SitesBLAST
Comparing PfGW456L13_3582 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3582 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
29% identity, 75% coverage: 32:444/548 of query aligns to 51:450/456 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)
29% identity, 75% coverage: 32:444/548 of query aligns to 53:452/458 of 6f34A
- binding arginine: E115 (≠ A98), Y116 (≠ F99), A119 (= A109), F228 (= F210), A229 (= A211), I231 (≠ L213), V314 (≠ C305)
- binding cholesterol: W201 (≠ T179), Y202 (≠ F180)
- binding : A178 (= A156), R179 (≠ K157), A186 (≠ M164), I187 (≠ F165), A190 (≠ I168), L194 (= L172), Q296 (≠ R279), V299 (≠ L290)
Sites not aligning to the query:
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, 72% coverage: 6:399/548 of query aligns to 25:409/487 of P82251
- V40 (≠ L21) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ IFGSG 24:28) binding
- I44 (≠ F25) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (≠ A32) to F: in CSNU; uncertain significance
- P52 (≠ A33) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (≠ L49) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y78) to H: in CSNU; uncertain significance
- G105 (= G84) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (≠ F93) to R: in CSNU; uncertain significance
- I120 (≠ F99) to L: in CSNU; uncertain significance
- T123 (≠ S101) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (≠ A124) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ S126) modified: Interchain (with C-114 in SLC3A1)
- V170 (= V152) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ M164) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (vs. gap) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ I208) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (≠ I209) 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 (≠ L213) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ L215) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ P217) mutation to A: Reduces amino acid transport activity.
- G259 (≠ S239) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ L241) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (≠ A271) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ M310) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ T313) to E: in CSNU; uncertain significance
- V330 (≠ G319) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ W320) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (≠ Q322) 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 (= A343) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (= S369) mutation to A: Markedly reduces amino acid transport activity.
- A382 (≠ L372) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (≠ V373) mutation to A: Complete loss of amino acid transport activity.
- Y386 (= Y376) mutation to A: Loss of amino acid transport activity.
- K401 (≠ P391) 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.
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
24% identity, 72% coverage: 4:400/548 of query aligns to 5:397/469 of P46349
- G33 (≠ A32) mutation to D: Lack of activity.
- G42 (= G41) mutation to S: Lack of activity.
- G301 (≠ Y309) mutation to V: Lack of activity.
- G338 (vs. gap) mutation to E: Lack of activity.
- F341 (≠ W345) mutation to S: Lack of activity.
Sites not aligning to the query:
- 414 G→R: Lack of activity.
6li9B Heteromeric amino acid transporter b0,+at-rbat complex bound with arginine (see paper)
25% identity, 71% coverage: 11:399/548 of query aligns to 1:380/458 of 6li9B
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, 78% coverage: 7:435/548 of query aligns to 36:457/535 of Q9UHI5
- I53 (= I24) binding
- Y93 (= Y62) 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 (≠ L102) 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 (≠ L121) modified: Interchain (with C-210 in SLC3A2)
- W174 (≠ M146) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (= F210) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ L213) 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 (≠ A268) to I: found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity
- N395 (≠ L372) binding ; mutation to Q: Strongly reduces L-leucine uptake activity. Strongly reduces L-tryptophan uptake activity.
- Y396 (≠ V373) mutation to A: Strongly reduces L-leucine uptake activity.
- T402 (≠ A379) to M: found in a patient with age-related hearing loss; strongly decreased L-alanine transport activity. Decreases L-tyrosine transport activity
- R418 (= R395) 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)
26% identity, 78% coverage: 7:435/548 of query aligns to 35:456/531 of Q9QXW9
- Y130 (≠ F99) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (≠ L102) 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 (= F210) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
25% identity, 71% coverage: 9:399/548 of query aligns to 2:381/433 of 6f2wA
7nf6B Ovine b0,+at-rbat heterodimer (see paper)
25% identity, 71% coverage: 10:399/548 of query aligns to 1:381/455 of 7nf6B
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
25% identity, 76% coverage: 19:435/548 of query aligns to 8:417/458 of 7cmiB
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
25% identity, 76% coverage: 19:435/548 of query aligns to 8:417/458 of 7cmhB
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
25% identity, 76% coverage: 19:435/548 of query aligns to 8:417/457 of 7b00A
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
26% identity, 62% coverage: 8:347/548 of query aligns to 14:352/489 of P25737
- Y102 (≠ T95) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ F99) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K166) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F210) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (≠ T216) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E224) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ G266) 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 (≠ E273) 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.
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
24% identity, 72% coverage: 8:399/548 of query aligns to 9:386/438 of O34739
- C94 (≠ M91) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (= C142) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ V173) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (= C305) 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.
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)
24% identity, 72% coverage: 1:392/548 of query aligns to 2:390/457 of P15993
- Y103 (≠ F99) 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%.
Q01650 Large neutral amino acids transporter small subunit 1; 4F2 light chain; 4F2 LC; 4F2LC; CD98 light chain; Integral membrane protein E16; E16; L-type amino acid transporter 1; hLAT1; Solute carrier family 7 member 5; y+ system cationic amino acid transporter from Homo sapiens (Human) (see 3 papers)
24% identity, 77% coverage: 2:424/548 of query aligns to 38:454/507 of Q01650
- Y117 (≠ V76) mutation to A: Strongly decreased leucine transport activity.
- C164 (≠ S126) modified: Interchain (with C-210 in SLC3A2)
- D223 (vs. gap) to V: in dbSNP:rs17853937
- N230 (= N185) to K: in dbSNP:rs1060250
- A246 (= A202) mutation to V: Nearly abolishes leucine transport activity.
- F252 (= F210) mutation to A: Nearly abolishes leucine transport activity.
- W257 (≠ L215) mutation to A: Nearly abolishes leucine transport activity.
- N258 (≠ T216) mutation to A: Decreased leucine transport activity.; mutation to D: Nearly abolishes leucine transport activity.
- Y259 (≠ P217) mutation to A: Strongly decreased leucine transport activity.
- E303 (= E261) mutation to K: Decreased leucine transport activity.
- P375 (= P342) mutation to L: Nearly abolishes leucine transport activity.
Sites not aligning to the query:
- 483:507 mutation Missing: Nearly abolishes leucine 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)
28% identity, 38% coverage: 190:395/548 of query aligns to 246:438/629 of P30825
Sites not aligning to the query:
- 226 modified: carbohydrate, N-linked (GlcNAc...) asparagine
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
25% identity, 64% coverage: 48:399/548 of query aligns to 39:379/455 of 7p9uB
7epzB Overall structure of erastin-bound xct-4f2hc complex (see paper)
25% identity, 64% coverage: 48:399/548 of query aligns to 39:379/453 of 7epzB
Sites not aligning to the query:
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)
25% identity, 77% coverage: 2:424/548 of query aligns to 36:450/503 of Q7YQK4
- C88 (≠ G51) 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 (≠ V61) 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 (≠ S126) mutation to S: No change to KM or Vmax for Phe.
- C172 (≠ F138) mutation to S: No change to KM or Vmax for Phe.
- C174 (≠ L140) mutation to S: No change to KM or Vmax for Phe.
- C183 (≠ Y149) 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 (≠ F194) 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 (≠ P302) mutation to S: No significant effect on inhibition by HgCl(2). Increased KM and Vmax for Phe.
- C377 (≠ F348) mutation to S: No significant effect on inhibition by HgCl(2).
- C403 (≠ S375) mutation to S: No significant effect on inhibition by HgCl(2).
- C439 (≠ A414) 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.
Query Sequence
>PfGW456L13_3582 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_3582
MSGQGKFKKQLSLIDLTFIGLGAIFGSGWLFAASHVSAIAGPAGIFSWLLGGFAVLLLGI
VYCELGAALPRAGGVVRYPVYSHGPLLGYLMGFITLIAFSSLVAIEVVAARQYAAAWFPA
LTQAGSSNPTAIGWLVQFGLLCLFFMLNYYSVKTFAKANNLISMFKFIVPLLVIGVLFTF
FKPENFQSQGFMPFGLSGVEMAVSAGGIIFAYLGLTPIISVASEVKNPQRTIPIALILSV
LLSTAIYVLLQVAFLGGVPTEMLANGWAGVAKELALPYRDIALALGVGWLAYLVVADAVI
SPSGCGNIYMNATPRVIYGWAQTGTFFKVFTRIDEKSGIPRPALWLTFALSVFWTLPFPS
WEALINVVSAALVLSYAVAPVSVAALRRNAPDMPRPFKVKRMGVLGPVSFIIAALIVYWS
GWSTVSWLLGLQILMFVVYLLCGRFVPTQHLSLAQQVRSSAWLIGFYAVTIVLSWLGSFG
GMGVLTHPFDTVVVAACAMGIYYWGAATGVPAHLVRLEDEDGESQADPVHTGTTAGQRPI
GVSAQTSR
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