SitesBLAST
Comparing AO356_23935 FitnessBrowser__pseudo5_N2C3_1:AO356_23935 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 13 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)
28% identity, 84% coverage: 28:445/497 of query aligns to 2:409/437 of 5j4nA
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
28% identity, 85% coverage: 26:445/497 of query aligns to 4:413/445 of P60061
- I23 (≠ M45) binding ; binding
- S26 (= S48) binding
- Y93 (= Y118) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ S121) binding ; binding
- C97 (≠ A122) binding
- N101 (= N126) 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 (≠ Y129) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (= W231) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ V232) binding
- I205 (= I234) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (= W322) 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 (≠ A384) 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, 85% coverage: 26:445/497 of query aligns to 4:413/445 of P60063
- N22 (≠ S44) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ M45) binding
- GSG 25:27 (= GSG 47:49) Helix-breaking GSG motif TM1
- S26 (= S48) binding ; mutation to K: 5% Agm antiport.
- G27 (= G49) binding
- Y74 (≠ F99) 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 (≠ F112) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y118) 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 (≠ S121) binding
- C97 (≠ A122) binding
- N101 (= N126) binding
- W202 (= W231) Periplasmic (proximal) gate; binding
- I205 (= I234) binding
- GVESA 206:210 (≠ GIEGA 235:239) Helix-breaking GVESA motif TM6
- E208 (= E237) mutation E->A,D: 5-10% Agm antiport.
- W293 (= W322) binding
- F337 (= F366) mutation to A: Severely decreased antiport.
- S357 (≠ A384) binding
- Y365 (= Y392) 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)
27% identity, 84% coverage: 30:445/497 of query aligns to 2:396/423 of 3l1lA
P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
25% identity, 82% coverage: 30:436/497 of query aligns to 5:400/444 of P0AAE8
- C12 (≠ L37) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- W41 (≠ I66) mutation to L: Moderate decrease in cadaverine uptake.
- W43 (≠ I68) mutation to L: Strong decrease in cadaverine uptake.
- Y55 (≠ L82) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y57 (= Y84) mutation to L: Strong decrease in cadaverine uptake.
- Y73 (= Y101) 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 (≠ A104) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y89 (= Y118) 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 (≠ W119) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
- Y107 (≠ A136) mutation to L: Strong decrease in cadaverine uptake.
- C125 (≠ A156) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- Y174 (≠ F205) mutation to L: Moderate decrease in cadaverine uptake.
- D185 (≠ S217) mutation to N: Moderate decrease in cadaverine uptake.
- C196 (≠ T229) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E204 (= E237) 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 (≠ L267) 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 (≠ L278) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C282 (≠ V315) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- R299 (≠ T332) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
- D303 (≠ E336) 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 (≠ L343) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y366 (= Y392) mutation to L: Strong decrease in cadaverine uptake. 15-fold increase in Km for cadaverine for cadaverine uptake.
- Y368 (≠ F394) mutation to L: Strong decrease in cadaverine uptake.
- C370 (≠ G396) mutation to S: Strong decrease in both cadaverine excretion and cadaverine uptake.
- E377 (≠ R413) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C389 (≠ V425) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C394 (= C430) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C397 (≠ L433) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
Sites not aligning to the query:
- 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, 86% coverage: 24:448/497 of query aligns to 1:417/439 of P0AAF1
- C62 (≠ L87) mutation C->A,T: Strong decrease in both uptake and excretion activities.; mutation to S: Moderate decrease in both uptake and excretion activities.
- K68 (≠ Q91) mutation to A: Slight decrease in both uptake and excretion activities.
- E77 (≠ A100) mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
- Y78 (= Y101) mutation to L: Uptake activity decreases more than excretion activity.
- K82 (≠ L105) mutation to A: Slight decrease in both uptake and excretion activities.
- Y90 (≠ W116) mutation to L: Uptake activity decreases more than excretion activity.
- Y92 (= Y118) mutation to L: Moderate decrease in both uptake and excretion activities.
- W201 (= W231) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- E207 (= E237) mutation E->A,D,N,Q: Lack of both uptake and excretion activities.
- C210 (vs. gap) mutation to A: Moderate decrease in both uptake and excretion activities.
- C285 (≠ V315) mutation to A: Moderate decrease in both uptake and excretion activities.
- C286 (≠ G316) mutation to A: Moderate decrease in both uptake and excretion activities.
- W292 (= W322) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- K301 (≠ F331) mutation to A: Excretion activity decreases more than uptake activity.
- Y308 (≠ V338) 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)
25% identity, 77% coverage: 30:410/497 of query aligns to 10:383/438 of O34739
- C94 (≠ S121) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ H164) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ L191) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ A318) 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)
25% identity, 61% coverage: 38:340/497 of query aligns to 10:308/433 of 6f2wA
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)
27% identity, 37% coverage: 30:213/497 of query aligns to 37:218/531 of Q9QXW9
- Y130 (≠ W123) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (= N126) 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)
26% identity, 43% coverage: 2:213/497 of query aligns to 5:219/535 of Q9UHI5
- I53 (≠ M45) binding
- Y93 (= Y84) 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 (= N126) 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.
- C154 (≠ F144) modified: Interchain (with C-210 in SLC3A2)
- W174 (= W165) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
Sites not aligning to the query:
- 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)
24% identity, 72% coverage: 40:397/497 of query aligns to 8:361/458 of 7cmiB
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
24% identity, 72% coverage: 40:397/497 of query aligns to 8:361/458 of 7cmhB
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
36% identity, 15% coverage: 40:116/497 of query aligns to 8:84/457 of 7b00A
Sites not aligning to the query:
Query Sequence
>AO356_23935 FitnessBrowser__pseudo5_N2C3_1:AO356_23935
MATHLQGTEPVIPTVTPHPLAGSLRKVEPRRLSLSLLIALVVGSMIGSGIFSLPQNMAAS
AGAGAILIGWLITGVGMLSLALVYQTLSNRQPELDNGVFAYARALGGEFLGFNSAWGYWI
SAWIGNVSYLVILFAALSYFFPLFGEGNNKAAIIGASVVLWALHWMILRGMRTAAKANAL
TTIAKVVPLLLFIGLVIAAFSKDTFMVDFWGTPALGSTLDQVKSTMLVTVWVFIGIEGAN
VFSARAAERADVGRATVMGFILTLLLLIAVSLLSLGILRQPELAALKNPSMAGVLEAVTG
PWGAVLISIGLIVSVGGALLAWTLLAAESVFTPAKEKVMPRLLATENQHGAPANALWITN
GCIQLFLLLTLYSSASYLALISLATSMILLPYLFSGLYALKMTWQGQTYAGHRGLQLRDM
AIAVVATGYCVWLLYAAGPRYMLLSALLYAPGSLIYLSAQRARTGRALTGFGWGLLIVIW
VAAIFAGWMLWAGQLSL
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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