SitesBLAST
Comparing AZOBR_RS13260 FitnessBrowser__azobra:AZOBR_RS13260 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 17 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)
32% identity, 88% coverage: 6:425/480 of query aligns to 2:407/437 of 5j4nA
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
31% identity, 89% coverage: 1:425/480 of query aligns to 1:411/445 of P60061
- I23 (≠ M23) binding ; binding
- S26 (≠ G26) binding
- Y93 (= Y96) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ S99) binding ; binding
- C97 (≠ A100) binding
- N101 (= N104) 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 (≠ Y107) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (= W215) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ V216) binding
- I205 (= I218) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (= W306) 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 (≠ A371) 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)
31% identity, 89% coverage: 1:425/480 of query aligns to 1:411/445 of P60063
- N22 (≠ S22) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ M23) binding
- GSG 25:27 (≠ GGG 25:27) Helix-breaking GSG motif TM1
- S26 (≠ G26) binding ; mutation to K: 5% Agm antiport.
- G27 (= G27) binding
- Y74 (= Y77) 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 (≠ F90) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y96) 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 (≠ S99) binding
- C97 (≠ A100) binding
- N101 (= N104) binding
- W202 (= W215) Periplasmic (proximal) gate; binding
- I205 (= I218) binding
- GVESA 206:210 (≠ GIEGA 219:223) Helix-breaking GVESA motif TM6
- E208 (= E221) mutation E->A,D: 5-10% Agm antiport.
- W293 (= W306) binding
- F337 (= F350) mutation to A: Severely decreased antiport.
- S357 (≠ A371) binding
- Y365 (= Y376) 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)
31% identity, 87% coverage: 7:425/480 of query aligns to 1:394/423 of 3l1lA
P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
28% identity, 70% coverage: 5:340/480 of query aligns to 2:323/444 of P0AAE8
- C12 (≠ L15) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- W41 (≠ I46) mutation to L: Moderate decrease in cadaverine uptake.
- W43 (= W48) mutation to L: Strong decrease in cadaverine uptake.
- Y55 (≠ F60) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y57 (= Y62) mutation to L: Strong decrease in cadaverine uptake.
- Y73 (= Y79) 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 (≠ A82) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y89 (= Y96) 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 (≠ W97) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
- Y107 (≠ A114) mutation to L: Strong decrease in cadaverine uptake.
- C125 (= C137) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- Y174 (vs. gap) mutation to L: Moderate decrease in cadaverine uptake.
- D185 (≠ G197) mutation to N: Moderate decrease in cadaverine uptake.
- C196 (≠ T213) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E204 (= E221) 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 (= Y251) 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 (≠ L262) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C282 (≠ V299) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- R299 (≠ T316) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
- D303 (= D320) 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 (≠ F327) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
Sites not aligning to the query:
- 366 Y→L: Strong decrease in cadaverine uptake. 15-fold increase in Km for cadaverine for cadaverine uptake.
- 368 Y→L: Strong decrease in cadaverine uptake.
- 370 C→S: Strong decrease in both cadaverine excretion and cadaverine uptake.
- 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.
P0AAF1 Putrescine transporter PotE; Putrescine-proton symporter / putrescine-ornithine antiporter from Escherichia coli (strain K12) (see 2 papers)
26% identity, 92% coverage: 6:446/480 of query aligns to 5:439/439 of P0AAF1
- C62 (≠ L65) mutation C->A,T: Strong decrease in both uptake and excretion activities.; mutation to S: Moderate decrease in both uptake and excretion activities.
- K68 (= K69) mutation to A: Slight decrease in both uptake and excretion activities.
- E77 (≠ K81) mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
- Y78 (≠ A82) mutation to L: Uptake activity decreases more than excretion activity.
- K82 (≠ P86) mutation to A: Slight decrease in both uptake and excretion activities.
- Y90 (≠ W94) mutation to L: Uptake activity decreases more than excretion activity.
- Y92 (= Y96) mutation to L: Moderate decrease in both uptake and excretion activities.
- W201 (= W215) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- E207 (= E221) mutation E->A,D,N,Q: Lack of both uptake and excretion activities.
- C210 (≠ S224) mutation to A: Moderate decrease in both uptake and excretion activities.
- C285 (≠ V299) mutation to A: Moderate decrease in both uptake and excretion activities.
- C286 (≠ G300) mutation to A: Moderate decrease in both uptake and excretion activities.
- W292 (= W306) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- K301 (≠ Y315) mutation to A: Excretion activity decreases more than uptake activity.
- Y308 (≠ T322) mutation to L: Excretion activity decreases more than uptake activity.
- W422 (≠ I435) mutation to L: Uptake activity decreases more than excretion activity.
- Y425 (= Y438) mutation to F: Moderate decrease in both uptake and excretion activities.; mutation to L: Strong decrease in both uptake and excretion activities.
- E433 (≠ R440) 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, 67% coverage: 16:338/480 of query aligns to 10:325/433 of 6f2wA
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
23% identity, 69% coverage: 7:336/480 of query aligns to 9:323/438 of O34739
- C94 (≠ S92) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ I141) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ L169) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ A302) 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.
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, 84% coverage: 3:403/480 of query aligns to 10:401/457 of P15993
- Y103 (≠ A100) 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%.
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
23% identity, 75% coverage: 1:361/480 of query aligns to 2:371/489 of P25737
- Y102 (= Y96) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ A100) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K163) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (≠ I218) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (≠ S224) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (≠ R232) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ E266) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-278.
- D278 (= D269) Essential for the stimulus-dependent interaction with CadC; mutation to A: Retains 88% of wild-type lysine uptake activity, but can hardly inhibit CadC. Cannot interact with CadC; when associated with A-275.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 438 E→A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 443 D→A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 446 D→A: Retains 13% of wild-type lysine uptake activity. Is unable to inhibit CadC.
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)
33% identity, 24% coverage: 7:120/480 of query aligns to 36:151/531 of Q9QXW9
- Y130 (≠ F101) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (= N104) 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.
Sites not aligning to the query:
- 242 F→W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
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)
32% identity, 24% coverage: 7:120/480 of query aligns to 37:152/535 of Q9UHI5
- I53 (≠ M23) binding
- Y93 (= Y62) 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 (= N104) 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.
Sites not aligning to the query:
- 154 modified: Interchain (with C-210 in SLC3A2)
- 174 W→A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- 243 F→A: Abolishes leucine and tryptophan transport activities.
- 246 Important for substrate specificity; binding ; G→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.
- 302 V → I: found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity
- 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
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
35% identity, 21% coverage: 18:120/480 of query aligns to 8:112/458 of 7cmiB
Sites not aligning to the query:
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
35% identity, 21% coverage: 18:120/480 of query aligns to 8:112/458 of 7cmhB
Sites not aligning to the query:
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
35% identity, 21% coverage: 18:120/480 of query aligns to 8:112/457 of 7b00A
Sites not aligning to the query:
Q9FFL1 Polyamine transporter RMV1; Protein RESISTANT TO METHYL VIOLOGEN 1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
29% identity, 25% coverage: 5:125/480 of query aligns to 48:166/490 of Q9FFL1
Sites not aligning to the query:
- 377 I→F: Loss of sensitivity to paraquat.
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
22% identity, 94% coverage: 2:453/480 of query aligns to 4:434/469 of P46349
- G33 (≠ L31) mutation to D: Lack of activity.
- G42 (≠ S40) mutation to S: Lack of activity.
- G301 (≠ W306) mutation to V: Lack of activity.
- G338 (≠ T343) mutation to E: Lack of activity.
- F341 (≠ L346) mutation to S: Lack of activity.
- G414 (≠ A428) mutation to R: Lack of activity.
Query Sequence
>AZOBR_RS13260 FitnessBrowser__azobra:AZOBR_RS13260
VAQTRKSDKLTLLPLVALVVGSMIGGGVFNLPSDMSKGASPGAILIGWMITGIGMMMLAF
VYQNLAVRKPNLNAGPYAYAKAGFGPFVGFNSAWGYWLSAFLGNVAYAVAIFSALSHFFP
IFGDGNNLPSIVGASLCLWLIHALVLSGIKQAAFVNVVTSIAKLVPLFLFVLVAIVGFHW
DRFTVDFWGTGAGSGTGGLGSVMEQVKSTMLVTLWVFIGIEGASVYSARAARRSDVGRAT
VIGFVGALGIYVLVSLLATGVLRQPELADLKVPSMAGVFESLVGPWGAALINIGLVISVG
GAFLSWTLLCAEIPYTCGRDGTFPKWFAAENANGSPVNALWATNLLIQLFLALSFFSRSA
YQFFYFIASVAILPPYVLSGAYALKLALTGEGYGAESRTKGILVGALATAYGLWLVYAAG
LQYLLMCAVLFAPGILVYVRARREHGERTFTGVEMAIAAAIAVLAVLAAWLMWTGRISPL
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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