SitesBLAST
Comparing BWI76_RS19685 FitnessBrowser__Koxy:BWI76_RS19685 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)
93% identity, 100% coverage: 1:488/489 of query aligns to 1:488/489 of P25737
- M1 (= M1) modified: Initiator methionine, Removed
- Y102 (= Y102) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (= W106) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K163) 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 (= D275) 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 (= D278) 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 (= E438) mutation to A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D443 (= D443) mutation to A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D446 (= D446) mutation to A: Retains 13% of wild-type lysine uptake activity. Is unable to inhibit CadC.
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
44% identity, 83% coverage: 12:418/489 of query aligns to 7:402/469 of P46349
- G33 (≠ A38) mutation to D: Lack of activity.
- G42 (= G47) mutation to S: Lack of activity.
- G301 (= G315) mutation to V: Lack of activity.
- G338 (≠ T352) mutation to E: Lack of activity.
- F341 (≠ I355) mutation to S: Lack of activity.
Sites not aligning to the query:
- 414 G→R: Lack of activity.
P04817 Arginine permease CAN1; Canavanine resistance protein 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
37% identity, 97% coverage: 3:476/489 of query aligns to 74:553/590 of P04817
- P113 (≠ T42) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
- P148 (= P77) 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 (= V78) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
- S152 (= S81) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
- Y173 (= Y102) 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 (≠ VK 276:277) mutation Missing: In CAN1-318; confers citrulline transport activity in GAP1-deleted cells.
- Y356 (≠ D278) 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 (= W373) 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 (= F383) mutation to S: In CAN1-307; confers citrulline transport activity in GAP1-deleted cells.
P19145 General amino-acid permease GAP1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
37% identity, 95% coverage: 7:471/489 of query aligns to 81:551/602 of P19145
- A297 (≠ Q219) 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)
Q9URZ4 Cationic amino acid transporter 1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
34% identity, 96% coverage: 3:469/489 of query aligns to 65:540/587 of Q9URZ4
Sites not aligning to the query:
- 29 modified: Phosphoserine
- 30 modified: Phosphoserine
- 37 modified: Phosphoserine
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
38% identity, 85% coverage: 3:420/489 of query aligns to 9:413/458 of P24207
- R26 (= R20) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P48) 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 (= F82) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y85) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ Q87) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (= Y89) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ V90) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ G93) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F96) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W100) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (= Y102) mutation to L: No effect on phenylalanine transport activity.
- W108 (= W103) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ W106) 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 (≠ D113) mutation E->G,L,V,N: Loss of activity.
- K168 (= K163) 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 (= P345) 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)
37% identity, 80% coverage: 13:404/489 of query aligns to 11:392/457 of P15993
- Y103 (≠ W106) 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%.
P48813 High-affinity glutamine permease from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
28% identity, 96% coverage: 4:471/489 of query aligns to 136:612/663 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)
26% identity, 98% coverage: 5:481/489 of query aligns to 269:816/852 of Q03770
- T382 (≠ Q118) 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.
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
29% identity, 85% coverage: 13:428/489 of query aligns to 21:419/456 of 5oqtA
- binding alanine: I38 (≠ S30), G40 (= G32), T41 (= T33), G42 (= G34), F226 (= F216), A227 (≠ S217), I229 (≠ Q219)
- binding : E24 (= E16), G26 (≠ K18), F28 (≠ R20), D29 (≠ H21), M32 (= M24), A176 (≠ G153), R177 (≠ E154), A184 (≠ L161), A188 (= A165), L192 (≠ I169), Q294 (vs. gap), V297 (vs. gap)
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
29% identity, 85% coverage: 13:428/489 of query aligns to 23:421/458 of 6f34A
- binding arginine: I40 (≠ S30), G42 (= G32), T43 (= T33), G44 (= G34), E115 (≠ N105), Y116 (≠ W106), A119 (vs. gap), F228 (= F216), A229 (≠ S217), I231 (≠ Q219), V314 (≠ A307)
- binding cholesterol: W201 (≠ M176), Y202 (≠ M177)
- binding : G28 (≠ K18), F30 (≠ R20), D31 (≠ H21), M34 (= M24), A178 (≠ G153), R179 (≠ E154), A186 (≠ L161), I187 (= I162), A190 (= A165), L194 (≠ I169), Q296 (vs. gap), V299 (vs. gap)
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
24% identity, 79% coverage: 13:398/489 of query aligns to 18:388/461 of P76037
- Y110 (≠ W106) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
27% identity, 51% coverage: 8:255/489 of query aligns to 3:242/438 of O34739
- C94 (≠ L98) 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 (≠ V175) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
Sites not aligning to the query:
- 291 C→S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
- 415 C→S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
21% identity, 91% coverage: 15:460/489 of query aligns to 2:424/433 of 6f2wA
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)
21% identity, 66% coverage: 7:330/489 of query aligns to 22:369/629 of P30825
- N226 (≠ G202) modified: carbohydrate, N-linked (GlcNAc...) asparagine
Q22397 Amino acid transporter protein 6 from Caenorhabditis elegans (see paper)
23% identity, 67% coverage: 27:356/489 of query aligns to 30:356/523 of Q22397
Sites not aligning to the query:
- 521:523 PDZ-binding motif; mutation Missing: Abolishes the interaction with nrfl-1.
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, 72% coverage: 12:363/489 of query aligns to 34:381/531 of Q9QXW9
- Y130 (= Y102) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (= N105) 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 (= F216) 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, 72% coverage: 13:363/489 of query aligns to 36:382/535 of Q9UHI5
- I53 (≠ S30) binding
- Y93 (≠ L69) 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 (= N105) 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 (≠ Y123) modified: Interchain (with C-210 in SLC3A2)
- W174 (≠ L143) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (= F216) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ Q219) 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 (≠ K277) 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
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
26% identity, 71% coverage: 22:369/489 of query aligns to 11:343/437 of 5j4nA
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
26% identity, 71% coverage: 22:369/489 of query aligns to 15:347/445 of P60061
- I23 (≠ S30) binding ; binding
- S26 (≠ T33) binding
- Y93 (= Y102) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (vs. gap) binding ; binding
- C97 (≠ N105) binding
- N101 (≠ T109) 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 (≠ V112) 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 (= S217) binding
- I205 (≠ Q219) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (≠ G315) 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
>BWI76_RS19685 FitnessBrowser__Koxy:BWI76_RS19685
MVSDTKTTEAPGLRRELKARHLTMIAIGGSIGTGLFVASGATISQAGPGGALLSYILIGL
MVYFLMTSLGELAAFMPVSGSFATYGQNYVEEGFGFALGWNYWYNWAVTIAVDLVAAQLV
MTYWFPDAPGWVWSALFLGIMFLLNWISVKGFGEAEYWFSLIKVATVIIFIIVGVMMIFG
IFKGAQPAGWSNWVIDDAPFAGGFAAMIGVAMIVGFSFQGTELIGIAAGESENPEKNIPR
AVRQVFWRILLFYVFAILIISLIIPYTDPSLLRNDVKDISVSPFTLVFQHAGLLSAAAIM
NAVILTAVLSAGNSGMYASTRMLYTLACDGKAPRIFSKLSKGGVPRNALYATTVIAGLCF
LSSMFGNQTVYLWLLNTSGMTGFIAWLGIAISHYRFRRGYVLQGNDLNDLPYRSGFFPLG
PIFAFVLCLIITLGQNYEAFLKDTIDWGGVAATYIGIPLFLVIWFGYKLAKGTRFVRYSE
MKFPERFKG
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