SitesBLAST
Comparing N515DRAFT_1063 FitnessBrowser__Dyella79:N515DRAFT_1063 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)
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
37% identity, 97% coverage: 13:433/434 of query aligns to 11:435/437 of 5j4nA
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
37% identity, 97% coverage: 13:433/434 of query aligns to 15:439/445 of P60061
- I23 (≠ M21) binding ; binding
- S26 (= S24) binding
- Y93 (= Y91) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ C94) binding ; binding
- C97 (≠ V95) binding
- N101 (= N99) 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 (≠ I102) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (= W200) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ A201) binding
- I205 (≠ L203) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (= W291) 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 (= S355) 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)
37% identity, 97% coverage: 13:433/434 of query aligns to 15:439/445 of P60063
- N22 (= N20) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ M21) binding
- GSG 25:27 (= GSG 23:25) Helix-breaking GSG motif TM1
- S26 (= S24) binding ; mutation to K: 5% Agm antiport.
- G27 (= G25) binding
- Y74 (= Y72) 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 (≠ F85) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y91) 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 (≠ C94) binding
- C97 (≠ V95) binding
- N101 (= N99) binding
- W202 (= W200) Periplasmic (proximal) gate; binding
- I205 (≠ L203) binding
- GVESA 206:210 (≠ GLEAA 204:208) Helix-breaking GVESA motif TM6
- E208 (= E206) mutation E->A,D: 5-10% Agm antiport.
- W293 (= W291) binding
- F337 (≠ L335) mutation to A: Severely decreased antiport.
- S357 (= S355) binding
- Y365 (= Y363) mutation to A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.
3l1lA Structure of arg-bound escherichia coli adic (see paper)
36% identity, 97% coverage: 13:433/434 of query aligns to 9:422/423 of 3l1lA
P0AAF1 Putrescine transporter PotE; Putrescine-proton symporter / putrescine-ornithine antiporter from Escherichia coli (strain K12) (see 2 papers)
32% identity, 94% coverage: 5:414/434 of query aligns to 6:421/439 of P0AAF1
- C62 (≠ L61) mutation C->A,T: Strong decrease in both uptake and excretion activities.; mutation to S: Moderate decrease in both uptake and excretion activities.
- K68 (≠ N67) mutation to A: Slight decrease in both uptake and excretion activities.
- E77 (≠ R76) mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
- Y78 (≠ Q77) mutation to L: Uptake activity decreases more than excretion activity.
- K82 (≠ D81) mutation to A: Slight decrease in both uptake and excretion activities.
- Y90 (≠ W89) mutation to L: Uptake activity decreases more than excretion activity.
- Y92 (= Y91) mutation to L: Moderate decrease in both uptake and excretion activities.
- W201 (= W200) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- E207 (= E206) mutation E->A,D,N,Q: Lack of both uptake and excretion activities.
- C210 (≠ T209) mutation to A: Moderate decrease in both uptake and excretion activities.
- C285 (= C284) mutation to A: Moderate decrease in both uptake and excretion activities.
- C286 (≠ L285) mutation to A: Moderate decrease in both uptake and excretion activities.
- W292 (= W291) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- K301 (≠ Y300) mutation to A: Excretion activity decreases more than uptake activity.
- Y308 (≠ L307) 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.
P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
33% identity, 89% coverage: 3:387/434 of query aligns to 2:387/444 of P0AAE8
- C12 (≠ L13) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- W41 (≠ L42) mutation to L: Moderate decrease in cadaverine uptake.
- W43 (= W44) mutation to L: Strong decrease in cadaverine uptake.
- Y55 (≠ L56) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y57 (≠ H58) mutation to L: Strong decrease in cadaverine uptake.
- Y73 (= Y74) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake. 9-fold increase in Km for cadaverine for cadaverine uptake and 10-fold increase in Km for cadaverine for cadaverine excretion.
- E76 (≠ Q77) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y89 (= Y91) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake. 10-fold increase in Km for cadaverine for cadaverine uptake and 5-fold increase in Km for cadaverine for cadaverine excretion.
- Y90 (≠ W92) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
- Y107 (≠ S109) mutation to L: Strong decrease in cadaverine uptake.
- C125 (≠ A128) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- Y174 (= Y177) mutation to L: Moderate decrease in cadaverine uptake.
- D185 (≠ L187) mutation to N: Moderate decrease in cadaverine uptake.
- C196 (≠ T198) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E204 (= E206) mutation to Q: Strong decrease in both cadaverine excretion and cadaverine uptake. 22-fold increase in Km for cadaverine for cadaverine uptake and 6-fold increase in Km for cadaverine for cadaverine excretion.
- Y235 (≠ T237) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake. 23-fold increase in Km for cadaverine for cadaverine uptake and 7-fold increase in Km for cadaverine for cadaverine excretion.
- Y246 (≠ L248) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C282 (= C284) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- R299 (≠ A301) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
- D303 (= D305) mutation to N: Strong decrease in both cadaverine excretion and cadaverine uptake. 24-fold increase in Km for cadaverine for cadaverine uptake and 9-fold increase in Km for cadaverine for cadaverine excretion.
- Y310 (≠ F312) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y366 (= Y363) mutation to L: Strong decrease in cadaverine uptake. 15-fold increase in Km for cadaverine for cadaverine uptake.
- Y368 (≠ L365) mutation to L: Strong decrease in cadaverine uptake.
- C370 (≠ V367) mutation to S: Strong decrease in both cadaverine excretion and cadaverine uptake.
- E377 (≠ D374) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
Sites not aligning to the query:
- 389 C→S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- 394 C→S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- 397 C→S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- 408 E→Q: Moderate decrease in cadaverine uptake.
- 423 Y→L: Strong decrease in both cadaverine excretion and cadaverine uptake.
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
27% identity, 95% coverage: 16:426/434 of query aligns to 20:437/438 of O34739
- C94 (= C94) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (= C135) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ V163) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ A287) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
- C415 (≠ G407) mutation to 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)
25% identity, 94% coverage: 16:424/434 of query aligns to 12:430/433 of 6f2wA
7nf6B Ovine b0,+at-rbat heterodimer (see paper)
28% identity, 78% coverage: 14:350/434 of query aligns to 8:352/455 of 7nf6B
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, 87% coverage: 2:379/434 of query aligns to 24:409/487 of P82251
- V40 (= V18) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ MIGSG 21:25) binding
- I44 (= I22) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (≠ L29) to F: in CSNU; uncertain significance
- P52 (= P30) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (= A45) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y74) to H: in CSNU; uncertain significance
- G105 (= G80) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W89) to R: in CSNU; uncertain significance
- I120 (≠ V95) to L: in CSNU; uncertain significance
- T123 (= T97) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (≠ A116) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ N118) modified: Interchain (with C-114 in SLC3A1)
- V170 (= V143) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (= A155) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (= G168) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ A195) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (= A196) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (vs. gap) to D: in CSNU; decreased amino acid transport activity
- W230 (= W200) to R: in CSNU; complete loss of amino acid transport activity; mutation to A: Abolishes amino acid transport activity.
- D233 (≠ L203) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ L205) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ A207) mutation to A: Reduces amino acid transport activity.
- G259 (= G234) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ A236) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (≠ A261) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ V292) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ Q295) to E: in CSNU; uncertain significance
- V330 (≠ A301) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (= A302) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (≠ Q304) 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 (≠ G324) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (≠ T349) mutation to A: Markedly reduces amino acid transport activity.
- A382 (≠ I352) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (≠ L353) mutation to A: Complete loss of amino acid transport activity.
- Y386 (≠ T356) mutation to A: Loss of amino acid transport activity.
- K401 (≠ W371) 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.
6li9B Heteromeric amino acid transporter b0,+at-rbat complex bound with arginine (see paper)
25% identity, 84% coverage: 15:379/434 of query aligns to 8:380/458 of 6li9B
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
30% identity, 73% coverage: 6:322/434 of query aligns to 23:348/456 of 5oqtA
- binding alanine: I38 (≠ M21), G40 (= G23), T41 (≠ S24), G42 (= G25), F226 (≠ W200), A227 (= A201), I229 (≠ L203)
- binding : E24 (≠ L7), G26 (= G9), F28 (≠ W11), D29 (≠ M12), M32 (≠ A15), A176 (≠ G147), R177 (= R148), A184 (= A155), A188 (≠ I159), L192 (≠ V163), Q294 (≠ A272), V297 (≠ A275)
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
30% identity, 73% coverage: 6:322/434 of query aligns to 25:350/458 of 6f34A
- binding arginine: I40 (≠ M21), G42 (= G23), T43 (≠ S24), G44 (= G25), E115 (≠ C94), Y116 (≠ V95), A119 (= A98), F228 (≠ W200), A229 (= A201), I231 (≠ L203), V314 (vs. gap)
- binding cholesterol: W201 (≠ A170), Y202 (≠ L171)
- binding : G28 (= G9), F30 (≠ W11), D31 (≠ M12), M34 (≠ A15), A178 (≠ G147), R179 (= R148), A186 (= A155), I187 (≠ L156), A190 (≠ I159), L194 (≠ V163), Q296 (≠ A272), V299 (≠ A275)
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
25% identity, 76% coverage: 16:345/434 of query aligns to 8:348/457 of 7b00A
Sites not aligning to the query:
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
25% identity, 76% coverage: 16:345/434 of query aligns to 8:348/458 of 7cmiB
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
25% identity, 76% coverage: 16:345/434 of query aligns to 8:348/458 of 7cmhB
Sites not aligning to the query:
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)
25% identity, 76% coverage: 16:345/434 of query aligns to 48:388/535 of Q9UHI5
- I53 (≠ M21) binding
- Y93 (≠ H58) 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 (= N99) 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 (≠ A117) modified: Interchain (with C-210 in SLC3A2)
- W174 (≠ A137) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (vs. gap) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (vs. gap) 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 (≠ P259) 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
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, 76% coverage: 16:345/434 of query aligns to 47:387/531 of Q9QXW9
- Y130 (≠ W96) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (= N99) 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 (vs. gap) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
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, 97% coverage: 13:433/434 of query aligns to 17:458/469 of P46349
- G33 (≠ L29) mutation to D: Lack of activity.
- G42 (= G37) mutation to S: Lack of activity.
- G301 (≠ W291) mutation to V: Lack of activity.
- G338 (≠ S328) mutation to E: Lack of activity.
- F341 (≠ L331) mutation to S: Lack of activity.
- G414 (vs. gap) 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)
22% identity, 74% coverage: 18:339/434 of query aligns to 25:351/457 of P15993
- Y103 (≠ W96) 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%.
Query Sequence
>N515DRAFT_1063 FitnessBrowser__Dyella79:N515DRAFT_1063
MTSPARLLGPWMLTALVVGNMIGSGVFVLPAALAPYGAASLLGWAFTMGGALLLALVHAW
LAQLVANHGGAYAYARQAFGDTAGFVAAWSYWTCVWTANAAIAVAFAGSLGAIWPAANAT
PWRGTAAALAVLWLCTAINAAGVREAGRMQLVTTALKVIPLLVFGVCGLALVHGAAYQPF
NPSGQSLPSVTTATAALTLWAFLGLEAATVPTGVVRDPQRTVPRATVAGMLVAGVATMLA
CTAVIGLLPHGAAQGSAAPMAAAAAQTWGPAAGWAMGLVATVSCLGALNGWVLLQGQTPY
AAAQDGLFPAPFARTDARGTPWFGLLLSSVLASVLIAANGSKSLVALFTLSILLSTAATL
LPYVLSVLAWWRIDRGAGVARRTAAALALAYSLWALIGTGAEALLWGGVLLLLGLPVFLW
QRYRAAVKPAAPDL
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