SitesBLAST
Comparing WP_012783773.1 NCBI__GCF_000022745.1:WP_012783773.1 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)
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
39% identity, 99% coverage: 1:463/467 of query aligns to 1:458/458 of P24207
- R26 (= R26) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P54) 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 (= F87) mutation to L: No effect on phenylalanine transport activity.
- F90 (= F90) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ G92) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (= Y94) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ L95) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ C98) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F101) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W105) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (= Y107) mutation to L: No effect on phenylalanine transport activity.
- W108 (= W108) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ W111) 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 (= E118) mutation E->G,L,V,N: Loss of activity.
- K168 (= K168) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (= E229) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (= R255) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P344) 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.
- P442 (= P447) mutation to A: 46% of wild-type phenylalanine transport activity.; mutation to G: 52% of wild-type phenylalanine transport activity.; mutation to L: 43% of wild-type phenylalanine transport activity.
Q88CZ8 L-histidine transporter HutT from Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) (see paper)
42% identity, 95% coverage: 14:457/467 of query aligns to 2:445/467 of Q88CZ8
- T27 (= T39) mutation T->A,S: Retains 60% of wild-type activity.; mutation to N: Retains 20% of wild-type activity.
- E98 (≠ C110) mutation to A: Retains 80% of wild-type activity.
- K156 (= K168) mutation K->A,Q: Retains less than 10% of wild-type activity.; mutation to R: Retains 40% of wild-type activity.
- F212 (= F223) mutation F->A,Q: Loss of activity.; mutation to Y: No change in activity.
- E218 (= E229) mutation E->A,Q: Loss of activity.; mutation to D: Retains 70% of wild-type 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)
39% identity, 95% coverage: 13:457/467 of query aligns to 5:444/457 of P15993
- Y103 (≠ W111) 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%.
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
37% identity, 86% coverage: 13:412/467 of query aligns to 2:396/469 of P46349
- G33 (= G44) mutation to D: Lack of activity.
- G42 (= G53) mutation to S: Lack of activity.
- G301 (= G314) mutation to V: Lack of activity.
- G338 (≠ S351) mutation to E: Lack of activity.
- F341 (= F354) mutation to S: Lack of activity.
Sites not aligning to the query:
- 414 G→R: Lack of activity.
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
36% identity, 94% coverage: 10:449/467 of query aligns to 4:447/489 of P25737
- Y102 (= Y107) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (= W111) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K168) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F223) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E229) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E237) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ Q275) 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 (= D277) 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 (≠ D438) mutation to A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D443 (≠ V445) mutation to A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D446 (≠ L448) 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
P04817 Arginine permease CAN1; Canavanine resistance protein 1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
32% identity, 85% coverage: 10:406/467 of query aligns to 75:487/590 of P04817
- P113 (≠ A48) mutation to L: In CAN1-343; confers citrulline transport activity in GAP1-deleted cells.
- P148 (≠ L82) 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 (≠ Q83) mutation to F: In CAN1-315; confers citrulline transport activity in GAP1-deleted cells.
- S152 (= S86) mutation to F: In CAN1-342; confers citrulline transport activity in GAP1-deleted cells.
- Y173 (= Y107) 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 (≠ A236) mutation to A: In CAN1-341; confers citrulline transport activity in GAP1-deleted cells.
- P313 (= P241) 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 (≠ L374) 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 (≠ I384) 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)
32% identity, 85% coverage: 19:415/467 of query aligns to 86:495/602 of P19145
- A297 (≠ V226) 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)
31% identity, 82% coverage: 14:398/467 of query aligns to 75:466/587 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)
27% identity, 84% coverage: 6:399/467 of query aligns to 132:535/663 of P48813
- K132 (= K6) 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, 85% coverage: 18:413/467 of query aligns to 276:750/852 of Q03770
- T382 (≠ S123) 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.
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, 87% coverage: 4:409/467 of query aligns to 14:446/629 of P30825
- N226 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
27% identity, 45% coverage: 202:413/467 of query aligns to 207:408/458 of 6f34A
Sites not aligning to the query:
- binding arginine: 40, 42, 43, 44, 115, 116, 119
- binding cholesterol: 201, 202
- binding : 28, 30, 31, 34, 178, 179, 186, 187, 190, 194
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
27% identity, 45% coverage: 202:413/467 of query aligns to 205:406/456 of 5oqtA
Sites not aligning to the query:
- binding alanine: 38, 40, 41, 42
- binding : 24, 26, 28, 29, 32, 176, 177, 184, 188, 192
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
22% identity, 74% coverage: 90:433/467 of query aligns to 76:402/445 of P60061
- Y93 (= Y107) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (vs. gap) binding agmatine; binding L-arginine
- C97 (= C110) binding agmatine
- N101 (≠ T114) binding agmatine; 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 (≠ E118) binding agmatine; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (≠ F223) binding L-arginine; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ A224) binding agmatine
- I205 (≠ V226) binding agmatine; binding L-arginine; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (≠ G314) binding agmatine; 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 (= S379) binding L-arginine; mutation to A: 20% decreased affinity for Arg, 40% decrease affinity for Agm.
Sites not aligning to the query:
- 23 binding agmatine; binding L-arginine
- 26 binding L-arginine
P60063 Arginine/agmatine antiporter from Escherichia coli O157:H7 (see 3 papers)
22% identity, 74% coverage: 90:433/467 of query aligns to 76:402/445 of P60063
- Y87 (≠ F101) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y107) 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 L-arginine
- C97 (= C110) binding L-arginine
- N101 (≠ T114) binding L-arginine
- W202 (≠ F223) Periplasmic (proximal) gate; binding L-arginine
- I205 (≠ V226) binding L-arginine
- GVESA 206:210 (≠ GIELV 227:231) Helix-breaking GVESA motif TM6
- E208 (= E229) mutation E->A,D: 5-10% Agm antiport.
- W293 (≠ G314) binding L-arginine
- F337 (= F354) mutation to A: Severely decreased antiport.
- S357 (= S379) binding L-arginine
- Y365 (≠ W387) mutation to A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.
Sites not aligning to the query:
- 22 N→A: No change in antiport activity, 6-fold higher affinity for Arg.
- 23 binding L-arginine
- 25:27 Helix-breaking GSG motif TM1
- 26 binding L-arginine; S→K: 5% Agm antiport.
- 27 binding L-arginine
- 74 Y→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.; Y→F: Approximately wild-type antiport.
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
22% identity, 74% coverage: 90:433/467 of query aligns to 72:398/437 of 5j4nA
Sites not aligning to the query:
3l1lA Structure of arg-bound escherichia coli adic (see paper)
22% identity, 87% coverage: 28:433/467 of query aligns to 9:385/423 of 3l1lA
P63235 Glutamate/gamma-aminobutyrate antiporter; Glu/GABA antiporter; Extreme acid sensitivity protein from Escherichia coli (strain K12) (see 2 papers)
24% identity, 51% coverage: 186:424/467 of query aligns to 163:417/511 of P63235
- L212 (≠ F223) mutation to A: 70% decrease in substrate transport.
- E218 (= E229) mutation to A: At least 90% decrease in substrate transport.
- E304 (≠ S310) mutation to A: At least 90% decrease in substrate transport.
- W308 (≠ G314) mutation to A: At least 90% decrease in substrate transport.
- Y378 (≠ F383) mutation to A: At least 90% decrease in substrate transport.
- Y382 (≠ W387) mutation to A: At least 90% decrease in substrate transport.
Sites not aligning to the query:
- 25 M→A: 25% decrease in substrate transport.
- 30 Y→A: At least 90% decrease in substrate transport.
- 471:511 mutation Missing: Shifts the pH-dependent substrate transport towards higher pH values. Transports Gln, but not Glu, at pH 7.0 or higher.
- 491 H→A: Allows substrate transport at pH 6.5.
- 497 R→A: Allows substrate transport at pH 6.5.
- 499 R→A: Allows substrate transport at pH 6.5.
- 502 H→A: Allows substrate transport at pH 6.5.
- 503 Y→A: Allows substrate transport at pH 6.5.
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
24% identity, 38% coverage: 73:249/467 of query aligns to 62:242/461 of P76037
- Y110 (≠ W111) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
P0AAF1 Putrescine transporter PotE; Putrescine-proton symporter / putrescine-ornithine antiporter from Escherichia coli (strain K12) (see 2 papers)
22% identity, 77% coverage: 19:379/467 of query aligns to 1:356/439 of P0AAF1
- C62 (≠ L74) mutation C->A,T: Strong decrease in both uptake and excretion activities.; mutation to S: Moderate decrease in both uptake and excretion activities.
- K68 (≠ S80) mutation to A: Slight decrease in both uptake and excretion activities.
- E77 (≠ D89) mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
- Y78 (≠ F90) mutation to L: Uptake activity decreases more than excretion activity.
- K82 (≠ P97) mutation to A: Slight decrease in both uptake and excretion activities.
- Y90 (≠ W105) mutation to L: Uptake activity decreases more than excretion activity.
- Y92 (= Y107) mutation to L: Moderate decrease in both uptake and excretion activities.
- W201 (≠ F223) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- E207 (= E229) mutation E->A,D,N,Q: Lack of both uptake and excretion activities.
- C210 (≠ G232) mutation to A: Moderate decrease in both uptake and excretion activities.
- C285 (≠ A307) mutation to A: Moderate decrease in both uptake and excretion activities.
- C286 (≠ S308) mutation to A: Moderate decrease in both uptake and excretion activities.
- W292 (≠ G314) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- K301 (≠ Y323) mutation to A: Excretion activity decreases more than uptake activity.
- Y308 (≠ L330) mutation to L: Excretion activity decreases more than uptake activity.
Sites not aligning to the query:
- 422 W→L: Uptake activity decreases more than excretion activity.
- 425 Y→F: Moderate decrease in both uptake and excretion activities.; Y→L: Strong decrease in both uptake and excretion activities.
- 433 mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
Query Sequence
>WP_012783773.1 NCBI__GCF_000022745.1:WP_012783773.1
MNTISKPSVDLHREEEPHLARNLSNRHLQLIAIGGTIGTGLFMGSGKAVSLAGPSILLIY
AITGFMLFFVMRALGEILLSNLQYRSFADFAGDYLGPCAQFFTGWTYWLCWIVTAVAEVV
AVSGYVSFWFPHLAPWIPALGLITILLILNLPTVRNFGEIEFWFALIKIITIIGLIITGI
YMLMTGFVLPNGTQASIAHLWNHGGFFPNGSLGFIAGFQISVFAFVGIELVGTAAAEAEN
PMRNLPKAINNIPIRIVLFYIGALFVIITVTPWNQVDPNSSPFVAMFSLAGIGIAAHFIN
FVVLTSASSSSNSGIYSTSRMVYGLATVGLAPKAFSKLSNRKVPVHALIFSCIFLLSSVV
LLYAGQSMIQVFTLVTTISALLFIFIWSIILVSYLQYRRKHLERHEKSTFKMPGGRASVV
MVFIFFAFVLWALTQEPDTLAAMKVTPLWFVLLGIAYWVMKLKQKQS
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