SitesBLAST
Comparing GFF272 FitnessBrowser__psRCH2:GFF272 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
30% identity, 89% coverage: 3:423/475 of query aligns to 1:409/437 of 5j4nA
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
30% identity, 89% coverage: 3:423/475 of query aligns to 5:413/445 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)
30% identity, 89% coverage: 3:423/475 of query aligns to 5:413/445 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.
3l1lA Structure of arg-bound escherichia coli adic (see paper)
30% identity, 86% coverage: 16:423/475 of query aligns to 12:396/423 of 3l1lA
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 (≠ L247) 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.
P0AAF1 Putrescine transporter PotE; Putrescine-proton symporter / putrescine-ornithine antiporter from Escherichia coli (strain K12) (see 2 papers)
25% identity, 93% coverage: 3:446/475 of query aligns to 4:432/439 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 (≠ A294) 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.
- W422 (≠ K436) mutation to L: Uptake activity decreases more than excretion activity.
- Y425 (≠ H439) 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.
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
24% identity, 72% coverage: 15:356/475 of query aligns to 11:349/433 of 6f2wA
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
26% identity, 83% coverage: 4:395/475 of query aligns to 6:382/438 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 (≠ 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.
P82251 b(0,+)-type amino acid transporter 1; b(0,+)AT1; Glycoprotein-associated amino acid transporter b0,+AT1; Solute carrier family 7 member 9 from Homo sapiens (Human) (see 11 papers)
23% identity, 54% coverage: 5:261/475 of query aligns to 27:283/487 of P82251
- V40 (= V18) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ MIGGG 21:25) binding
- I44 (= I22) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (≠ L29) to F: in CSNU; uncertain significance
- P52 (= P30) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (= A47) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y77) to H: in CSNU; uncertain significance
- G105 (= G83) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W92) to R: in CSNU; uncertain significance
- I120 (= I100) to L: in CSNU; uncertain significance
- T123 (≠ V103) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (≠ E122) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ N124) modified: Interchain (with C-114 in SLC3A1)
- V170 (≠ I147) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ I159) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (≠ A173) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ Q198) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (≠ Q199) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (= N202) to D: in CSNU; decreased amino acid transport activity
- W230 (= W209) to R: in CSNU; complete loss of amino acid transport activity; mutation to A: Abolishes amino acid transport activity.
- D233 (≠ I212) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ I214) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ G216) mutation to A: Reduces amino acid transport activity.
- G259 (= G237) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ C239) to L: in CSNU; types I and III; dbSNP:rs121908486
Sites not aligning to the query:
- 286 S → F: in CSNU; uncertain significance; dbSNP:rs755135545
- 321 C→S: Does not affect amino acid transport activity.
- 324 A → E: in CSNU; uncertain significance
- 330 V → M: in CSNU; type III; dbSNP:rs201618022
- 331 A → V: in CSNU; non-classic type I; dbSNP:rs768466784
- 333 R → Q: in CSNU; decreased amino acid transport activity; dbSNP:rs769576205; R → W: in CSNU; severe loss of amino acid transport activity; dbSNP:rs121908484
- 354 A → T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- 379 S→A: Markedly reduces amino acid transport activity.
- 382 A → T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- 383 W→A: Complete loss of amino acid transport activity.
- 386 Y→A: Loss of amino acid transport activity.
- 401 K → E: in CSNU; uncertain significance; dbSNP:rs760264924
- 426 L → P: in CSNU; uncertain significance
- 482 P → L: in CSNU; severe loss of amino acid transport activity; no effect on localization to the apical membrane; dbSNP:rs146815072; mutation P->A,G,S,V: No effect on amino acid transport activity.; mutation P->F,I,M,W: Decreased amino acid transport activity.
Query Sequence
>GFF272 FitnessBrowser__psRCH2:GFF272
MAANSKQLKLGALVALVVGSMIGGGIFSLPQNMAASASAGGILIGWAITAVGMLTLAFVF
QSLANRKPELDAGVYAYAKAGFGDYMGFSSAWGYWISAWIGNVSYFVLLFSTLGYFVPMF
GEGNTLPAVIGASLVLWGVHFLVLRGIREAAFINLVTTIAKIVPLILFIVITAVAFRLEV
FTADFWGRGNIELGGVMQQVRNMMLVTVWVFIGIEGASIFSARAERRSDVGRATVIGFCS
VLALLVLVNVLSMGIMSQAELAGLKNPSMAGVLEQVVGRWGAVLISVGLVVSLAGALLSW
TLLCAEILFAAARDHTMPQFLRKENAKHVPVNALWLSNGLIQLFLIITLFNASTYLSLLY
LATSMILVPYFWSAAYGLLLGLRGEGYEGAPRERRKDLLNAAIATLYAMWLVYAGGMQYV
LLSALLYAPGVLFFAKAKHELGQPVFTAIERLIFAAVLIGAAIAAYGLYDGFLSL
Or try a new SitesBLAST search
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