SitesBLAST
Comparing BWI76_RS10720 FitnessBrowser__Koxy:BWI76_RS10720 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 15 hits to proteins with known functional sites (download)
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
92% identity, 98% coverage: 1:456/463 of query aligns to 1:455/461 of P76037
- Y110 (= Y110) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
25% identity, 81% coverage: 16:391/463 of query aligns to 11:400/489 of P25737
- Y102 (≠ S106) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ Y110) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (≠ Q167) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F216) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (≠ D222) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E230) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ A276) 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 (≠ E279) 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.
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
26% identity, 94% coverage: 7:440/463 of query aligns to 12:450/458 of 6f34A
- binding arginine: I40 (≠ L35), G42 (≠ P37), T43 (≠ M38), G44 (≠ T39), E115 (≠ D109), Y116 (= Y110), A119 (vs. gap), F228 (= F216), A229 (≠ S217), I231 (≠ L219), V314 (≠ T301)
- binding cholesterol: W201 (= W192), Y202 (≠ S193)
- binding : G28 (≠ K23), F30 (≠ W25), D31 (≠ Q26), M34 (= M29), A178 (= A157), R179 (≠ N158), A186 (≠ L165), I187 (≠ V166), A190 (≠ S169), L194 (≠ V173), Q296 (≠ L282), V299 (= V284)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
26% identity, 94% coverage: 7:440/463 of query aligns to 10:448/456 of 5oqtA
- binding alanine: I38 (≠ L35), G40 (≠ P37), T41 (≠ M38), G42 (≠ T39), F226 (= F216), A227 (≠ S217), I229 (≠ L219)
- binding : E24 (≠ S21), G26 (≠ K23), F28 (≠ W25), D29 (≠ Q26), M32 (= M29), A176 (= A157), R177 (≠ N158), A184 (≠ L165), A188 (≠ S169), L192 (≠ V173), Q294 (≠ L282), V297 (= V284)
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
27% identity, 52% coverage: 2:242/463 of query aligns to 4:246/458 of P24207
- R26 (≠ W25) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (≠ G53) 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 (≠ A86) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y89) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ Q91) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (≠ S93) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ I94) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ H97) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F100) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W104) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (≠ S106) mutation to L: No effect on phenylalanine transport activity.
- W108 (≠ L107) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ Y110) 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 (≠ N117) mutation E->G,L,V,N: Loss of activity.
- K168 (≠ Q167) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (≠ D222) mutation E->A,Q,K,R,W: Loss of activity.
Sites not aligning to the query:
- 252 mutation R->D,E,F,W,P: Loss of activity.
- 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.
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)
21% identity, 79% coverage: 15:382/463 of query aligns to 25:428/629 of P30825
- N226 (≠ S199) modified: carbohydrate, N-linked (GlcNAc...) asparagine
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
25% identity, 69% coverage: 9:328/463 of query aligns to 2:321/469 of P46349
- G33 (≠ T43) mutation to D: Lack of activity.
- G42 (≠ N52) mutation to S: Lack of activity.
- G301 (= G305) 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.
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)
25% identity, 36% coverage: 74:241/463 of query aligns to 67:237/457 of P15993
- Y103 (= Y110) 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%.
Q9URZ4 Cationic amino acid transporter 1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
25% identity, 49% coverage: 18:242/463 of query aligns to 80:308/587 of Q9URZ4
Sites not aligning to the query:
- 29 modified: Phosphoserine
- 30 modified: Phosphoserine
- 37 modified: Phosphoserine
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
25% identity, 61% coverage: 60:340/463 of query aligns to 56:328/438 of O34739
- C94 (≠ V102) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ A143) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ I170) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (= C295) 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.
Q9UT18 Thiamine transporter thi9 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
22% identity, 81% coverage: 5:379/463 of query aligns to 55:494/591 of Q9UT18
- E81 (≠ Q26) mutation to K: Accumulates in the endoplasmic reticulum and punctuate cytoplasmic structures.
Sites not aligning to the query:
- 585 modified: Phosphoserine
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)
22% identity, 70% coverage: 67:388/463 of query aligns to 91:411/501 of Q9UPY5
- R135 (vs. gap) binding ; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (≠ A127) 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 (≠ N160) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ V166) 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 (≠ Q167) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
- Y244 (≠ F216) binding
- F254 (≠ T226) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ F243) 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 (≠ F298) 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 (≠ A310) 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 (≠ A373) 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.
Sites not aligning to the query:
- 86 C→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.
- 414 C→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.
- 435 C→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.
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
27% identity, 67% coverage: 80:389/463 of query aligns to 64:370/433 of 6f2wA
Sites not aligning to the query:
7epzB Overall structure of erastin-bound xct-4f2hc complex (see paper)
22% identity, 70% coverage: 67:388/463 of query aligns to 47:367/453 of 7epzB
Sites not aligning to the query:
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
22% identity, 70% coverage: 67:388/463 of query aligns to 47:367/455 of 7p9uB
Query Sequence
>BWI76_RS10720 FitnessBrowser__Koxy:BWI76_RS10720
MAINTSLDNASEAGKPRLRKSLKLWQVVMMGLAYLTPMTVFDTFGIVSGISNGHVPASYL
LALAGVLFTAISYGKLVRQFPQAGSAYTYAQKSISPHVGFMVGWSSLLDYLFLPMINVLL
AKIYLSALFPDVPPWVWVVTFVAILTAANLKSVNLVANFNTLFVLVQISIMVVFIVLVVQ
GLHKGEGVGTVWSLQPFISQNAHLIPIITGATIVCFSFLGFDAVTTLSEETPDAARVIPK
AIFLTAVYGGVIFIAASFFMQLFFPDISRFKDPDAALPEIALYVGGKLFQSIFLCTTFVN
TLASGLASHASVSRLLYVMGRDNVFPERIFGYVHPKWRTPALNVIMVGIVALSALFFDLV
TATALINFGALVAFTFVNLSVFNHFWRRKGFNKTWKDRFHYLLLPMVGALTVGVLWINLE
ATSLTLGLIWAGLGLLYLTYLTRRFRKPPPQFDGAKAEQAWES
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