SitesBLAST
Comparing WP_047215491.1 NCBI__GCF_001931675.1:WP_047215491.1 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)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
26% identity, 73% coverage: 42:429/533 of query aligns to 51:421/456 of 5oqtA
Sites not aligning to the query:
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
26% identity, 73% coverage: 42:429/533 of query aligns to 53:423/458 of 6f34A
- binding arginine: E115 (≠ A104), Y116 (= Y105), A119 (≠ E112), F228 (= F217), A229 (≠ S218), I231 (≠ L220), V314 (≠ T313)
- binding cholesterol: W201 (= W191), Y202 (≠ D192)
- binding : A178 (≠ W171), R179 (vs. gap), A186 (≠ V176), I187 (≠ P177), A190 (≠ T180), L194 (= L184), Q296 (≠ L295), V299 (≠ M298)
Sites not aligning to the query:
Q88CZ8 L-histidine transporter HutT from Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) (see paper)
24% identity, 73% coverage: 13:401/533 of query aligns to 7:392/467 of Q88CZ8
- T27 (≠ S33) mutation T->A,S: Retains 60% of wild-type activity.; mutation to N: Retains 20% of wild-type activity.
- E98 (≠ A104) mutation to A: Retains 80% of wild-type activity.
- K156 (≠ P177) mutation K->A,Q: Retains less than 10% of wild-type activity.; mutation to R: Retains 40% of wild-type activity.
- F212 (= F217) mutation F->A,Q: Loss of activity.; mutation to Y: No change in activity.
- E218 (≠ R223) mutation E->A,Q: Loss of activity.; mutation to D: Retains 70% of wild-type activity.
8xyjA Structure of y+lat1 bound with lys
25% identity, 74% coverage: 12:407/533 of query aligns to 4:389/459 of 8xyjA
8xxiA Structure of y+lat1 bound with leu
25% identity, 74% coverage: 12:407/533 of query aligns to 4:389/465 of 8xxiA
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
23% identity, 80% coverage: 13:441/533 of query aligns to 1:418/433 of 6f2wA
9h76A Bacterial lat transporter basc in complex with l-ala and nb53 (see paper)
23% identity, 77% coverage: 29:441/533 of query aligns to 14:416/430 of 9h76A
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, 74% coverage: 13:407/533 of query aligns to 36:423/535 of Q9UHI5
- I53 (= I30) binding L-leucine
- Y93 (≠ F68) 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 (≠ V111) Important for substrate specificity; binding L-tryptophan; 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 (= C144) modified: Interchain (with C-210 in SLC3A2)
- W174 (≠ L153) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (= F217) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ L220) Important for substrate specificity; binding L-leucine; 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 (≠ L289) to I: found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity; dbSNP:rs142951280
- N395 (≠ T379) binding L-tryptophan; mutation to Q: Strongly reduces L-leucine uptake activity. Strongly reduces L-tryptophan uptake activity.
- Y396 (≠ V380) mutation to A: Strongly reduces L-leucine uptake activity.
- T402 (≠ G386) to M: found in a patient with age-related hearing loss; strongly decreased L-alanine transport activity. Decreases L-tyrosine transport activity; dbSNP:rs758342760
- R418 (= R402) to C: found in a patient with age-related hearing loss; decreases L-alanine transport activity. Decreases L-tyrosine transport activity; dbSNP:rs146946494
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; dbSNP:rs2048595742
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
25% identity, 71% coverage: 29:407/533 of query aligns to 12:383/458 of 7cmiB
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
25% identity, 71% coverage: 29:407/533 of query aligns to 12:383/458 of 7cmhB
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
25% identity, 71% coverage: 29:407/533 of query aligns to 12:383/457 of 7b00A
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)
24% identity, 74% coverage: 13:407/533 of query aligns to 35:422/531 of Q9QXW9
- Y130 (≠ I108) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (≠ V111) 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 (= F217) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
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)
22% identity, 74% coverage: 10:406/533 of query aligns to 23:409/487 of P82251
- V40 (≠ T27) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ IVGSG 30:34) binding L-arginine
- I44 (≠ V31) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (≠ G38) to F: in CSNU; uncertain significance
- P52 (vs. gap) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (≠ I55) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (≠ M84) to H: in CSNU; uncertain significance
- G105 (= G90) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W99) to R: in CSNU; uncertain significance
- I120 (≠ Y105) to L: in CSNU; uncertain significance
- T123 (≠ E112) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (≠ I128) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ S132) modified: Interchain (with C-114 in SLC3A1)
- V170 (= V159) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ W171) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (≠ L184) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ I215) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (≠ I216) 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 (≠ L220) binding L-arginine; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ F222) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ T224) mutation to A: Reduces amino acid transport activity.
- G259 (≠ S246) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ L248) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (≠ G273) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ M316) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ T319) to E: in CSNU; uncertain significance
- V330 (≠ A327) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ V328) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (≠ E330) 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 (≠ S350) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (≠ T376) mutation to A: Markedly reduces amino acid transport activity.
- A382 (≠ T379) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (≠ V380) mutation to A: Complete loss of amino acid transport activity.
- Y386 (= Y383) mutation to A: Loss of amino acid transport activity.
- K401 (≠ P398) 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.
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, 76% coverage: 13:415/533 of query aligns to 8:403/469 of P46349
- G33 (= G38) mutation to D: Lack of activity.
- G42 (= G47) mutation to S: Lack of activity.
- G301 (= G314) mutation to V: Lack of activity.
- G338 (vs. gap) mutation to E: Lack of activity.
- F341 (≠ M354) mutation to S: Lack of activity.
Sites not aligning to the query:
- 414 G→R: Lack of activity.
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
25% identity, 83% coverage: 15:457/533 of query aligns to 4:431/437 of 5j4nA
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
25% identity, 83% coverage: 15:457/533 of query aligns to 8:435/445 of P60061
- I23 (= I30) binding agmatine; binding L-arginine
- S26 (= S33) binding L-arginine
- Y93 (≠ L101) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (= A104) binding agmatine; binding L-arginine
- C97 (≠ Y105) binding agmatine
- N101 (≠ A113) 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 (≠ I116) binding agmatine; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (≠ F217) binding L-arginine; mutation to L: Halves Arg uptake into liposomes.
- S203 (= S218) binding agmatine
- I205 (≠ L220) binding agmatine; binding L-arginine; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (≠ S322) 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 (≠ T379) binding L-arginine; 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)
25% identity, 83% coverage: 15:457/533 of query aligns to 8:435/445 of P60063
- N22 (≠ S29) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (= I30) binding L-arginine
- GSG 25:27 (= GSG 32:34) Helix-breaking GSG motif TM1
- S26 (= S33) binding L-arginine; mutation to K: 5% Agm antiport.
- G27 (= G34) binding L-arginine
- Y74 (≠ V82) 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 (≠ R95) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (≠ L101) 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 (= A104) binding L-arginine
- C97 (≠ Y105) binding L-arginine
- N101 (≠ A113) binding L-arginine
- W202 (≠ F217) Periplasmic (proximal) gate; binding L-arginine
- I205 (≠ L220) binding L-arginine
- GVESA 206:210 (≠ GFRTA 221:225) Helix-breaking GVESA motif TM6
- E208 (≠ R223) mutation E->A,D: 5-10% Agm antiport.
- W293 (≠ S322) binding L-arginine
- F337 (= F361) mutation to A: Severely decreased antiport.
- S357 (≠ T379) binding L-arginine
- Y365 (= Y383) mutation to A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.
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)
22% identity, 69% coverage: 31:396/533 of query aligns to 29:387/457 of P15993
- Y103 (= Y105) 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%.
6li9B Heteromeric amino acid transporter b0,+at-rbat complex bound with arginine (see paper)
23% identity, 71% coverage: 29:406/533 of query aligns to 13:380/458 of 6li9B
3l1lA Structure of arg-bound escherichia coli adic (see paper)
26% identity, 83% coverage: 15:457/533 of query aligns to 2:418/423 of 3l1lA
Query Sequence
>WP_047215491.1 NCBI__GCF_001931675.1:WP_047215491.1
MANATGVSVTGKLRRDAGIIGLLFASTSSIVGSGWLFGAFHASKIAGPLSIWSWIIGAFI
IMLIALCFAELAALFPRSGALVHMSHASHGDGLGRIWSWMLFLAYVPIPAVEAEAIVTYA
NNYLPYFIQPGSQGLLTVAGFITCAALLGLMALLNLMTVRWLLNFNSTITWWKILVPAIT
IVALIGASTHWDVMHADPTGYKFSGVFTALPAAGIIFSYLGFRTAIDLGGESSNPNRNIP
LAVIGSVLLAAVLYVLLQIAFLKALAPADLARGWANLNFTGQMGPFAGLAATLGLGWMAT
LLYIDAYISPGGTGLMYMTGGSRVLFAVGELDAGPRWLAKLNNNQVPWASVILMWLVGVI
FLLPFPAWQQMVNYITSITVLTYGLGPVALLVMRRSLPNLKRPFHLKGAWLIAPFAFVCS
NWVIYWTGYKTNTFLFILITVGFILYALHYHLVARKPARDFGWRHIAWLLPWFGGLWVLS
LLGGIGGGKDLLGFGWEVVCVAVWSLIVLWLAVATALPKHETAEIMSRMEKTV
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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