SitesBLAST
Comparing Pf1N1B4_4214 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4214 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 17 hits to proteins with known functional sites (download)
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
28% identity, 87% coverage: 14:436/488 of query aligns to 1:413/445 of P60061
- I23 (≠ M34) binding ; binding
- S26 (≠ G37) binding
- Y93 (= Y107) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ S110) binding ; binding
- C97 (≠ A111) binding
- N101 (= N115) 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 (≠ Y118) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (= W222) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ V223) binding
- I205 (= I225) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (= W313) 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 (= S377) 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, 87% coverage: 14:436/488 of query aligns to 1:413/445 of P60063
- N22 (≠ S33) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ M34) binding
- GSG 25:27 (≠ GGG 36:38) Helix-breaking GSG motif TM1
- S26 (≠ G37) binding ; mutation to K: 5% Agm antiport.
- G27 (= G38) binding
- Y74 (= Y88) 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 (≠ F101) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y107) 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 (≠ S110) binding
- C97 (≠ A111) binding
- N101 (= N115) binding
- W202 (= W222) Periplasmic (proximal) gate; binding
- I205 (= I225) binding
- GVESA 206:210 (≠ GIEGA 226:230) Helix-breaking GVESA motif TM6
- E208 (= E228) mutation E->A,D: 5-10% Agm antiport.
- W293 (= W313) binding
- F337 (= F357) mutation to A: Severely decreased antiport.
- S357 (= S377) binding
- Y365 (= Y383) 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)
28% identity, 86% coverage: 16:436/488 of query aligns to 1:409/437 of 5j4nA
3l1lA Structure of arg-bound escherichia coli adic (see paper)
29% identity, 84% coverage: 29:436/488 of query aligns to 12:396/423 of 3l1lA
P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
26% identity, 76% coverage: 16:387/488 of query aligns to 2:370/444 of P0AAE8
- C12 (≠ L26) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- W41 (≠ I57) mutation to L: Moderate decrease in cadaverine uptake.
- W43 (= W59) mutation to L: Strong decrease in cadaverine uptake.
- Y55 (≠ F71) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y57 (≠ F73) mutation to L: Strong decrease in cadaverine uptake.
- Y73 (= Y90) 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 (≠ A93) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y89 (= Y107) 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 (≠ W108) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
- Y107 (≠ T125) mutation to L: Strong decrease in cadaverine uptake.
- C125 (≠ A145) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- Y174 (≠ F194) mutation to L: Moderate decrease in cadaverine uptake.
- D185 (= D205) mutation to N: Moderate decrease in cadaverine uptake.
- C196 (≠ T220) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E204 (= E228) 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 (≠ L256) 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 (≠ F264) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C282 (≠ L306) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- R299 (≠ A323) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
- D303 (= D327) 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 (≠ L334) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y366 (= Y383) mutation to L: Strong decrease in cadaverine uptake. 15-fold increase in Km for cadaverine for cadaverine uptake.
- Y368 (≠ W385) mutation to L: Strong decrease in cadaverine uptake.
- C370 (≠ A387) 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)
23% identity, 87% coverage: 16:439/488 of query aligns to 4:417/439 of P0AAF1
- C62 (≠ L76) mutation C->A,T: Strong decrease in both uptake and excretion activities.; mutation to S: Moderate decrease in both uptake and excretion activities.
- K68 (= K80) mutation to A: Slight decrease in both uptake and excretion activities.
- E77 (≠ K92) mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
- Y78 (≠ A93) mutation to L: Uptake activity decreases more than excretion activity.
- K82 (≠ D97) mutation to A: Slight decrease in both uptake and excretion activities.
- Y90 (≠ W105) mutation to L: Uptake activity decreases more than excretion activity.
- Y92 (= Y107) mutation to L: Moderate decrease in both uptake and excretion activities.
- W201 (= W222) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- E207 (= E228) mutation E->A,D,N,Q: Lack of both uptake and excretion activities.
- C210 (≠ S231) mutation to A: Moderate decrease in both uptake and excretion activities.
- C285 (≠ L306) mutation to A: Moderate decrease in both uptake and excretion activities.
- C286 (≠ V307) mutation to A: Moderate decrease in both uptake and excretion activities.
- W292 (= W313) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- K301 (≠ F322) mutation to A: Excretion activity decreases more than uptake activity.
- Y308 (≠ T329) 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.
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
24% identity, 78% coverage: 27:407/488 of query aligns to 18:381/438 of O34739
- C94 (≠ S110) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ L152) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ L180) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ A309) 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)
21% identity, 70% coverage: 27:369/488 of query aligns to 10:349/433 of 6f2wA
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
25% identity, 66% coverage: 46:365/488 of query aligns to 49:369/456 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)
25% identity, 66% coverage: 46:365/488 of query aligns to 51:371/458 of 6f34A
- binding arginine: E115 (vs. gap), Y116 (= Y107), A119 (≠ S110), F228 (≠ W222), A229 (≠ V223), I231 (= I225), V314 (≠ A309)
- binding cholesterol: W201 (≠ A188), Y202 (≠ F189)
- binding : A178 (= A164), R179 (≠ F165), A186 (≠ I172), I187 (≠ A173), A190 (≠ V176), L194 (= L180), Q296 (≠ G291), V299 (≠ G294)
Sites not aligning to the query:
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)
34% identity, 20% coverage: 29:125/488 of query aligns to 47:143/531 of Q9QXW9
- Y130 (≠ W112) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (= N115) 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.
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
34% identity, 20% coverage: 29:125/488 of query aligns to 8:104/458 of 7cmiB
Sites not aligning to the query:
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
34% identity, 20% coverage: 29:125/488 of query aligns to 8:104/458 of 7cmhB
Sites not aligning to the query:
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
34% identity, 20% coverage: 29:125/488 of query aligns to 8:104/457 of 7b00A
Sites not aligning to the query:
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
21% identity, 74% coverage: 10:372/488 of query aligns to 6:375/489 of P25737
- Y102 (= Y107) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ A111) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K174) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (≠ W222) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E228) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (≠ R236) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ P280) 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 (vs. gap) 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.
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)
34% identity, 20% coverage: 29:125/488 of query aligns to 48:144/535 of Q9UHI5
- I53 (≠ M34) binding
- Y93 (≠ F73) 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 (= N115) 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
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)
25% identity, 40% coverage: 3:198/488 of query aligns to 12:207/487 of P82251
- V40 (= V31) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ MVGGG 34:38) binding
- I44 (≠ V35) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (≠ L42) to F: in CSNU; uncertain significance
- P52 (= P43) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (≠ L60) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y90) to H: in CSNU; uncertain significance
- G105 (= G96) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W105) to R: in CSNU; uncertain significance
- I120 (= I113) to L: in CSNU; uncertain significance
- T123 (≠ V116) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (≠ E135) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ N137) modified: Interchain (with C-114 in SLC3A1)
- V170 (≠ I160) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ I172) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (= G186) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
Sites not aligning to the query:
- 223 L → M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- 224 A → V: in CSNU; non-classic type I; dbSNP:rs140873167
- 227 N → D: in CSNU; decreased amino acid transport activity
- 230 W → R: in CSNU; complete loss of amino acid transport activity; W→A: Abolishes amino acid transport activity.
- 233 binding ; D→A: Complete loss of amino acid transport activity.
- 235 W→A: Complete loss of amino acid transport activity.
- 237 Q→A: Reduces amino acid transport activity.
- 259 G → R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- 261 P → L: in CSNU; types I and III; dbSNP:rs121908486
- 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
>Pf1N1B4_4214 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4214
MVDSVSNIDKDTQISASSDKLKFGALIALVVGSMVGGGIFSLPQNIAKSASAGATLIGWL
ITGVGMLMLAFVFQTLANRKPKLDGGVYAYAKAGFGDYMGFSSAWGYWISAWIGNVSYMV
LLFSTLGFFFPMFGEGNTLPAIICASVLLWLLHFLVLRGIKEAAFINVITTIAKMVPLAL
FIVIAGVAFKMDVFTSDFWGAGNSDLGTVMNQVRNMMLVTVWVFIGIEGASIFSARAEKR
SDVGKATVVGFVGVLLLLVLVNVFSQGIMAQAQLAGLKNPSMAGVLEHVVGHWGAVLISA
GLIVSLVGALLSWTLLCAEILFASARDHTMPEFLRKENANQVPANALWLSNGLIQLFLII
TLFNSSTYLSLLYLATSMILVPYFWSAAYALLLAWRNETYEEAQGERTKDLVIGVIAVLY
AVWLVYAAGAQYLLLSALLYAPGAILFAKAKRELGQPVFTSIEKVIFVVVMIGALIAGYG
LYSGFLSL
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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