SitesBLAST
Comparing SMa1667 FitnessBrowser__Smeli:SMa1667 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 9 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)
26% identity, 93% coverage: 3:444/475 of query aligns to 1:431/437 of 5j4nA
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
26% identity, 93% coverage: 3:444/475 of query aligns to 5:435/445 of P60061
- I23 (≠ M21) binding ; binding
- S26 (≠ A24) binding
- Y93 (= Y94) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ V97) binding ; binding
- C97 (≠ G98) binding
- N101 (≠ D102) 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 (≠ F209) 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 (≠ T362) 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)
26% identity, 93% coverage: 3:444/475 of query aligns to 5:435/445 of P60063
- N22 (≠ S20) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ M21) binding
- GSG 25:27 (≠ GAG 23:25) Helix-breaking GSG motif TM1
- S26 (≠ A24) 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 (≠ V97) binding
- C97 (≠ G98) binding
- N101 (≠ D102) binding
- W202 (≠ F209) 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 (= F344) mutation to A: Severely decreased antiport.
- S357 (≠ T362) binding
- Y365 (= Y370) 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)
26% identity, 93% coverage: 5:444/475 of query aligns to 1:418/423 of 3l1lA
P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
25% identity, 94% coverage: 3:447/475 of query aligns to 2:434/444 of P0AAE8
- C12 (≠ L13) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- W41 (≠ A42) mutation to L: Moderate decrease in cadaverine uptake.
- W43 (≠ V44) mutation to L: Strong decrease in cadaverine uptake.
- Y55 (≠ H58) 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 (vs. gap) 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 (≠ S132) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- Y174 (≠ F181) mutation to L: Moderate decrease in cadaverine uptake.
- D185 (≠ E193) 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 (≠ M245) 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 (≠ L256) 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 (≠ C310) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
- D303 (≠ N314) 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 (= Y376) mutation to L: Strong decrease in cadaverine uptake.
- C370 (≠ F378) mutation to S: Strong decrease in both cadaverine excretion and cadaverine uptake.
- E377 (= E385) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C389 (≠ L400) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C394 (≠ T405) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C397 (≠ A409) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E408 (≠ L420) mutation to Q: Moderate decrease in cadaverine uptake.
- Y423 (= Y436) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
P0AAF1 Putrescine transporter PotE; Putrescine-proton symporter / putrescine-ornithine antiporter from Escherichia coli (strain K12) (see 2 papers)
23% identity, 91% coverage: 3:434/475 of query aligns to 4:425/439 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 (≠ N79) 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 (≠ L92) mutation to L: Uptake activity decreases more than excretion activity.
- Y92 (= Y94) mutation to L: Moderate decrease in both uptake and excretion activities.
- W201 (≠ F209) 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 (≠ V293) 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 (≠ D316) mutation to L: Excretion activity decreases more than uptake activity.
- W422 (≠ T431) mutation to L: Uptake activity decreases more than excretion activity.
- Y425 (≠ F434) 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.
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
24% identity, 67% coverage: 16:331/475 of query aligns to 20:324/438 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 (≠ H140) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ I167) 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)
22% identity, 75% coverage: 6:361/475 of query aligns to 2:349/433 of 6f2wA
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
21% identity, 81% coverage: 6:388/475 of query aligns to 10:390/469 of P46349
- G33 (≠ L29) mutation to D: Lack of activity.
- G42 (= G38) mutation to S: Lack of activity.
- G301 (≠ W300) mutation to V: Lack of activity.
- G338 (≠ S337) mutation to E: Lack of activity.
- F341 (≠ V340) mutation to S: Lack of activity.
Sites not aligning to the query:
- 414 G→R: Lack of activity.
Query Sequence
>SMa1667 FitnessBrowser__Smeli:SMa1667
MTSTAQKLSLASLAALVVGSMVGAGIFSLPRTFGDATGPFGAIVAWCIAGAGIFTLAHVF
RVLAERKSDLDAGVYAYANAGFGDYAGFLSVLGYWLVGCIADVSYWVLIKATLGAFFPIF
GDGNTIAAVLVSSVALWGFHFMILRGIKEAAAINTVVTVAKIVPILIFIVILLGAFETDL
FRSNFWGGADMPEASLFEQIRATMLVTVFVFIGVEGASVYSRYARKRSDVGVATTLGFVV
VLGLMVLVTLLPYGALERPEIAAMRQPSMASVLESIVGPWGSVFVSAGLIVSVLGAYLAW
SLICVEVLFCAAKNGDMPSVLARENSNSVPAAALWLSNGVIQLFLISTLFSEDAFRLMVN
LTSAMVLIPYLLVAAYGFLVAKRGETYNIRPKERFRDLILAGAATVYTAFMIYAGGLKFL
LLSAILYALGTALFFYARREQKKPLFSPREWLVFIAVVAGCLVGIYGLVTGSITI
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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