SitesBLAST
Comparing BPHYT_RS01785 FitnessBrowser__BFirm:BPHYT_RS01785 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)
60% identity, 99% coverage: 3:462/463 of query aligns to 1:456/456 of 5oqtA
- binding alanine: I38 (= I39), G40 (= G41), T41 (= T42), G42 (= G43), F226 (= F231), A227 (= A232), I229 (= I234)
- binding : E24 (≠ A25), G26 (= G27), F28 (≠ L29), D29 (= D30), M32 (≠ F33), A176 (= A181), R177 (= R182), A184 (= A189), A188 (≠ V193), L192 (= L197), Q294 (≠ E300), V297 (= V303)
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
59% identity, 100% coverage: 1:462/463 of query aligns to 1:458/458 of 6f34A
- binding arginine: I40 (= I39), G42 (= G41), T43 (= T42), G44 (= G43), E115 (= E113), Y116 (= Y114), A119 (= A117), F228 (= F231), A229 (= A232), I231 (= I234), V314 (= V318)
- binding cholesterol: W201 (≠ F204), Y202 (≠ H205)
- binding : G28 (= G27), F30 (≠ L29), D31 (= D30), M34 (≠ F33), A178 (= A181), R179 (= R182), A186 (= A189), I187 (= I190), A190 (≠ V193), L194 (= L197), Q296 (≠ E300), V299 (= V303)
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)
35% identity, 88% coverage: 1:407/463 of query aligns to 11:438/629 of P30825
- N226 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
24% identity, 95% coverage: 18:459/463 of query aligns to 4:437/438 of O34739
- C94 (≠ I106) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ M167) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ L197) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ V318) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
- C415 (≠ F440) mutation to 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)
24% identity, 98% coverage: 5:460/463 of query aligns to 9:467/487 of P82251
- V40 (= V36) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ IIGTG 39:43) binding
- I44 (= I40) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (vs. gap) to F: in CSNU; uncertain significance
- P52 (vs. gap) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (≠ I68) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y93) to H: in CSNU; uncertain significance
- G105 (= G99) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W108) to R: in CSNU; uncertain significance
- I120 (≠ E113) to L: in CSNU; uncertain significance
- T123 (≠ L116) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (vs. gap) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ A150) modified: Interchain (with C-114 in SLC3A1)
- V170 (= V177) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (= A189) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (= G202) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ V228) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (≠ M229) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (vs. gap) to D: in CSNU; decreased amino acid transport activity
- W230 (vs. gap) to R: in CSNU; complete loss of amino acid transport activity; mutation to A: Abolishes amino acid transport activity.
- D233 (≠ I234) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ F236) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ S238) mutation to A: Reduces amino acid transport activity.
- G259 (≠ S260) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ G262) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (≠ N286) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ A323) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ Q326) to E: in CSNU; uncertain significance
- V330 (≠ A332) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ M333) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (= R335) 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 (≠ T356) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (≠ T384) mutation to A: Markedly reduces amino acid transport activity.
- A382 (= A387) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (vs. gap) mutation to A: Complete loss of amino acid transport activity.
- Y386 (≠ F388) mutation to A: Loss of amino acid transport activity.
- K401 (≠ P403) to E: in CSNU; uncertain significance; dbSNP:rs760264924
- L426 (≠ V430) to P: in CSNU; uncertain significance
Sites not aligning to the query:
- 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)
24% identity, 97% coverage: 13:461/463 of query aligns to 9:448/461 of P76037
- Y110 (= Y114) 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)
24% identity, 95% coverage: 22:460/463 of query aligns to 1:433/433 of 6f2wA
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
24% identity, 72% coverage: 15:349/463 of query aligns to 12:338/458 of P24207
- R26 (≠ L29) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P57) 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 (≠ I90) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y93) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (= Y95) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (≠ T97) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ L98) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ L101) mutation to L: No effect on phenylalanine transport activity.
- F101 (≠ W104) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W108) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (≠ L110) mutation to L: No effect on phenylalanine transport activity.
- W108 (≠ M111) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ Y114) 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 (≠ V121) mutation E->G,L,V,N: Loss of activity.
- K168 (= K191) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (≠ D237) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (≠ V263) mutation R->D,E,F,W,P: Loss of activity.
Sites not aligning to the query:
- 341 P→A: 5% of wild-type phenylalanine transport activity.; mutation P->G,Q,K,R: Loss of activity.; P→S: 3% of wild-type phenylalanine transport activity.; P→T: 17% of wild-type phenylalanine transport activity.
- 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.
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)
27% identity, 92% coverage: 5:429/463 of query aligns to 23:443/503 of Q7YQK4
- C88 (≠ A69) mutation to 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.
- C98 (≠ A76) mutation to 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.
- C160 (≠ L140) mutation to S: No change to KM or Vmax for Phe.
- C172 (≠ F163) mutation to S: No change to KM or Vmax for Phe.
- C174 (≠ V165) mutation to S: No change to KM or Vmax for Phe.
- C183 (≠ S174) mutation to 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.
- G219 (vs. gap) mutation to D: Decreased KM and Vmax for Trp. Increased KM and Vmax for Phe; when associated with L-234.
- W234 (= W219) 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 (≠ D308) mutation to S: No significant effect on inhibition by HgCl(2). Increased KM and Vmax for Phe.
- C377 (≠ T357) mutation to S: No significant effect on inhibition by HgCl(2).
- C403 (≠ A377) mutation to S: No significant effect on inhibition by HgCl(2).
- C439 (= C425) mutation to S: Prevents insertion into the plasma membrane and possibly protein folding.
Sites not aligning to the query:
- 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)
27% identity, 84% coverage: 22:410/463 of query aligns to 36:421/535 of Q9UHI5
- I53 (= I39) binding
- Y93 (= Y77) 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 (≠ A117) 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 (≠ A150) modified: Interchain (with C-210 in SLC3A2)
- W174 (≠ A171) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (= F231) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ I234) 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 (≠ H289) to I: found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity
- N395 (≠ A387) binding ; mutation to Q: Strongly reduces L-leucine uptake activity. Strongly reduces L-tryptophan uptake activity.
- Y396 (≠ F388) mutation to A: Strongly reduces L-leucine uptake activity.
- T402 (≠ A394) to M: found in a patient with age-related hearing loss; strongly decreased L-alanine transport activity. Decreases L-tyrosine transport activity
- R418 (= R407) 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
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, 84% coverage: 22:410/463 of query aligns to 35:420/531 of Q9QXW9
- Y130 (= Y114) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (≠ A117) 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 (= F231) mutation to 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)
27% identity, 81% coverage: 36:410/463 of query aligns to 10:381/458 of 7cmiB
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
27% identity, 81% coverage: 36:410/463 of query aligns to 10:381/458 of 7cmhB
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
27% identity, 81% coverage: 36:410/463 of query aligns to 10:381/457 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)
23% identity, 87% coverage: 12:412/463 of query aligns to 1:398/457 of P15993
- Y103 (= Y114) 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%.
6li9B Heteromeric amino acid transporter b0,+at-rbat complex bound with arginine (see paper)
25% identity, 92% coverage: 36:460/463 of query aligns to 11:438/458 of 6li9B
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
25% identity, 95% coverage: 16:455/463 of query aligns to 7:468/489 of P25737
- Y102 (≠ L110) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ Y114) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (≠ A189) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F231) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (≠ D237) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E245) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ Q283) 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 (≠ N286) 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 (≠ Q433) mutation to A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D443 (vs. gap) mutation to A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D446 (≠ T436) 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
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)
25% identity, 83% coverage: 46:429/463 of query aligns to 69:439/501 of Q9UPY5
- C86 (≠ A66) 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 (≠ Y114) 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 (≠ N184) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ I190) 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 (= K191) 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 (≠ S241) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ I258) 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 (≠ M315) 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 (≠ Y324) 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 (≠ A387) 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 (≠ H402) 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 (= C425) 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)
25% identity, 83% coverage: 46:429/463 of query aligns to 25:395/453 of 7epzB
Sites not aligning to the query:
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
25% identity, 83% coverage: 46:429/463 of query aligns to 25:395/455 of 7p9uB
Query Sequence
>BPHYT_RS01785 FitnessBrowser__BFirm:BPHYT_RS01785
MSLFRKKNVEHMIAASAQNAGLKKALGALDLTFLGVGAIIGTGIFVLTGTGAVQAGPALM
ISFLIAAIACGFAALAYAEFASTIPVAGSIYTYSYATLGELAAWIIGWDLMLEYGLATSA
VSVGWSGYLQSLLSGFGVSLPVALTAAPGALPGHDTLFNLPAFLVMMAITALLSVGVRES
ARINNVMVAIKVVVVLLVIGVGVFHVTPANWHPFMPNGWNGVFGAAAVMFFAFIGFDSVS
SAAEEVKDPKRDLPIGIIASLGVCAVLYVAVAAVVTGIVPSAQFANISHPVSYALQVAGE
KWVAGFIDLGAVLGMLTVILVMAYGQTRVIFAMSRDGLLPERLSRVHPRFATPFFTTWLV
GIFFGLIGALVPLNVLAELINIGTLAAFSMVSIAVLVLRKTHPDLPRAFRCPGVPVVPVL
AVAACLFLMVNLQAVTWVAFVVWLLVGMVIYFGYSRRHSKLSK
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