SitesBLAST
Comparing PP_1259 FitnessBrowser__Putida:PP_1259 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)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
30% identity, 80% coverage: 6:435/537 of query aligns to 22:447/456 of 5oqtA
- binding alanine: I38 (= I22), G40 (vs. gap), T41 (vs. gap), G42 (vs. gap), F226 (= F208), A227 (= A209), I229 (≠ L211)
- binding : E24 (≠ Q8), G26 (≠ S10), F28 (≠ L12), D29 (= D13), M32 (≠ F16), A176 (= A154), R177 (≠ K155), A184 (≠ V162), A188 (≠ I166), L192 (= L170), Q294 (≠ R277), V297 (≠ L288)
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
30% identity, 80% coverage: 6:435/537 of query aligns to 24:449/458 of 6f34A
- binding arginine: I40 (= I22), G42 (vs. gap), T43 (vs. gap), G44 (vs. gap), E115 (≠ A96), Y116 (≠ F97), A119 (= A107), F228 (= F208), A229 (= A209), I231 (≠ L211), V314 (≠ C303)
- binding cholesterol: W201 (≠ T177), Y202 (≠ F178)
- binding : G28 (≠ S10), F30 (≠ L12), D31 (= D13), M34 (≠ F16), A178 (= A154), R179 (≠ K155), A186 (≠ V162), I187 (≠ F163), A190 (≠ I166), L194 (= L170), Q296 (≠ R277), V299 (≠ L288)
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)
25% identity, 73% coverage: 4:393/537 of query aligns to 27:438/629 of P30825
- N226 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
25% identity, 77% coverage: 7:418/537 of query aligns to 2:401/433 of 6f2wA
P82251 b(0,+)-type amino acid transporter 1; b(0,+)AT1; Glycoprotein-associated amino acid transporter b0,+AT1; Solute carrier family 7 member 9 from Homo sapiens (Human) (see 11 papers)
25% identity, 74% coverage: 2:397/537 of query aligns to 23:409/487 of P82251
- V40 (≠ L19) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ IFGSG 22:26) binding
- I44 (≠ F23) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (≠ A30) to F: in CSNU; uncertain significance
- P52 (≠ A31) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (≠ F47) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y76) to H: in CSNU; uncertain significance
- G105 (= G82) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (≠ F91) to R: in CSNU; uncertain significance
- I120 (≠ F97) to L: in CSNU; uncertain significance
- T123 (≠ S99) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (≠ A122) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ S124) modified: Interchain (with C-114 in SLC3A1)
- V170 (= V150) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ V162) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (vs. gap) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ I206) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (≠ I207) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (vs. gap) to D: in CSNU; decreased amino acid transport activity
- W230 (vs. gap) to R: in CSNU; complete loss of amino acid transport activity; mutation to A: Abolishes amino acid transport activity.
- D233 (≠ L211) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ L213) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ P215) mutation to A: Reduces amino acid transport activity.
- G259 (≠ S237) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ L239) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (≠ N263) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ M308) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ T311) to E: in CSNU; uncertain significance
- V330 (≠ G317) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ W318) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (≠ Q320) to Q: in CSNU; decreased amino acid transport activity; dbSNP:rs769576205; to W: in CSNU; severe loss of amino acid transport activity; dbSNP:rs121908484
- A354 (= A341) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (= S367) mutation to A: Markedly reduces amino acid transport activity.
- A382 (≠ L370) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (≠ V371) mutation to A: Complete loss of amino acid transport activity.
- Y386 (= Y374) mutation to A: Loss of amino acid transport activity.
- K401 (≠ P389) to E: in CSNU; uncertain significance; dbSNP:rs760264924
Sites not aligning to the query:
- 426 L → P: in CSNU; uncertain significance
- 482 P → L: in CSNU; severe loss of amino acid transport activity; no effect on localization to the apical membrane; dbSNP:rs146815072; mutation P->A,G,S,V: No effect on amino acid transport activity.; mutation P->F,I,M,W: Decreased amino acid transport activity.
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
27% identity, 63% coverage: 6:345/537 of query aligns to 14:352/489 of P25737
- Y102 (≠ T93) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ F97) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K164) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F208) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (≠ T214) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E222) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ G264) 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 (≠ S267) 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.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 438 E→A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 443 D→A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 446 D→A: Retains 13% of wild-type lysine uptake activity. Is unable to inhibit CadC.
6li9B Heteromeric amino acid transporter b0,+at-rbat complex bound with arginine (see paper)
25% identity, 71% coverage: 17:397/537 of query aligns to 9:380/458 of 6li9B
7nf6B Ovine b0,+at-rbat heterodimer (see paper)
25% identity, 73% coverage: 8:397/537 of query aligns to 1:381/455 of 7nf6B
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)
24% identity, 73% coverage: 6:398/537 of query aligns to 37:423/535 of Q9UHI5
- I53 (= I22) binding
- Y93 (= Y60) 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 (≠ S99) 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 (≠ L119) modified: Interchain (with C-210 in SLC3A2)
- W174 (≠ F144) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (= F208) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ L211) 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 (≠ A266) to I: found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity
- N395 (≠ L370) binding ; mutation to Q: Strongly reduces L-leucine uptake activity. Strongly reduces L-tryptophan uptake activity.
- Y396 (≠ V371) mutation to A: Strongly reduces L-leucine uptake activity.
- T402 (≠ A377) to M: found in a patient with age-related hearing loss; strongly decreased L-alanine transport activity. Decreases L-tyrosine transport activity
- R418 (= R393) to C: found in a patient with age-related hearing loss; decreases L-alanine transport activity. Decreases L-tyrosine transport activity
Sites not aligning to the query:
- 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
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
23% identity, 73% coverage: 6:398/537 of query aligns to 9:397/469 of P46349
- G33 (≠ A30) mutation to D: Lack of activity.
- G42 (= G39) mutation to S: Lack of activity.
- G301 (≠ Y307) mutation to V: Lack of activity.
- G338 (vs. gap) mutation to E: Lack of activity.
- F341 (≠ W343) mutation to S: Lack of activity.
Sites not aligning to the query:
- 414 G→R: Lack of activity.
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)
24% identity, 73% coverage: 6:397/537 of query aligns to 36:421/531 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 (≠ S99) 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 (= F208) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
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)
25% identity, 71% coverage: 4:386/537 of query aligns to 10:386/457 of P15993
- Y103 (≠ F97) 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%.
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
24% identity, 71% coverage: 17:398/537 of query aligns to 8:383/458 of 7cmiB
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
24% identity, 71% coverage: 17:398/537 of query aligns to 8:383/458 of 7cmhB
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
24% identity, 71% coverage: 17:398/537 of query aligns to 8:383/457 of 7b00A
Sites not aligning to the query:
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
23% identity, 73% coverage: 6:397/537 of query aligns to 9:386/438 of O34739
- C94 (≠ M89) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ L139) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ V171) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (= C303) 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.
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
26% identity, 63% coverage: 7:342/537 of query aligns to 4:323/437 of 5j4nA
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
28% identity, 52% coverage: 7:284/537 of query aligns to 8:271/445 of P60061
- I23 (= I22) binding ; binding
- S26 (= S25) binding
- Y93 (≠ T93) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (= A96) binding ; binding
- C97 (≠ F97) binding
- N101 (≠ I101) 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 (≠ E104) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (≠ F208) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ A209) binding
- I205 (≠ L211) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
Sites not aligning to the query:
- 293 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.
- 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)
28% identity, 52% coverage: 7:284/537 of query aligns to 8:271/445 of P60063
- N22 (≠ A21) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (= I22) binding
- GSG 25:27 (= GSG 24:26) Helix-breaking GSG motif TM1
- S26 (= S25) binding ; mutation to K: 5% Agm antiport.
- G27 (= G26) binding
- Y74 (≠ V74) 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 (= Y87) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (≠ T93) 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 (= A96) binding
- C97 (≠ F97) binding
- N101 (≠ I101) binding
- W202 (≠ F208) Periplasmic (proximal) gate; binding
- I205 (≠ L211) binding
- GVESA 206:210 (≠ GLTPI 212:216) Helix-breaking GVESA motif TM6
- E208 (≠ T214) mutation E->A,D: 5-10% Agm antiport.
Sites not aligning to the query:
- 293 binding
- 337 F→A: Severely decreased antiport.
- 357 binding
- 365 Y→A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.
3l1lA Structure of arg-bound escherichia coli adic (see paper)
27% identity, 52% coverage: 7:284/537 of query aligns to 2:254/423 of 3l1lA
Sites not aligning to the query:
Query Sequence
>PP_1259 FitnessBrowser__Putida:PP_1259
MSGKFKKQLSLLDLTFIGLGAIFGSGWLFAASHVSAIAGPAGILSWFLGGFAVLLLGIVY
CELGAALPRAGGVVRYPVYSHGPLLGYLMGFITLIAFSSLIAIEVVASRQYAAAWFPGLT
KAGSSDPTVLGWLVQFALLGLFFFLNYRSVKTFAKANNLVSVFKFIVPLLVIGVLFTFFK
PENFEVQGFAPFGLSGVEMAVSAGGIIFAYLGLTPIISVASEVKNPQRTIPIALILSVLL
STAIYALLQLAFLGSVPTEMLANGWASVTKELALPYRDIALALGVGWLAYLVVADAVISP
SGCGNIYMNATPRVIYGWAQTGTFFKYFTRIDAESGIPRPALWLTFGLSVFWTLPFPSWE
ALINVVSAALVLSYAVAPVSVAALRRNAPHMPRPFRVKGMTVLGPLSFIIAALIVYWSGW
NTVSWLLALQIVMFVLYLLCSRFVPTQHLSLGQQVRSSAWLIGFYALTILLSWLGSFGGL
GVIGHPFDTVVVAACALGIYYWGAATGVPAHLVRLEGDDESEACAETSNGRPVAVAS
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