGW456L13_3211 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3211 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)
43% identity, 93% coverage: 4:445/474 of query aligns to 3:448/489 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 (≠ Y221) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E227) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E235) 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 (≠ D435) mutation to A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D443 (≠ P440) mutation to A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D446 (≠ Y443) 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, 95% coverage: 16:463/474 of query aligns to 8:449/469 of P46349
- G33 (= G41) mutation to D: Lack of activity.
- G42 (= G50) mutation to S: Lack of activity.
- G301 (= G312) mutation to V: Lack of activity.
- G338 (≠ T349) mutation to E: Lack of activity.
- F341 (= F352) mutation to S: Lack of activity.
- G414 (≠ S427) 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: 10:443/474 of query aligns to 5:431/457 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%.
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
37% identity, 92% coverage: 5:441/474 of query aligns to 8:437/458 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 (≠ H88) 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 (≠ I93) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ A96) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F99) 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 (= E227) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (= R253) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P342) 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)
33% identity, 87% coverage: 12:424/474 of query aligns to 80:505/590 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 (= V81) 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 (= G234) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
- P313 (= P239) 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 (≠ V370) 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 (≠ T380) 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)
33% identity, 88% coverage: 7:425/474 of query aligns to 71:500/587 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: 16:412/474 of query aligns to 86:493/602 of P19145
- A297 (≠ Q224) 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, 86% coverage: 3:411/474 of query aligns to 132:551/663 of P48813
- K132 (≠ E3) 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, 90% coverage: 6:430/474 of query aligns to 267:767/852 of Q03770
- T382 (≠ G121) 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)
23% identity, 96% coverage: 7:463/474 of query aligns to 14:454/458 of 6f34A
- binding arginine: I40 (≠ V33), G42 (= G35), T43 (= T36), G44 (= G37), E115 (≠ S108), Y116 (≠ W109), A119 (≠ G114), F228 (≠ Y221), A229 (= A222), I231 (≠ Q224), V314 (= V308)
- binding cholesterol: W201 (vs. gap), Y202 (vs. gap)
- binding : G28 (≠ K21), F30 (≠ R23), D31 (≠ H24), M34 (= M27), A178 (≠ M195), R179 (≠ A196), A186 (vs. gap), I187 (vs. gap), A190 (vs. gap), L194 (vs. gap), Q296 (≠ I290), V299 (≠ A293)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
23% identity, 96% coverage: 7:463/474 of query aligns to 12:452/456 of 5oqtA
- binding alanine: I38 (≠ V33), G40 (= G35), T41 (= T36), G42 (= G37), F226 (≠ Y221), A227 (= A222), I229 (≠ Q224)
- binding : E24 (≠ A19), G26 (≠ K21), F28 (≠ R23), D29 (≠ H24), M32 (= M27), A176 (≠ M195), R177 (≠ A196), A184 (vs. gap), A188 (vs. gap), L192 (vs. gap), Q294 (≠ I290), V297 (≠ A293)
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
23% identity, 88% coverage: 4:422/474 of query aligns to 2:397/438 of O34739
- C94 (≠ I101) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ V142) 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 (≠ V308) 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.
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
24% identity, 49% coverage: 15:247/474 of query aligns to 17:242/461 of P76037
- Y110 (≠ W109) 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, 92% coverage: 30:465/474 of query aligns to 14:433/433 of 6f2wA
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)
22% identity, 73% coverage: 13:360/474 of query aligns to 33:382/535 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 (≠ G146) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (≠ Y221) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ Q224) 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 (= V288) 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)
23% identity, 70% coverage: 30:360/474 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: 30:360/474 of query aligns to 10:342/458 of 7cmiB
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
23% identity, 70% coverage: 30:360/474 of query aligns to 10:342/458 of 7cmhB
Sites not aligning to the query:
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, 75% coverage: 4:360/474 of query aligns to 23:381/531 of Q9QXW9
- Y130 (≠ W106) 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 (≠ Y221) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
Q9UPY5 Cystine/glutamate transporter; Amino acid transport system xc-; Calcium channel blocker resistance protein CCBR1; Solute carrier family 7 member 11; xCT from Homo sapiens (Human) (see 4 papers)
23% identity, 64% coverage: 42:346/474 of query aligns to 67:369/501 of Q9UPY5
- C86 (≠ A61) mutation to S: Does not affect L-cystine transport activity; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- R135 (≠ S108) binding ; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (vs. gap) modified: Interchain (with C-210 in SLC3A2); mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- Q191 (≠ E159) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ I165) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-271; S-327; S-414 and S-435.
- K198 (= K166) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
- Y244 (= Y221) binding
- F254 (≠ V231) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ R248) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- C327 (≠ A304) mutation to A: Does not affect L-glutamate transport activity. Does not affect location at cell membrane Does not affect expression level.; mutation to L: Loss of L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.; mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Loss of inhibitio nof L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid. Decrease L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.; mutation to T: Does not affect L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.
- F336 (≠ Y314) mutation to A: Decreases L-cystine transport activity about 50%. Increases sensitivity to erastin-induced ferroptosis. Significantly decreases the L-cystine transport activity.; mutation to Y: Does not affect L-cystine transport activity.
Sites not aligning to the query:
- 396 R→A: Loss of L-cystine transport activity.; R→K: Loss of L-cystine transport activity.; R→N: Loss of L-cystine transport activity.
- 414 C→S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- 435 C→S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
Query Sequence
>PfGW456L13_3211 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3211
MNENTDRSTDHKGIQLTRALKSRHIFMLSLGGVIGTGLFMGSGVTINQGGPVGAILAYLV
AGFLMYLVMVCLGELSVQMPVSGSFQTHATKYIGPATGFMIGWVYWMSWATTVGLEFTAA
GMLMTRWFPEVPIWYWSALFVVVLFGINAMATRAFGEAEYWFSGIKVAAILGFIVVGVLV
IFGVMPLSSGAPAPMATNLIGDSLFPNGLSAVFAVMMTVVYAFQGCEIMGVAAGETDQPE
KSIPRAVRNVVFRVLIFYVLAIIVLSAIVPWQQAGLMESPFVQVFDMVGIPYAADLMNFV
ILTAILSVGNSGLYASTRILWAMSKTGMAPKSLSPLSKRGVPLRALSITLCFALVSLMTS
FVAADTLFMVLMAVSGMSGTVTWIVIALAQYKFRKAYLRDGGKLRDLKYRAPWFPVLPLM
CITLCCSLFVFLALDETQRPSLYWGFGFIALCYGAYFLIHRKRGAVLAPSLPAA
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