SitesBLAST
Comparing WP_038806034.1 NCBI__GCF_000382825.1:WP_038806034.1 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)
45% identity, 99% coverage: 1:462/465 of query aligns to 1:458/458 of 6f34A
- binding arginine: I40 (≠ M33), G42 (= G35), T43 (= T36), G44 (= G37), E115 (= E108), Y116 (≠ F109), A119 (= A112), F228 (= F231), A229 (≠ G232), I231 (≠ L234), V314 (= V317)
- binding cholesterol: W201 (= W197), Y202 (= Y198)
- binding : G28 (≠ K21), F30 (≠ W23), D31 (= D24), M34 (≠ L27), A178 (≠ L174), R179 (= R175), A186 (≠ V182), I187 (≠ L183), A190 (≠ S186), L194 (= L190), Q296 (≠ I299), V299 (≠ A302)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
45% identity, 99% coverage: 3:462/465 of query aligns to 1:456/456 of 5oqtA
- binding alanine: I38 (≠ M33), G40 (= G35), T41 (= T36), G42 (= G37), F226 (= F231), A227 (≠ G232), I229 (≠ L234)
- binding : E24 (≠ H19), G26 (≠ K21), F28 (≠ W23), D29 (= D24), M32 (≠ L27), A176 (≠ L174), R177 (= R175), A184 (≠ V182), A188 (≠ S186), L192 (= L190), Q294 (≠ I299), V297 (≠ A302)
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)
29% identity, 87% coverage: 1:405/465 of query aligns to 11:438/629 of P30825
- N226 (= N206) modified: carbohydrate, N-linked (GlcNAc...) asparagine
Q88CZ8 L-histidine transporter HutT from Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440) (see paper)
27% identity, 95% coverage: 10:449/465 of query aligns to 6:436/467 of Q88CZ8
- T27 (= T36) mutation T->A,S: Retains 60% of wild-type activity.; mutation to N: Retains 20% of wild-type activity.
- E98 (= E108) mutation to A: Retains 80% of wild-type activity.
- K156 (= K184) mutation K->A,Q: Retains less than 10% of wild-type activity.; mutation to R: Retains 40% of wild-type activity.
- F212 (= F231) mutation F->A,Q: Loss of activity.; mutation to Y: No change in activity.
- E218 (= E237) mutation E->A,Q: Loss of activity.; mutation to D: Retains 70% of wild-type activity.
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
25% identity, 80% coverage: 53:426/465 of query aligns to 31:392/455 of 7p9uB
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)
26% identity, 80% coverage: 53:426/465 of query aligns to 75:436/501 of Q9UPY5
- C86 (= C64) 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 (≠ M110) binding L-glutamate; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (≠ M135) 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 (≠ N177) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ L183) 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 (= K184) 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 L-glutamate
- F254 (≠ M241) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ V258) 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 (≠ V317) 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 (≠ Y323) 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 (≠ T383) 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 (≠ D400) 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, 80% coverage: 53:426/465 of query aligns to 31:392/453 of 7epzB
Sites not aligning to the query:
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
25% identity, 90% coverage: 16:435/465 of query aligns to 13:438/489 of P25737
- Y102 (≠ A122) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ Y131) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K184) 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 (= E237) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E245) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ N285) 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 (= D288) 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 (= E435) mutation to A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 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.
8j8mB Overall structure of the lat1-4f2hc bound with tryptophan
26% identity, 94% coverage: 16:452/465 of query aligns to 3:430/463 of 8j8mB
8j8lB Overall structure of the lat1-4f2hc bound with l-dopa
26% identity, 94% coverage: 16:452/465 of query aligns to 3:430/463 of 8j8lB
8xpuB Overall structure of the lat1-4f2hc bound with jph203 (see paper)
26% identity, 94% coverage: 16:452/465 of query aligns to 3:430/464 of 8xpuB