SitesBLAST
Comparing BWI76_RS07190 FitnessBrowser__Koxy:BWI76_RS07190 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)
P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
91% identity, 100% coverage: 1:445/445 of query aligns to 1:444/444 of P0AAE8
- C12 (= C12) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- W41 (= W41) mutation to L: Moderate decrease in cadaverine uptake.
- W43 (= W43) mutation to L: Strong decrease in cadaverine uptake.
- Y55 (= Y55) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y57 (= Y57) mutation to L: Strong decrease in cadaverine uptake.
- Y73 (= Y73) 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 (= E76) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y89 (= Y89) 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 (= Y90) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
- Y107 (= Y107) mutation to L: Strong decrease in cadaverine uptake.
- C125 (= C125) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- Y174 (= Y174) mutation to L: Moderate decrease in cadaverine uptake.
- D185 (= D185) mutation to N: Moderate decrease in cadaverine uptake.
- C196 (= C196) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E204 (= E204) 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 (= Y235) 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 (= Y246) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C282 (= C282) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- R299 (= R299) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
- D303 (= D303) 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 (= Y310) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y366 (= Y366) mutation to L: Strong decrease in cadaverine uptake. 15-fold increase in Km for cadaverine for cadaverine uptake.
- Y368 (= Y368) mutation to L: Strong decrease in cadaverine uptake.
- C370 (= C370) mutation to S: Strong decrease in both cadaverine excretion and cadaverine uptake.
- E377 (= E377) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C389 (= C389) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C394 (= C394) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C397 (= C397) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E408 (= E408) mutation to Q: Moderate decrease in cadaverine uptake.
- Y423 (= Y423) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
39% identity, 98% coverage: 2:439/445 of query aligns to 5:440/445 of P60061
- I23 (≠ M20) binding ; binding
- S26 (= S23) binding
- Y93 (= Y89) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (= A92) binding ; binding
- C97 (≠ N93) binding
- N101 (= N97) 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 (≠ I100) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (= W198) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ A199) binding
- I205 (≠ V201) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (= W289) 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 (≠ A358) 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)
39% identity, 98% coverage: 2:439/445 of query aligns to 5:440/445 of P60063
- N22 (= N19) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ M20) binding
- GSG 25:27 (= GSG 22:24) Helix-breaking GSG motif TM1
- S26 (= S23) binding ; mutation to K: 5% Agm antiport.
- G27 (= G24) binding
- Y74 (≠ I71) 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 (≠ F83) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y89) 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 (= A92) binding
- C97 (≠ N93) binding
- N101 (= N97) binding
- W202 (= W198) Periplasmic (proximal) gate; binding
- I205 (≠ V201) binding
- GVESA 206:210 (= GVESA 202:206) Helix-breaking GVESA motif TM6
- E208 (= E204) mutation E->A,D: 5-10% Agm antiport.
- W293 (= W289) binding
- F337 (≠ L333) mutation to A: Severely decreased antiport.
- S357 (≠ A358) binding
- Y365 (= Y366) mutation to A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
39% identity, 98% coverage: 2:439/445 of query aligns to 1:436/437 of 5j4nA
3l1lA Structure of arg-bound escherichia coli adic (see paper)
38% identity, 98% coverage: 4:439/445 of query aligns to 1:423/423 of 3l1lA
P0AAF1 Putrescine transporter PotE; Putrescine-proton symporter / putrescine-ornithine antiporter from Escherichia coli (strain K12) (see 2 papers)
33% identity, 95% coverage: 1:424/445 of query aligns to 1:426/439 of P0AAF1
- C62 (≠ L60) mutation C->A,T: Strong decrease in both uptake and excretion activities.; mutation to S: Moderate decrease in both uptake and excretion activities.
- K68 (≠ Q66) mutation to A: Slight decrease in both uptake and excretion activities.
- E77 (≠ S78) mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
- Y78 (≠ P79) mutation to L: Uptake activity decreases more than excretion activity.
- K82 (vs. gap) mutation to A: Slight decrease in both uptake and excretion activities.
- Y90 (≠ V87) mutation to L: Uptake activity decreases more than excretion activity.
- Y92 (= Y89) mutation to L: Moderate decrease in both uptake and excretion activities.
- W201 (= W198) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- E207 (= E204) mutation E->A,D,N,Q: Lack of both uptake and excretion activities.
- C210 (≠ A207) mutation to A: Moderate decrease in both uptake and excretion activities.
- C285 (= C282) mutation to A: Moderate decrease in both uptake and excretion activities.
- C286 (≠ L283) mutation to A: Moderate decrease in both uptake and excretion activities.
- W292 (= W289) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- K301 (≠ V298) mutation to A: Excretion activity decreases more than uptake activity.
- Y308 (≠ N305) mutation to L: Excretion activity decreases more than uptake activity.
- W422 (≠ L420) mutation to L: Uptake activity decreases more than excretion activity.
- Y425 (= Y423) mutation to F: Moderate decrease in both uptake and excretion activities.; mutation to L: Strong decrease in both uptake and excretion activities.
Sites not aligning to the query:
- 433 mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
Q22397 Amino acid transporter protein 6 from Caenorhabditis elegans (see paper)
24% identity, 73% coverage: 2:325/445 of query aligns to 15:351/523 of Q22397
Sites not aligning to the query:
- 521:523 PDZ-binding motif; mutation Missing: Abolishes the interaction with nrfl-1.
P39277 L-methionine/branched-chain amino acid exporter YjeH from Escherichia coli (strain K12) (see paper)
25% identity, 63% coverage: 5:286/445 of query aligns to 6:283/418 of P39277
- T24 (≠ S23) mutation to Y: Strong decrease in methionine efflux.
- G25 (= G24) mutation to F: Strong decrease in methionine efflux.
- W195 (= W198) mutation to A: Strong decrease in methionine efflux.
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
22% identity, 69% coverage: 123:429/445 of query aligns to 155:454/456 of 5oqtA
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)
24% identity, 76% coverage: 5:344/445 of query aligns to 38:392/535 of Q9UHI5
- I53 (≠ M20) binding
- Y93 (= Y57) 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 (vs. gap) 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 (≠ L115) modified: Interchain (with C-210 in SLC3A2)
- W174 (≠ F134) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (≠ W198) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ V201) 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 (≠ P257) 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
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
28% identity, 59% coverage: 5:268/445 of query aligns to 10:273/438 of O34739
- C94 (≠ T85) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ T133) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ M160) 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.
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: 5:344/445 of query aligns to 37:391/531 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 (vs. gap) 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 (≠ W198) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
22% identity, 69% coverage: 123:429/445 of query aligns to 157:456/458 of 6f34A
- binding arginine: F228 (≠ W198), A229 (= A199), I231 (≠ V201), V314 (≠ L286)
- binding cholesterol: W201 (= W166), Y202 (≠ H167)
- binding : A178 (≠ S144), R179 (= R145), A186 (≠ V152), I187 (≠ L153), A190 (≠ I156), L194 (≠ M160), Q296 (≠ G267), V299 (≠ A270)
Sites not aligning to the query:
P63235 Glutamate/gamma-aminobutyrate antiporter; Glu/GABA antiporter; Extreme acid sensitivity protein from Escherichia coli (strain K12) (see 2 papers)
21% identity, 68% coverage: 66:367/445 of query aligns to 71:383/511 of P63235
- L212 (≠ W198) mutation to A: 70% decrease in substrate transport.
- E218 (= E204) mutation to A: At least 90% decrease in substrate transport.
- E304 (≠ S285) mutation to A: At least 90% decrease in substrate transport.
- W308 (= W289) mutation to A: At least 90% decrease in substrate transport.
- Y378 (≠ T362) mutation to A: At least 90% decrease in substrate transport.
- Y382 (= Y366) 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.
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
24% identity, 76% coverage: 8:344/445 of query aligns to 1:352/457 of 7b00A
Sites not aligning to the query:
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
24% identity, 76% coverage: 8:344/445 of query aligns to 1:352/458 of 7cmiB
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
24% identity, 76% coverage: 8:344/445 of query aligns to 1:352/458 of 7cmhB
Sites not aligning to the query:
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
25% identity, 61% coverage: 5:275/445 of query aligns to 2:276/433 of 6f2wA
Q9FFL1 Polyamine transporter RMV1; Protein RESISTANT TO METHYL VIOLOGEN 1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
23% identity, 65% coverage: 44:333/445 of query aligns to 91:378/490 of Q9FFL1
- I377 (≠ V332) mutation to F: Loss of sensitivity to paraquat.
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
21% identity, 45% coverage: 184:383/445 of query aligns to 206:399/458 of P24207
- E226 (= E204) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (≠ L230) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P319) 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:
- 26 mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- 54 P→A: 50% of wild-type phenylalanine transport activity.; P→G: No change in phenylalanine transport activity.; P→L: 26% of wild-type phenylalanine transport activity.
- 87 F→L: No effect on phenylalanine transport activity.
- 90 F→L: 65% of wild-type phenylalanine transport activity.
- 92 Y→L: 41% of wild-type phenylalanine transport activity.
- 94 Y→L: 69% of wild-type phenylalanine transport activity.
- 95 W→L: 10% of wild-type phenylalanine transport activity.
- 98 F→L: No effect on phenylalanine transport activity.
- 101 F→L: 38% of wild-type phenylalanine transport activity.
- 105 W→L: 39% of wild-type phenylalanine transport activity.
- 107 Y→L: No effect on phenylalanine transport activity.
- 108 W→L: 71% of wild-type phenylalanine transport activity.
- 111 F→L: 60% of wild-type phenylalanine transport activity.; F→Y: Enables the transport of tryptophan to almost the same steady-state level as that of phenylalanine.
- 118 mutation E->G,L,V,N: Loss of activity.
- 168 mutation K->L,R: Strong decrease in phenylalanine transport activity.; K→N: Loss of activity.
- 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.
Query Sequence
>BWI76_RS07190 FitnessBrowser__Koxy:BWI76_RS07190
MSSAKKIGLFACTGVVAGNMMGSGIALLPANLASIGSIAIWGWVISIIGAMSLAYVYARL
ATKNPQQGGPIAYAGEISPAFGFQTGVLYYHANWIGNLAIGITAVSYLSTFFPILNNPVP
AGIACIAIVWIFTFVNMLGGTWVSRLTTIGLVLVLIPVVMTAVVGWHWFDVATYQANWNT
SATTDSHAVVKSILLCLWAFVGVESAAVSTGMVKNPKRTVPLATMLGTALAGIVYIAATQ
VIAGMYPASEMAASGAPFAISASTILGGWAAPMVSAFTAFACLTSLGSWMMLVGQAGVRA
ANDGNFPKIYGELDKNGNPKKGLLLAAVKMTVLMVLITLMNSTGGKASDLFGELTGIAVL
LTMLPYFYSCVDLIRFEGINVRNFVSLICSVLGCGFCFIALMGASSFELAGTFIVSLIIL
MFYGRKMHQRQSNDGSADSSTASAH
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