SitesBLAST
Comparing N515DRAFT_0722 FitnessBrowser__Dyella79:N515DRAFT_0722 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 20 (the maximum) hits to proteins with known functional sites (download)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
49% identity, 97% coverage: 7:473/479 of query aligns to 1:453/456 of 5oqtA
- binding alanine: I38 (≠ V40), G40 (= G42), T41 (≠ A43), G42 (= G44), F226 (≠ Y245), A227 (= A246), I229 (= I248)
- binding : E24 (≠ T26), G26 (= G28), F28 (≠ K30), D29 (≠ E31), M32 (≠ V34), A176 (≠ T188), R177 (≠ M189), A184 (= A196), A188 (≠ I200), L192 (= L204), Q294 (≠ L314), V297 (≠ L317)
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
49% identity, 98% coverage: 6:473/479 of query aligns to 2:455/458 of 6f34A
- binding arginine: I40 (≠ V40), G42 (= G42), T43 (≠ A43), G44 (= G44), E115 (= E115), Y116 (= Y116), A119 (= A119), F228 (≠ Y245), A229 (= A246), I231 (= I248), V314 (= V332)
- binding cholesterol: W201 (≠ Q211), Y202 (= Y212)
- binding : G28 (= G28), F30 (≠ K30), D31 (≠ E31), M34 (≠ V34), A178 (≠ T188), R179 (≠ M189), A186 (= A196), I187 (≠ L197), A190 (≠ I200), L194 (= L204), Q296 (≠ L314), V299 (≠ L317)
P30825 High affinity cationic amino acid transporter 1; CAT-1; CAT1; Ecotropic retroviral leukemia receptor homolog; Ecotropic retrovirus receptor homolog; Solute carrier family 7 member 1; System Y+ basic amino acid transporter from Homo sapiens (Human) (see paper)
36% identity, 87% coverage: 5:419/479 of query aligns to 11:439/629 of P30825
- N226 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
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)
22% identity, 89% coverage: 11:434/479 of query aligns to 14:419/487 of P82251
- V40 (= V37) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ VIGAG 40:44) binding
- I44 (= I41) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (≠ I48) to F: in CSNU; uncertain significance
- P52 (≠ T49) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (≠ V66) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y95) to H: in CSNU; uncertain significance
- G105 (= G101) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W110) to R: in CSNU; uncertain significance
- I120 (≠ E115) to L: in CSNU; uncertain significance
- T123 (≠ L118) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (≠ F153) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ D155) modified: Interchain (with C-114 in SLC3A1)
- V170 (≠ T184) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (= A196) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (= G209) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ R238) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (= A239) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (≠ S242) to D: in CSNU; decreased amino acid transport activity
- W230 (≠ Y245) to R: in CSNU; complete loss of amino acid transport activity; mutation to A: Abolishes amino acid transport activity.
- D233 (≠ I248) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ F250) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ A252) mutation to A: Reduces amino acid transport activity.
- G259 (≠ S274) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ A276) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (≠ A301) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ T330) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ L340) to E: in CSNU; uncertain significance
- V330 (≠ S346) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ M347) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (≠ G349) to Q: in CSNU; decreased amino acid transport activity; dbSNP:rs769576205; to W: in CSNU; severe loss of amino acid transport activity; dbSNP:rs121908484
- A354 (≠ T370) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (= S395) mutation to A: Markedly reduces amino acid transport activity.
- A382 (≠ T398) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (≠ L399) mutation to A: Complete loss of amino acid transport activity.
- Y386 (≠ F402) mutation to A: Loss of amino acid transport activity.
- K401 (≠ P417) to E: in CSNU; uncertain significance; dbSNP:rs760264924
Sites not aligning to the query:
- 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.
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
27% identity, 94% coverage: 23:472/479 of query aligns to 18:447/461 of P76037
- Y110 (= Y116) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
23% identity, 87% coverage: 23:437/479 of query aligns to 1:393/433 of 6f2wA
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
24% identity, 96% coverage: 14:471/479 of query aligns to 4:468/489 of P25737
- Y102 (= Y130) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ L134) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K198) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (≠ Y245) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (≠ D251) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E259) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ V304) 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 (≠ A307) 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.
- E438 (≠ C439) mutation to A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D443 (≠ A444) mutation to A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D446 (≠ N447) mutation to A: Retains 13% of wild-type lysine uptake activity. Is unable to inhibit CadC.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6li9B Heteromeric amino acid transporter b0,+at-rbat complex bound with arginine (see paper)
22% identity, 85% coverage: 27:434/479 of query aligns to 1:390/458 of 6li9B
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
22% identity, 89% coverage: 18:445/479 of query aligns to 3:406/438 of O34739
- C94 (≠ I108) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ T177) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ L204) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ V332) 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.
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
23% identity, 81% coverage: 58:444/479 of query aligns to 33:396/455 of 7p9uB
Q9UPY5 Cystine/glutamate transporter; Amino acid transport system xc-; Calcium channel blocker resistance protein CCBR1; Solute carrier family 7 member 11; xCT from Homo sapiens (Human) (see 4 papers)
23% identity, 81% coverage: 58:444/479 of query aligns to 77:440/501 of Q9UPY5
- C86 (≠ A68) mutation to S: Does not affect L-cystine transport activity; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-158; S-197; S-271; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- R135 (≠ A119) binding ; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (vs. gap) modified: Interchain (with C-210 in SLC3A2); mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-197; S-271; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- Q191 (≠ T188) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ V194) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-271; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-271; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-271; S-327; S-414 and S-435.
- K198 (= K198) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
- Y244 (vs. gap) binding
- F254 (≠ T255) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ L272) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-327; S-414 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- C327 (≠ Q322) mutation to A: Does not affect L-glutamate transport activity. Does not affect location at cell membrane Does not affect expression level.; mutation to L: Loss of L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.; mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-414 and S-435. Loss of inhibitio nof L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid. Decrease L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.; mutation to T: Does not affect L-glutamate transport activity. Does not affect location at cell membrane. Does not affect expression level.
- F336 (≠ L338) mutation to A: Decreases L-cystine transport activity about 50%. Increases sensitivity to erastin-induced ferroptosis. Significantly decreases the L-cystine transport activity.; mutation to Y: Does not affect L-cystine transport activity.
- R396 (≠ T398) mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.; mutation to N: Loss of L-cystine transport activity.
- C414 (≠ H416) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-327 and S-435. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
- C435 (= C439) mutation to S: Does not affect L-cystine transport activity; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Does not affect affinity for L-cystine; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Significantly increases L-glutamate affinity; when associated with S-86; S-158; S-197; S-271; S-327 and S-414. Does not affect inhibition of L-glutamate transport activity by p-chloromercuribenzoic acid and p-chloromercuribenzenesulfonic acid.
7epzB Overall structure of erastin-bound xct-4f2hc complex (see paper)
23% identity, 81% coverage: 58:444/479 of query aligns to 33:396/453 of 7epzB
Sites not aligning to the query:
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
23% identity, 73% coverage: 19:369/479 of query aligns to 4:321/469 of P46349
- G33 (≠ I48) mutation to D: Lack of activity.
- G42 (= G58) mutation to S: Lack of activity.
- G301 (= G339) mutation to V: Lack of activity.
Sites not aligning to the query:
- 338 G→E: Lack of activity.
- 341 F→S: Lack of activity.
- 414 G→R: Lack of activity.
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)
23% identity, 84% coverage: 22:425/479 of query aligns to 34:421/531 of Q9QXW9
- Y130 (= Y116) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (≠ A119) 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.
- F242 (≠ Y245) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
Q7YQK4 Large neutral amino acids transporter small subunit 1; 4F2 light chain; 4F2 LC; 4F2LC; L-type amino acid transporter 1; LAT1; Solute carrier family 7 member 5 from Oryctolagus cuniculus (Rabbit) (see 2 papers)
28% identity, 45% coverage: 228:444/479 of query aligns to 231:444/503 of Q7YQK4
- W234 (≠ Y231) mutation to L: Decreased KM and Vmax for Trp. Increased KM but decreased Vmax for Phe. Increased KM and Vmax for Phe; when associated with D-219.
- C331 (≠ Q322) mutation to S: No significant effect on inhibition by HgCl(2). Increased KM and Vmax for Phe.
- C377 (≠ G375) mutation to S: No significant effect on inhibition by HgCl(2).
- C403 (≠ A401) mutation to S: No significant effect on inhibition by HgCl(2).
- C439 (= C439) mutation to S: Prevents insertion into the plasma membrane and possibly protein folding.
Sites not aligning to the query:
- 88 C→S: No significant effect on inhibition by HgCl(2). Decreased KM and Vmax for Phe. Similar affect on KM and Vmax for Phe; when associated with S-183.
- 98 C→S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe. Slightly less decreased KM and Vmax for Phe; when associated with S-183.
- 160 C→S: No change to KM or Vmax for Phe.
- 172 C→S: No change to KM or Vmax for Phe.
- 174 C→S: No change to KM or Vmax for Phe.
- 183 C→S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe. Similar affect on KM and Vmax for Phe; when associated with S-88. Slightly less decreased KM and Vmax for Phe; when associated with S-98.
- 219 G→D: Decreased KM and Vmax for Trp. Increased KM and Vmax for Phe; when associated with L-234.
- 454 C→S: No significant effect on inhibition by HgCl(2). Slightly increased KM but slightly decreased Vmax for Phe.
- 492 C→S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe.
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)
23% identity, 84% coverage: 22:425/479 of query aligns to 35:422/535 of Q9UHI5
- I53 (≠ V40) binding
- Y93 (= Y79) 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 (≠ A119) 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 (≠ G156) modified: Interchain (with C-210 in SLC3A2)
- W174 (≠ A178) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (≠ Y245) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ I248) Important for substrate specificity; binding ; mutation to 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.
- V302 (= V304) to I: found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity
- N395 (≠ T398) binding ; mutation to Q: Strongly reduces L-leucine uptake activity. Strongly reduces L-tryptophan uptake activity.
- Y396 (≠ L399) mutation to A: Strongly reduces L-leucine uptake activity.
- T402 (≠ V405) to M: found in a patient with age-related hearing loss; strongly decreased L-alanine transport activity. Decreases L-tyrosine transport activity
- R418 (= R421) to C: found in a patient with age-related hearing loss; decreases L-alanine transport activity. Decreases L-tyrosine transport activity
Sites not aligning to the query:
- 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
7nf6B Ovine b0,+at-rbat heterodimer (see paper)
22% identity, 84% coverage: 27:426/479 of query aligns to 2:382/455 of 7nf6B
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
21% identity, 84% coverage: 14:413/479 of query aligns to 10:393/458 of P24207
- R26 (≠ K30) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P59) mutation to A: 50% of wild-type phenylalanine transport activity.; mutation to G: No change in phenylalanine transport activity.; mutation to L: 26% of wild-type phenylalanine transport activity.
- F87 (≠ A92) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y95) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (= Y97) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (≠ T99) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ F100) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ L103) mutation to L: No effect on phenylalanine transport activity.
- F101 (≠ W106) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W110) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (≠ V112) mutation to L: No effect on phenylalanine transport activity.
- W108 (≠ V113) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ Y116) mutation to L: 60% of wild-type phenylalanine transport activity.; mutation to Y: Enables the transport of tryptophan to almost the same steady-state level as that of phenylalanine.
- E118 (≠ L134) mutation E->G,L,V,N: Loss of activity.
- K168 (≠ V195) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (≠ D251) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (≠ I277) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P367) mutation to A: 5% of wild-type phenylalanine transport activity.; mutation P->G,Q,K,R: Loss of activity.; mutation to S: 3% of wild-type phenylalanine transport activity.; mutation to T: 17% of wild-type phenylalanine transport activity.
Sites not aligning to the query:
- 442 P→A: 46% of wild-type phenylalanine transport activity.; P→G: 52% of wild-type phenylalanine transport activity.; P→L: 43% of wild-type phenylalanine transport activity.
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
23% identity, 81% coverage: 37:425/479 of query aligns to 10:382/457 of 7b00A
Sites not aligning to the query:
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, 89% coverage: 21:444/479 of query aligns to 9:414/457 of P15993
- Y103 (= Y116) 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%.
Query Sequence
>N515DRAFT_0722 FitnessBrowser__Dyella79:N515DRAFT_0722
MSLIRSLFAVKPVEASLTADDSLRRTLGLKELVVLGVGAVIGAGIFVITGQAAAEHAGPA
LTLSFVLAGLAAALAALSYAEFAAMLPVSGSAYVYAYATFGELLAWFIGWNVVAEYLLAV
SSVAVGWSGYGVGLLKSLGIEVPAALANAPLSFKDGHLELTGALLNLPALLVVAALTALL
YRGTRQSTMFASVVVALKVIVVVLFVVCGLQYVDPSLWHPYVPANQGGDHYGWAGVFRAA
TSVFYAYIGFDAVATAAQETRNPQRNVPAGILISLAICTVLYIIVAAVLTGLVPYPQLAT
AEPVATALAAHPPLAWLKLLTQVGAVAGLTSVILVMHLGLSRILYSMAGDGLLPTFFGAV
HERHRTPHRTTLLVGAVGGVLAAVFPLSLLGDLLSMGTLLAFATVCIGVLVLRRTHPNLP
RGFRVPAAPAVCTLGVLVCAFLLAQMNLGNWILLAAWTTLGMLIYIAYGYRHSLMRRRG
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