SitesBLAST
Comparing AO353_03465 FitnessBrowser__pseudo3_N2E3:AO353_03465 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 10 hits to proteins with known functional sites (download)
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
28% identity, 89% coverage: 1:423/475 of query aligns to 1:413/445 of P60061
- I23 (≠ M21) binding ; binding
- S26 (≠ G24) binding
- Y93 (= Y94) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ S97) binding ; binding
- C97 (≠ A98) binding
- N101 (= N102) 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 (≠ Y105) 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 (= S364) 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)
28% identity, 89% coverage: 1:423/475 of query aligns to 1:413/445 of P60063
- N22 (≠ S20) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ M21) binding
- GSG 25:27 (≠ GGG 23:25) Helix-breaking GSG motif TM1
- S26 (≠ G24) binding ; mutation to K: 5% Agm antiport.
- G27 (= G25) binding
- Y74 (= Y75) 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 (≠ F88) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y94) 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 (≠ S97) binding
- C97 (≠ A98) binding
- N101 (= N102) binding
- W202 (= W209) Periplasmic (proximal) gate; binding
- I205 (= I212) binding
- GVESA 206:210 (≠ GIEGA 213:217) Helix-breaking GVESA motif TM6
- E208 (= E215) mutation E->A,D: 5-10% Agm antiport.
- W293 (= W300) binding
- F337 (= F344) mutation to A: Severely decreased antiport.
- S357 (= S364) binding
- Y365 (= Y370) 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)
29% identity, 88% coverage: 7:423/475 of query aligns to 5:409/437 of 5j4nA
3l1lA Structure of arg-bound escherichia coli adic (see paper)
28% identity, 88% coverage: 7:423/475 of query aligns to 3:396/423 of 3l1lA
P0AAF1 Putrescine transporter PotE; Putrescine-proton symporter / putrescine-ornithine antiporter from Escherichia coli (strain K12) (see 2 papers)
25% identity, 90% coverage: 1:426/475 of query aligns to 1:417/439 of P0AAF1
- C62 (≠ L63) mutation C->A,T: Strong decrease in both uptake and excretion activities.; mutation to S: Moderate decrease in both uptake and excretion activities.
- K68 (= K67) mutation to A: Slight decrease in both uptake and excretion activities.
- E77 (≠ K79) mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
- Y78 (≠ A80) mutation to L: Uptake activity decreases more than excretion activity.
- K82 (≠ D84) mutation to A: Slight decrease in both uptake and excretion activities.
- Y90 (≠ W92) mutation to L: Uptake activity decreases more than excretion activity.
- Y92 (= Y94) 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 (≠ S218) mutation to A: Moderate decrease in both uptake and excretion activities.
- C285 (≠ L293) mutation to A: Moderate decrease in both uptake and excretion activities.
- C286 (≠ L294) 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 (≠ F309) mutation to A: Excretion activity decreases more than uptake activity.
- Y308 (≠ T316) 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)
27% identity, 78% coverage: 3:374/475 of query aligns to 2:370/444 of P0AAE8
- C12 (≠ L13) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- W41 (≠ I44) mutation to L: Moderate decrease in cadaverine uptake.
- W43 (= W46) mutation to L: Strong decrease in cadaverine uptake.
- Y55 (≠ F58) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y57 (≠ F60) mutation to L: Strong decrease in cadaverine uptake.
- Y73 (= Y77) 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 (≠ A80) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y89 (= Y94) 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 (≠ W95) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
- Y107 (≠ T112) mutation to L: Strong decrease in cadaverine uptake.
- C125 (≠ A132) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- Y174 (≠ F181) mutation to L: Moderate decrease in cadaverine uptake.
- D185 (≠ L193) 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 (≠ F244) 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 (≠ M256) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C282 (≠ L293) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- R299 (≠ A310) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
- D303 (= D314) 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 (≠ L321) 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 (≠ W372) mutation to L: Strong decrease in cadaverine uptake.
- C370 (≠ A374) mutation to S: Strong decrease in both cadaverine excretion and cadaverine uptake.
Sites not aligning to the query:
- 377 E→Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- 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)
25% identity, 82% coverage: 2:390/475 of query aligns to 3:383/438 of O34739
- C94 (≠ S90) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ W137) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ L167) 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.
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
24% identity, 70% coverage: 1:333/475 of query aligns to 1:326/433 of 6f2wA
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
24% identity, 66% coverage: 33:344/475 of query aligns to 49:361/456 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)
24% identity, 66% coverage: 33:344/475 of query aligns to 51:363/458 of 6f34A
- binding arginine: E115 (vs. gap), Y116 (= Y94), A119 (≠ S97), F228 (≠ W209), A229 (≠ V210), I231 (= I212), V314 (≠ A296)
- binding cholesterol: W201 (≠ F174), Y202 (≠ A175)
- binding : A178 (= A151), R179 (≠ F152), A186 (≠ V159), I187 (≠ A160), A190 (≠ V163), L194 (= L167), Q296 (≠ G278), V299 (≠ G281)
Sites not aligning to the query:
Query Sequence
>AO353_03465 FitnessBrowser__pseudo3_N2E3:AO353_03465
MSESSGKLRLGALVALVVGSMIGGGIFSLPQNMAASADVGAVLIGWVITAVGMLTLAFVF
QTLANRKPDLDGGVYAYAKAGFGDYMGFSSAWGYWISAWLGNVGYFVLLFSTLGYFFPLF
GEGNTPAAVIGASLLLWAVHFLVLRGIKEAAFINLVTTVAKVVPLVLFVLIAIFAFKLDI
FTADIWGLKNPDLGSVMNQVRNMMLVTVWVFIGIEGASIFSARAEKRSDVGKATVIGFIT
VLLFLMLVNVLSLGIMTQPALAKLQNPSMAAVLEHVVGHWGAVLISVGLVISLLGALLSW
VLLCAEIMFAAAKDHTMPEFLRKENSKQVPVNALWLTNAMVQIFLVITLFSASTYLSLIY
LATSMILVPYLWSAAYALLLAVRGESYENALAERKKDLVIGAIALIYAIWLLYAGGIKYL
LLSALLYAPGAILFAKAKRELGKAVFTNVEKLIFTAVVIGALVAAYGLYDGFLTL
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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