SitesBLAST
Comparing N515DRAFT_2924 FitnessBrowser__Dyella79:N515DRAFT_2924 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)
51% identity, 97% coverage: 12:488/492 of query aligns to 5:456/456 of 5oqtA
- binding alanine: I38 (= I46), G40 (= G48), T41 (≠ A49), G42 (= G50), F226 (= F257), A227 (≠ S258), I229 (= I260)
- binding : E24 (≠ A32), G26 (≠ T34), F28 (≠ R36), D29 (≠ H37), M32 (≠ L40), A176 (= A200), R177 (≠ F201), A184 (= A208), A188 (≠ T212), L192 (= L216), Q294 (≠ L326), V297 (≠ L329)
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
50% identity, 99% coverage: 4:488/492 of query aligns to 2:458/458 of 6f34A
- binding arginine: I40 (= I46), G42 (= G48), T43 (≠ A49), G44 (= G50), E115 (= E121), Y116 (= Y122), A119 (≠ T125), F228 (= F257), A229 (≠ S258), I231 (= I260), V314 (= V344)
- binding cholesterol: W201 (≠ K223), Y202 (= Y224)
- binding : G28 (≠ T34), F30 (≠ R36), D31 (≠ H37), M34 (≠ L40), A178 (= A200), R179 (≠ F201), A186 (= A208), I187 (= I209), A190 (≠ T212), L194 (= L216), Q296 (≠ L326), V299 (≠ L329)
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)
34% identity, 84% coverage: 23:433/492 of query aligns to 22:438/629 of P30825
- N226 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
23% identity, 92% coverage: 25:475/492 of query aligns to 14:436/461 of P76037
- Y110 (= Y122) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
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, 91% coverage: 43:490/492 of query aligns to 40:468/487 of P82251
- V40 (≠ I43) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ IIGAG 46:50) binding
- I44 (= I47) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (≠ I54) to F: in CSNU; uncertain significance
- P52 (≠ T55) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (≠ V72) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y101) to H: in CSNU; uncertain significance
- G105 (= G107) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W116) to R: in CSNU; uncertain significance
- I120 (≠ E121) to L: in CSNU; uncertain significance
- T123 (≠ F124) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (= V165) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ I170) modified: Interchain (with C-114 in SLC3A1)
- V170 (≠ I196) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (= A208) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (≠ A221) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ I254) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (≠ V255) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (≠ S258) 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 (≠ I260) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ F262) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ A264) mutation to A: Reduces amino acid transport activity.
- G259 (≠ S286) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ I288) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (≠ T312) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ L349) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ Q352) to E: in CSNU; uncertain significance
- V330 (≠ S358) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ M359) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (= R361) 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 (≠ G382) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (≠ A407) mutation to A: Markedly reduces amino acid transport activity.
- A382 (≠ T410) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (≠ L411) mutation to A: Complete loss of amino acid transport activity.
- Y386 (≠ F414) mutation to A: Loss of amino acid transport activity.
- K401 (≠ P429) to E: in CSNU; uncertain significance; dbSNP:rs760264924
- L426 (≠ M452) 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.
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, 89% coverage: 21:460/492 of query aligns to 4:417/457 of P15993
- Y103 (= Y122) 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)
24% identity, 91% coverage: 43:490/492 of query aligns to 11:439/458 of 6li9B
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
23% identity, 85% coverage: 24:439/492 of query aligns to 2:388/438 of O34739
- C94 (≠ V114) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ V165) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ L216) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ V344) 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.
7nf6B Ovine b0,+at-rbat heterodimer (see paper)
23% identity, 91% coverage: 43:490/492 of query aligns to 12:440/455 of 7nf6B
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
27% identity, 83% coverage: 43:449/492 of query aligns to 14:392/433 of 6f2wA
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
24% identity, 70% coverage: 29:374/492 of query aligns to 13:341/489 of P25737
- Y102 (≠ L118) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ Y122) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K210) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F257) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (≠ D263) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E271) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ P313) 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 (≠ P315) 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.
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
27% identity, 58% coverage: 11:294/492 of query aligns to 1:268/458 of P24207
- R26 (= R36) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P65) 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 (≠ A98) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y101) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (= Y103) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (≠ T105) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ L106) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ Y109) mutation to L: No effect on phenylalanine transport activity.
- F101 (≠ W112) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W116) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (≠ L118) mutation to L: No effect on phenylalanine transport activity.
- W108 (vs. gap) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ E121) 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 (≠ T128) mutation E->G,L,V,N: Loss of activity.
- K168 (≠ T197) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (≠ D263) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (vs. gap) 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)
31% identity, 41% coverage: 257:459/492 of query aligns to 248:447/503 of Q7YQK4
- C331 (≠ S343) mutation to S: No significant effect on inhibition by HgCl(2). Increased KM and Vmax for Phe.
- C377 (≠ G387) mutation to S: No significant effect on inhibition by HgCl(2).
- C403 (≠ A413) mutation to S: No significant effect on inhibition by HgCl(2).
- C439 (= C451) 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.
- 234 W→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.
- 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.
6irtB Human lat1-4f2hc complex bound with bch (see paper)
30% identity, 41% coverage: 257:459/492 of query aligns to 202:401/457 of 6irtB
Sites not aligning to the query:
7dsqB Overall structure of the lat1-4f2hc bound with 3,5-diiodo-l-tyrosine (see paper)
30% identity, 41% coverage: 257:459/492 of query aligns to 209:408/464 of 7dsqB
Sites not aligning to the query:
7dsnB Overall structure of the lat1-4f2hc bound with jx-119 (see paper)
30% identity, 41% coverage: 257:459/492 of query aligns to 209:408/464 of 7dsnB
Sites not aligning to the query:
- binding (2~{S})-2-azanyl-7-[[2-(1,3-benzoxazol-2-yl)phenyl]methoxy]-3,4-dihydro-1~{H}-naphthalene-2-carboxylic acid: 19, 20, 22, 23, 24, 97, 104
- binding cholesterol hemisuccinate: 109, 145, 148, 153, 457
7dslB Overall structure of the lat1-4f2hc bound with jx-078 (see paper)
30% identity, 41% coverage: 257:459/492 of query aligns to 209:408/464 of 7dslB
Sites not aligning to the query:
7dskB Overall structure of the lat1-4f2hc bound with jx-075 (see paper)
30% identity, 41% coverage: 257:459/492 of query aligns to 209:408/464 of 7dskB
Sites not aligning to the query:
- binding (2~{S})-2-azanyl-7-(naphthalen-1-ylmethoxy)-3,4-dihydro-1~{H}-naphthalene-2-carboxylic acid: 19, 20, 23, 24, 97, 100, 101
- binding cholesterol hemisuccinate: 148, 149, 153, 157, 457
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)
30% identity, 41% coverage: 257:459/492 of query aligns to 252:451/507 of Q01650
- F252 (= F257) mutation to A: Nearly abolishes leucine transport activity.
- W257 (≠ F262) mutation to A: Nearly abolishes leucine transport activity.
- N258 (≠ D263) mutation to A: Decreased leucine transport activity.; mutation to D: Nearly abolishes leucine transport activity.
- Y259 (≠ A264) mutation to A: Strongly decreased leucine transport activity.
- E303 (≠ P313) mutation to K: Decreased leucine transport activity.
- P375 (vs. gap) mutation to L: Nearly abolishes leucine transport activity.
Sites not aligning to the query:
- 117 Y→A: Strongly decreased leucine transport activity.
- 164 modified: Interchain (with C-210 in SLC3A2)
- 223 D → V: in dbSNP:rs17853937
- 230 N → K: in dbSNP:rs1060250
- 246 A→V: Nearly abolishes leucine transport activity.
- 483:507 mutation Missing: Nearly abolishes leucine 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)
23% identity, 72% coverage: 24:375/492 of query aligns to 3:328/469 of P46349
- G33 (≠ I54) mutation to D: Lack of activity.
- G42 (= G64) mutation to S: Lack of activity.
- G301 (≠ M348) 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.
Query Sequence
>N515DRAFT_2924 FitnessBrowser__Dyella79:N515DRAFT_2924
MLKNLFATTQISPASADLPGGGAHGEATLKRALTARHLVLLGIGAIIGAGIFVITGQAAA
EHAGPAIVLSFVFAGIACALAALCYAEFAAMLPVSGSAYSYSYATLGEYVAWFVGWSLVL
EYLFTVATVAAGWSGYFNKLLALISGWIGHDVSLPQTLAAAPFTVVDGHIQATGMFINLP
AVAIIAAITGLCYVGITQSAFVNSIIVAIKVTVILLFIAFATKYINPDNWHPFIPASEGA
SKYGWAGVGRAAAIVFFSYIGFDAVSTAAGEAKNPQRDMPIGIIGSLILCTILYIIVAGI
LTGIADFRLLGTPEPVSTALDNYPSLHWLQIIVVIGAVTGLSSVMLVMLMGQPRIFYSMA
RDGLIPAVFGRIHQKFRTPHVGTVVVGVLAAALGGLFNIGVLGEMVAMGTLLAFATVCIG
VLVLRYTRPELPRAFRVPVPWIVCPLGALACMALFLQSFLEHWRWMLAWIAIGQAIYFLY
GYSHSKLRKPAA
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