SitesBLAST
Comparing BWI76_RS06025 FitnessBrowser__Koxy:BWI76_RS06025 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
38% identity, 99% coverage: 2:464/468 of query aligns to 6:480/489 of P25737
- Y102 (= Y100) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (= W104) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K161) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F216) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E222) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E230) 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 (≠ G270) 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 (≠ D430) 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)
38% identity, 98% coverage: 4:462/468 of query aligns to 2:454/469 of P46349
- G33 (≠ N36) mutation to D: Lack of activity.
- G42 (= G45) mutation to S: Lack of activity.
- G301 (= G307) mutation to V: Lack of activity.
- G338 (≠ S344) mutation to E: Lack of activity.
- F341 (≠ G347) mutation to S: Lack of activity.
- G414 (≠ V422) 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)
35% identity, 99% coverage: 1:465/468 of query aligns to 1:457/457 of P15993
- Y103 (≠ W104) 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)
35% identity, 90% coverage: 2:422/468 of query aligns to 10:428/458 of P24207
- R26 (= R18) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (≠ A46) 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 (= F80) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y83) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ A85) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (= Y87) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ L88) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ A91) mutation to L: No effect on phenylalanine transport activity.
- F101 (≠ Y94) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W98) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (= Y100) mutation to L: No effect on phenylalanine transport activity.
- W108 (= W101) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ W104) 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 (≠ S111) mutation E->G,L,V,N: Loss of activity.
- K168 (= K161) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (= E222) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (= R248) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P337) 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, 88% coverage: 5:417/468 of query aligns to 78:500/590 of P04817
- P113 (≠ I40) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
- P148 (= P75) 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 (≠ E76) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
- S152 (≠ A79) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
- Y173 (= Y100) 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 (= G229) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
- P313 (= P234) 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 (≠ -A 269) mutation Missing: In CAN1-318; confers citrulline transport activity in GAP1-deleted cells.
- Y356 (≠ G270) 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 (≠ A365) 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 (≠ V375) 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, 90% coverage: 2:423/468 of query aligns to 71:503/587 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)
32% identity, 92% coverage: 2:431/468 of query aligns to 136:579/663 of P48813
Sites not aligning to the query:
- 132 modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
P19145 General amino-acid permease GAP1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
31% identity, 85% coverage: 11:407/468 of query aligns to 86:493/602 of P19145
- A297 (≠ S219) 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)
Q03770 SPS-sensor component SSY1; Amino-acid permease homolog SSY1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
23% identity, 97% coverage: 10:464/468 of query aligns to 276:815/852 of Q03770
- T382 (≠ G116) 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)
25% identity, 97% coverage: 5:459/468 of query aligns to 12:448/461 of P76037
- Y110 (≠ W104) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
23% identity, 94% coverage: 26:463/468 of query aligns to 21:435/445 of P60061
- I23 (≠ V28) binding ; binding
- S26 (≠ T31) binding
- Y93 (= Y100) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ T103) binding ; binding
- C97 (vs. gap) binding
- N101 (≠ A107) 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 (≠ S110) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (≠ F216) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ A217) binding
- I205 (≠ S219) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (≠ G307) 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.
- S357 (= S370) binding ; mutation to 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, 94% coverage: 26:463/468 of query aligns to 21:435/445 of P60063
- N22 (≠ G27) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ V28) binding
- GSG 25:27 (≠ GTG 30:32) Helix-breaking GSG motif TM1
- S26 (≠ T31) binding ; mutation to K: 5% Agm antiport.
- G27 (= G32) binding
- Y74 (≠ H81) 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 (= Y94) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y100) 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 (≠ T103) binding
- C97 (vs. gap) binding
- N101 (≠ A107) binding
- W202 (≠ F216) Periplasmic (proximal) gate; binding
- I205 (≠ S219) binding
- GVESA 206:210 (≠ GTELI 220:224) Helix-breaking GVESA motif TM6
- E208 (= E222) mutation E->A,D: 5-10% Agm antiport.
- W293 (≠ G307) binding
- F337 (= F353) mutation to A: Severely decreased antiport.
- S357 (= S370) binding
- Y365 (≠ W378) mutation to 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)
23% identity, 94% coverage: 26:463/468 of query aligns to 17:431/437 of 5j4nA
3l1lA Structure of arg-bound escherichia coli adic (see paper)
23% identity, 94% coverage: 26:463/468 of query aligns to 15:418/423 of 3l1lA
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
21% identity, 90% coverage: 1:420/468 of query aligns to 13:421/458 of 6f34A
- binding arginine: I40 (≠ V28), G42 (= G30), T43 (= T31), G44 (= G32), E115 (≠ T103), Y116 (≠ W104), A119 (= A107), F228 (= F216), A229 (= A217), I231 (≠ S219), V314 (≠ A303)
- binding cholesterol: W201 (≠ R192), Y202 (≠ N193)
- binding : G28 (≠ K16), F30 (≠ R18), D31 (≠ H19), M34 (= M22), A178 (= A175), R179 (≠ I176), A186 (≠ Q183), I187 (≠ D184), A190 (≠ P187), L194 (vs. gap), Q296 (≠ I285), V299 (≠ A288)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
21% identity, 90% coverage: 1:420/468 of query aligns to 11:419/456 of 5oqtA
- binding alanine: I38 (≠ V28), G40 (= G30), T41 (= T31), G42 (= G32), F226 (= F216), A227 (= A217), I229 (≠ S219)
- binding : E24 (≠ T14), G26 (≠ K16), F28 (≠ R18), D29 (≠ H19), M32 (= M22), A176 (= A175), R177 (≠ I176), A184 (≠ Q183), A188 (≠ P187), L192 (vs. gap), Q294 (≠ I285), V297 (≠ A288)
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
22% identity, 84% coverage: 25:418/468 of query aligns to 14:393/433 of 6f2wA
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
22% identity, 88% coverage: 4:415/468 of query aligns to 3:395/438 of O34739
- C94 (≠ V96) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ A137) 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 (≠ A303) 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.
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: 5:324/468 of query aligns to 22:371/629 of P30825
- N226 (≠ P187) modified: carbohydrate, N-linked (GlcNAc...) asparagine
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, 96% coverage: 6:453/468 of query aligns to 35:466/501 of Q9UPY5
- C86 (≠ M64) 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 (vs. gap) binding ; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (≠ Y121) 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 (≠ E154) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ V160) 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 (= K161) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
- Y244 (≠ F216) binding
- F254 (≠ I226) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ R243) 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 (≠ A299) 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 (≠ Y309) 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.
- R396 (≠ V377) mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.; mutation to N: Loss of L-cystine transport activity.
- C414 (≠ L399) mutation to 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.
- C435 (= C420) mutation to 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
>BWI76_RS06025 FitnessBrowser__Koxy:BWI76_RS06025
MQTTQQQGGQLKRTMKTRHLIMLSLGGVIGTGLFFNTGYIISTTGAAGTLLAYLIGALVV
WLVMQCLGELSVAMPETGAFHVYAARYLGPATGYTVAWLYWLTWTVALGSSFTAAGFCMQ
YWFPQVPVWVWCVVFCAVIFALNVISTRFFAEGEFWFSLVKVITIIAFIILGGAAIFGII
PMQDGSPAPGLRNITAEGWFPHGGLPILMTMVAVNFAFSGTELIGIAAGETENPHKVIPV
AIRTTIARLIIFFIGTVFVLAALIPMQQAGVEKSPFVLVFEKVGIPYAADIFNFVILTAI
LSAANSGLYASGRMLWSLSNENTLPACFTKLTRNGVPLTAISVSMLGGVLALFSSVVAPD
TVFVALSAISGFAVVAVWLSICASHFMFRRRHLQQGKALSELHYRAPWYPLVPALGFVLC
LVACVGLAFDPSQRIALWCGIPFVALCYGAYYLTRSRKLTQEPQHVAE
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