SitesBLAST
Comparing WP_057509036.1 NCBI__GCF_001431535.1:WP_057509036.1 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)
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
41% identity, 100% coverage: 1:474/475 of query aligns to 1:458/458 of 6f34A
- binding arginine: I40 (= I38), G42 (= G40), T43 (= T41), G44 (= G42), E115 (= E112), Y116 (= Y113), A119 (≠ V116), F228 (= F243), A229 (= A244), I231 (≠ Y246), V314 (= V330)
- binding cholesterol: W201 (≠ P206), Y202 (≠ A207)
- binding : G28 (≠ S26), F30 (≠ P28), D31 (≠ H29), M34 (≠ A32), A178 (= A183), R179 (≠ T184), A186 (≠ V191), I187 (≠ L192), A190 (≠ I195), L194 (≠ V199), Q296 (≠ H312), V299 (≠ A315)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
41% identity, 99% coverage: 3:474/475 of query aligns to 1:456/456 of 5oqtA
- binding alanine: I38 (= I38), G40 (= G40), T41 (= T41), G42 (= G42), F226 (= F243), A227 (= A244), I229 (≠ Y246)
- binding : E24 (≠ T24), G26 (≠ S26), F28 (≠ P28), D29 (≠ H29), M32 (≠ A32), A176 (= A183), R177 (≠ T184), A184 (≠ V191), A188 (≠ I195), L192 (≠ V199), Q294 (≠ H312), V297 (≠ A315)
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: 1:417/475 of query aligns to 11:436/629 of P30825
- N226 (= N212) modified: carbohydrate, N-linked (GlcNAc...) asparagine
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
21% identity, 87% coverage: 59:469/475 of query aligns to 40:430/433 of 6f2wA
Sites not aligning to the query:
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
21% identity, 91% coverage: 7:438/475 of query aligns to 2:418/458 of P24207
- R26 (≠ P28) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (= P56) 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 (≠ A89) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y92) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (= Y94) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (≠ A96) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ L97) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ I100) mutation to L: No effect on phenylalanine transport activity.
- F101 (≠ W103) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W107) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (≠ L109) mutation to L: No effect on phenylalanine transport activity.
- W108 (≠ I110) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ Y113) 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 (= E133) mutation E->G,L,V,N: Loss of activity.
- K168 (≠ A187) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (≠ D249) mutation E->A,Q,K,R,W: Loss of activity.
- R252 (≠ G275) mutation R->D,E,F,W,P: Loss of activity.
- P341 (= P365) 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.
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
24% identity, 95% coverage: 20:469/475 of query aligns to 17:444/461 of P76037
- Y110 (= Y113) 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)
23% identity, 97% coverage: 4:466/475 of query aligns to 6:454/487 of P82251
- V40 (≠ I35) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ IVGTG 38:42) binding
- I44 (≠ V39) 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 (= A63) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y92) to H: in CSNU; uncertain significance
- G105 (= G98) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W107) to R: in CSNU; uncertain significance
- I120 (≠ E112) to L: in CSNU; uncertain significance
- T123 (≠ L115) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (≠ L149) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ A151) modified: Interchain (with C-114 in SLC3A1)
- V170 (≠ T179) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ V191) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (≠ A204) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ F243) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (= A244) 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 (vs. gap) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ F248) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ A250) mutation to A: Reduces amino acid transport activity.
- G259 (≠ S272) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ V274) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (= S299) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ M335) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ Q338) to E: in CSNU; uncertain significance
- V330 (= V344) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ M345) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (= R347) 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 (≠ T368) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (≠ T396) mutation to A: Markedly reduces amino acid transport activity.
- A382 (= A399) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (≠ F400) mutation to A: Complete loss of amino acid transport activity.
- Y386 (≠ V403) mutation to A: Loss of amino acid transport activity.
- K401 (≠ P415) to E: in CSNU; uncertain significance; dbSNP:rs760264924
- L426 (vs. gap) 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.
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, 76% coverage: 14:376/475 of query aligns to 1:346/469 of P46349
- G33 (≠ L46) mutation to D: Lack of activity.
- G42 (= G55) mutation to S: Lack of activity.
- G301 (≠ F334) mutation to V: Lack of activity.
- G338 (≠ T368) mutation to E: Lack of activity.
- F341 (= F371) 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)
23% identity, 92% coverage: 31:466/475 of query aligns to 7:425/458 of 6li9B
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)
24% identity, 85% coverage: 62:466/475 of query aligns to 83:467/501 of Q9UPY5
- C86 (≠ A65) 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 (≠ Y113) binding ; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (≠ W134) 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 (≠ N186) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ L192) 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 (= K193) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
- Y244 (≠ F243) binding
- F254 (≠ T253) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ I270) 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 (≠ T329) 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 (= F336) 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 (≠ A399) 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 (≠ E414) 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 (= C437) 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)
24% identity, 85% coverage: 63:466/475 of query aligns to 40:423/453 of 7epzB
Sites not aligning to the query:
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
24% identity, 85% coverage: 63:466/475 of query aligns to 40:423/455 of 7p9uB
7nf6B Ovine b0,+at-rbat heterodimer (see paper)
25% identity, 91% coverage: 35:466/475 of query aligns to 12:426/455 of 7nf6B
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
23% identity, 77% coverage: 10:374/475 of query aligns to 4:358/489 of P25737
- Y102 (≠ L109) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ Y113) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (≠ E181) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F243) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (≠ D249) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E257) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ A294) 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 (≠ G297) 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.
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, 82% coverage: 35:425/475 of query aligns to 49:423/531 of Q9QXW9
- Y130 (= Y113) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (≠ V116) 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 (= F243) 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)
29% identity, 47% coverage: 243:465/475 of query aligns to 248:470/503 of Q7YQK4
- C331 (≠ L327) mutation to S: No significant effect on inhibition by HgCl(2). Increased KM and Vmax for Phe.
- C377 (≠ A373) mutation to S: No significant effect on inhibition by HgCl(2).
- C403 (≠ A402) mutation to S: No significant effect on inhibition by HgCl(2).
- C439 (= C437) mutation to S: Prevents insertion into the plasma membrane and possibly protein folding.
- C454 (≠ T448) mutation to S: No significant effect on inhibition by HgCl(2). Slightly increased KM but slightly decreased Vmax for Phe.
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.
- 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)
29% identity, 47% coverage: 243:465/475 of query aligns to 202:424/457 of 6irtB
Sites not aligning to the query:
7dsqB Overall structure of the lat1-4f2hc bound with 3,5-diiodo-l-tyrosine (see paper)
29% identity, 47% coverage: 243:465/475 of query aligns to 209:431/464 of 7dsqB
Sites not aligning to the query:
7dsnB Overall structure of the lat1-4f2hc bound with jx-119 (see paper)
29% identity, 47% coverage: 243:465/475 of query aligns to 209:431/464 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)
29% identity, 47% coverage: 243:465/475 of query aligns to 209:431/464 of 7dslB
Sites not aligning to the query:
Query Sequence
>WP_057509036.1 NCBI__GCF_001431535.1:WP_057509036.1
MSLLRRKSLDTVTVHEAGRQLVRTLSWPHLIALGIGAIVGTGIYTLIGVGANLAGPAVLI
SFAIAGAVCACAALSYAELATMMPASGSAYTYSYTALGEIFAWVVGWSLILEYSLVVSTV
AVGWSGYFVGFLEWVNSQMGIDIRLPLALSAGPHVEGGVFNLPAVLITWLVAGGLMLGTK
ESATLNAVLVVLKLIALGVFIAVALPAFDSANLQPFMPYGFAKSLGPDGLERGVMAAAAI
IFFAFYGFDAIATAAEETKNPGRDLSIGIIGSMVGCTIVYMLVALAAVGAMSYAVFGSSA
EPLALIMRQLGHPTAALIIGVVAIVALPTVLLAFMFGQSRVFFVMGRDGMLPRRLSNVSK
RTGTPVATTLFSALLVSALAGVARLDEIAALANAGTLAAFTAVGVCLVVMRRREPDRART
FRTPLAWIVGPAAALGCVYLFFSLPHSTQLYFLIWNVIGLAVYFLYSRRNAVLGR
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