SitesBLAST
Comparing BPHYT_RS27675 FitnessBrowser__BFirm:BPHYT_RS27675 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 15 hits to proteins with known functional sites (download)
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
30% identity, 85% coverage: 22:441/493 of query aligns to 2:413/445 of P60061
- I23 (≠ M41) binding ; binding
- S26 (= S44) binding
- Y93 (= Y114) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ S117) binding ; binding
- C97 (≠ A118) binding
- N101 (= N122) 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 (≠ Y125) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (= W227) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ V228) binding
- I205 (= I230) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (= W318) 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 (= S382) 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)
30% identity, 85% coverage: 22:441/493 of query aligns to 2:413/445 of P60063
- N22 (≠ S40) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ M41) binding
- GSG 25:27 (= GSG 43:45) Helix-breaking GSG motif TM1
- S26 (= S44) binding ; mutation to K: 5% Agm antiport.
- G27 (= G45) binding
- Y74 (= Y95) 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 (≠ F108) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y114) 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 (≠ S117) binding
- C97 (≠ A118) binding
- N101 (= N122) binding
- W202 (= W227) Periplasmic (proximal) gate; binding
- I205 (= I230) binding
- GVESA 206:210 (≠ GIEGA 231:235) Helix-breaking GVESA motif TM6
- E208 (= E233) mutation E->A,D: 5-10% Agm antiport.
- W293 (= W318) binding
- F337 (= F362) mutation to A: Severely decreased antiport.
- S357 (= S382) binding
- Y365 (= Y388) 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)
30% identity, 85% coverage: 25:441/493 of query aligns to 1:409/437 of 5j4nA
3l1lA Structure of arg-bound escherichia coli adic (see paper)
29% identity, 84% coverage: 29:441/493 of query aligns to 3:396/423 of 3l1lA
P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
28% identity, 76% coverage: 23:397/493 of query aligns to 2:375/444 of P0AAE8
- C12 (≠ L33) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- W41 (≠ V62) mutation to L: Moderate decrease in cadaverine uptake.
- W43 (≠ I64) mutation to L: Strong decrease in cadaverine uptake.
- Y55 (≠ F78) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y57 (= Y80) mutation to L: Strong decrease in cadaverine uptake.
- Y73 (= Y97) 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 (≠ A100) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y89 (= Y114) 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 (≠ W115) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
- Y107 (≠ T132) mutation to L: Strong decrease in cadaverine uptake.
- C125 (≠ A152) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- Y174 (≠ F201) mutation to L: Moderate decrease in cadaverine uptake.
- D185 (≠ N213) mutation to N: Moderate decrease in cadaverine uptake.
- C196 (≠ T225) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E204 (= E233) 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 (≠ L263) 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 (≠ V274) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C282 (≠ V311) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- R299 (≠ T328) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
- D303 (≠ G332) 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 (≠ L339) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y366 (= Y388) mutation to L: Strong decrease in cadaverine uptake. 15-fold increase in Km for cadaverine for cadaverine uptake.
- Y368 (≠ F390) mutation to L: Strong decrease in cadaverine uptake.
- C370 (≠ A392) 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.
P0AAF1 Putrescine transporter PotE; Putrescine-proton symporter / putrescine-ornithine antiporter from Escherichia coli (strain K12) (see 2 papers)
26% identity, 87% coverage: 25:454/493 of query aligns to 4:422/439 of P0AAF1
- C62 (vs. gap) mutation C->A,T: Strong decrease in both uptake and excretion activities.; mutation to S: Moderate decrease in both uptake and excretion activities.
- K68 (= K87) mutation to A: Slight decrease in both uptake and excretion activities.
- E77 (≠ A96) mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
- Y78 (= Y97) mutation to L: Uptake activity decreases more than excretion activity.
- K82 (≠ S101) mutation to A: Slight decrease in both uptake and excretion activities.
- Y90 (≠ W112) mutation to L: Uptake activity decreases more than excretion activity.
- Y92 (= Y114) mutation to L: Moderate decrease in both uptake and excretion activities.
- W201 (= W227) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- E207 (= E233) mutation E->A,D,N,Q: Lack of both uptake and excretion activities.
- C210 (≠ N236) mutation to A: Moderate decrease in both uptake and excretion activities.
- C285 (≠ V311) mutation to A: Moderate decrease in both uptake and excretion activities.
- C286 (≠ G312) mutation to A: Moderate decrease in both uptake and excretion activities.
- W292 (= W318) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- K301 (≠ F327) mutation to A: Excretion activity decreases more than uptake activity.
- Y308 (≠ V334) mutation to L: Excretion activity decreases more than uptake activity.
- W422 (= W454) mutation to L: Uptake activity decreases more than excretion activity.
Sites not aligning to the query:
- 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.
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
26% identity, 76% coverage: 29:403/493 of query aligns to 11:380/438 of O34739
- C94 (≠ S117) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ M159) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ V187) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ A314) 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, 86% coverage: 36:461/493 of query aligns to 12:433/433 of 6f2wA
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
24% identity, 80% coverage: 18:409/493 of query aligns to 3:409/489 of P25737
- Y102 (= Y114) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ A118) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (≠ T178) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (≠ W227) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E233) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (≠ R241) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ P285) 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 (= D292) 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)
32% identity, 17% coverage: 29:112/493 of query aligns to 38:123/531 of Q9QXW9
Sites not aligning to the query:
- 130 Y→A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- 133 N→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.
- 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, 17% coverage: 29:112/493 of query aligns to 39:124/535 of Q9UHI5
- I53 (≠ M41) binding
- Y93 (= Y80) 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.
Sites not aligning to the query:
- 134 Important for substrate specificity; binding ; N→Q: Reduces L-leucine uptake activity. Abolishes L-tryptophan uptake.; N→S: The substrate specificity changed dramatically reducing L-glutamine, glycine and L-alanine uptake activity thus mimicking the selectivity of SLC7A5.
- 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
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
33% identity, 17% coverage: 31:112/493 of query aligns to 1:84/457 of 7b00A
Sites not aligning to the query:
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
33% identity, 17% coverage: 31:112/493 of query aligns to 1:84/458 of 7cmiB
Sites not aligning to the query:
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
33% identity, 17% coverage: 31:112/493 of query aligns to 1:84/458 of 7cmhB
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)
24% identity, 67% coverage: 20:348/493 of query aligns to 3:338/511 of P63235
- M25 (≠ I42) mutation to A: 25% decrease in substrate transport.
- Y30 (≠ F47) mutation to A: At least 90% decrease in substrate transport.
- L212 (≠ I230) mutation to A: 70% decrease in substrate transport.
- E218 (≠ N236) mutation to A: At least 90% decrease in substrate transport.
- E304 (≠ A314) mutation to A: At least 90% decrease in substrate transport.
- W308 (= W318) mutation to A: At least 90% decrease in substrate transport.
Sites not aligning to the query:
- 378 Y→A: At least 90% decrease in substrate transport.
- 382 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.
Query Sequence
>BPHYT_RS27675 FitnessBrowser__BFirm:BPHYT_RS27675
MKNLADSLTGASVPRPAAQTAAQTAKPLRLGLLTALVIGSMIGSGVFSLPQNMASGAGAA
AVLIGWLITGVGMLTLAFVYQTLSTRKPELDNGIYAYARASAGDFVGFNSAWGYWVSAWI
GNVGYLVIVFGTLGYFFPVFGDGNTRAAVLGASIVLWIMHAVILRGVRSAAVLNAITTVA
KVIPLLVFILLALAAFRSHVFAQDFWGSSKLGNVFTQVKSTMLITVWVFIGIEGANVFSA
RAQRRQDIGRATLLGFTVVLLLLMAVSLLSLGIVPQSELAAMKNPSMAGVLDKAVGTWGA
VLISIGLLVSVGGALLAWTLLAAETLFTPASGGVMPTFLARQNSHGVPANALWLTNGLVQ
LFLIITLVSNATYQALISLATSMILIPYLFSAVYATRIAMRGDGYTITDTTRSRDTLIGA
MATVYCCWLLYAAGPKYLLLSALLYAPGVLLFGWAKRERGASLFKPFEVAILAALIALAA
LAAWLLSSGALGL
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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