SitesBLAST
Comparing BWI76_RS16225 FitnessBrowser__Koxy:BWI76_RS16225 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 11 hits to proteins with known functional sites (download)
3l1lA Structure of arg-bound escherichia coli adic (see paper)
29% identity, 95% coverage: 3:437/460 of query aligns to 2:422/423 of 3l1lA
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
29% identity, 95% coverage: 3:437/460 of query aligns to 4:435/437 of 5j4nA
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
29% identity, 95% coverage: 3:437/460 of query aligns to 8:439/445 of P60061
- I23 (≠ M18) binding ; binding
- S26 (≠ A21) binding
- Y93 (= Y91) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ C94) binding ; binding
- C97 (≠ A95) 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 (≠ Y102) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (= W209) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ V210) binding
- I205 (= I212) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (= W300) 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 (≠ A362) 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)
29% identity, 95% coverage: 3:437/460 of query aligns to 8:439/445 of P60063
- N22 (≠ S17) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ M18) binding
- GSG 25:27 (≠ GAG 20:22) Helix-breaking GSG motif TM1
- S26 (≠ A21) binding ; mutation to K: 5% Agm antiport.
- G27 (= G22) binding
- Y74 (≠ F72) 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 (≠ A95) binding
- N101 (= N99) binding
- W202 (= W209) Periplasmic (proximal) gate; binding
- I205 (= I212) binding
- GVESA 206:210 (≠ GVEGA 213:217) Helix-breaking GVESA motif TM6
- E208 (= E215) mutation E->A,D: 5-10% Agm antiport.
- W293 (= W300) binding
- F337 (vs. gap) mutation to A: Severely decreased antiport.
- S357 (≠ A362) binding
- Y365 (= Y370) mutation to A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.
P0AAF1 Putrescine transporter PotE; Putrescine-proton symporter / putrescine-ornithine antiporter from Escherichia coli (strain K12) (see 2 papers)
28% identity, 90% coverage: 2:415/460 of query aligns to 6:417/439 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 (≠ D66) 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 (≠ E77) mutation to L: Uptake activity decreases more than excretion activity.
- K82 (≠ E81) 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 (= W209) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- E207 (= E215) mutation E->A,D,N,Q: Lack of both uptake and excretion activities.
- C210 (≠ V218) mutation to A: Moderate decrease in both uptake and excretion activities.
- C285 (≠ V293) mutation to A: Moderate decrease in both uptake and excretion activities.
- C286 (= C294) mutation to A: Moderate decrease in both uptake and excretion activities.
- W292 (= W300) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- K301 (≠ Y309) mutation to A: Excretion activity decreases more than uptake activity.
- Y308 (≠ A316) 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.
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
23% identity, 93% coverage: 1:430/460 of query aligns to 1:431/433 of 6f2wA
P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
23% identity, 94% coverage: 3:434/460 of query aligns to 5:432/444 of P0AAE8
- C12 (≠ L10) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- W41 (≠ L39) mutation to L: Moderate decrease in cadaverine uptake.
- W43 (≠ I41) mutation to L: Strong decrease in cadaverine uptake.
- Y55 (≠ F55) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y57 (≠ M57) 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 (= E77) 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 (≠ A109) mutation to L: Strong decrease in cadaverine uptake.
- C125 (≠ A134) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- Y174 (≠ F183) mutation to L: Moderate decrease in cadaverine uptake.
- D185 (≠ V196) mutation to N: Moderate decrease in cadaverine uptake.
- C196 (≠ T207) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E204 (= E215) 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 (= Y245) 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 (≠ V256) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C282 (≠ V293) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- R299 (≠ L310) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
- D303 (≠ H314) 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 (≠ F321) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y366 (= Y370) mutation to L: Strong decrease in cadaverine uptake. 15-fold increase in Km for cadaverine for cadaverine uptake.
- Y368 (≠ L372) mutation to L: Strong decrease in cadaverine uptake.
- C370 (≠ G374) mutation to S: Strong decrease in both cadaverine excretion and cadaverine uptake.
- E377 (≠ A381) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C389 (≠ V389) 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 (≠ G397) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E408 (≠ H408) mutation to Q: Moderate decrease in cadaverine uptake.
- Y423 (= Y425) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
24% identity, 83% coverage: 1:383/460 of query aligns to 8:375/438 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 (≠ V141) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ A169) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ A296) 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.
P63235 Glutamate/gamma-aminobutyrate antiporter; Glu/GABA antiporter; Extreme acid sensitivity protein from Escherichia coli (strain K12) (see 2 papers)
26% identity, 70% coverage: 68:391/460 of query aligns to 72:405/511 of P63235
- L212 (vs. gap) mutation to A: 70% decrease in substrate transport.
- E218 (= E215) mutation to A: At least 90% decrease in substrate transport.
- E304 (≠ A296) mutation to A: At least 90% decrease in substrate transport.
- W308 (= W300) mutation to A: At least 90% decrease in substrate transport.
- Y378 (vs. gap) mutation to A: At least 90% decrease in substrate transport.
- Y382 (= Y370) 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.
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
24% identity, 74% coverage: 1:341/460 of query aligns to 21:358/456 of 5oqtA
- binding alanine: I38 (≠ M18), G40 (= G20), T41 (≠ A21), G42 (= G22), F226 (≠ W209), A227 (≠ V210), I229 (= I212)
- binding : E24 (≠ K4), G26 (= G6), F28 (≠ S8), D29 (≠ A9), M32 (≠ A12), A176 (= A153), R177 (≠ G154), A184 (≠ L161), A188 (≠ L165), L192 (≠ A169), Q294 (≠ G278), V297 (≠ G281)
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
24% identity, 74% coverage: 1:341/460 of query aligns to 23:360/458 of 6f34A
- binding arginine: I40 (≠ M18), G42 (= G20), T43 (≠ A21), G44 (= G22), E115 (≠ C94), Y116 (≠ A95), A119 (= A98), F228 (≠ W209), A229 (≠ V210), I231 (= I212), V314 (≠ A296)
- binding cholesterol: W201 (≠ M176), Y202 (≠ A177)
- binding : G28 (= G6), F30 (≠ S8), D31 (≠ A9), M34 (≠ A12), A178 (= A153), R179 (≠ G154), A186 (≠ L161), I187 (≠ A162), A190 (≠ L165), L194 (≠ A169), Q296 (≠ G278), V299 (≠ G281)
Query Sequence
>BWI76_RS16225 FitnessBrowser__Koxy:BWI76_RS16225
MEKKLGLSALTALVLSSMLGAGVFSLPQNMAAVASPSALLIGWGITGVGILFLAFAMLLL
TRIRPDLDGGIFTYAREGFGELIGFCSAWGYWLCAVVANVSYLVIVFSALSFFTDTPELR
LFGDGNTWQSIIGASVLLWIVHFLVLRGVQTAAGINLAATLAKLLPLGAFIALAAMAFRM
ETFRLDFSGLALGVPVWEQVKNTMLITLWVFIGVEGAVVVSARARNKQDVGRATLLAVLS
ALAVYLLVTLLSLGVVPRSELAEIRNPSMAGLMVNMMGSWGEIVIAAGLIISVCGAYLSW
TIMAAEVPYLAATHKAFPRLFARTNKNNAPSSSLWLTNISVQASLVLIWLTGSDYSTLLT
IASEMILVPYFLVGAFLLKIARRPLHKAVGVGACIYGLWLLYASGPVHLLLSVILYAPGL
LVFLYARRTHQHDRPLKRRDLALIGFLLVAAVPATWMLVG
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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