SitesBLAST
Comparing WP_025763755.1 NCBI__GCF_000566685.1:WP_025763755.1 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)
40% identity, 99% coverage: 6:559/561 of query aligns to 2:457/458 of 6f34A
- binding arginine: I40 (= I44), G42 (= G46), T43 (≠ A47), G44 (= G48), E115 (= E118), Y116 (= Y119), A119 (≠ S122), F228 (= F268), A229 (= A269), I231 (= I271), V314 (≠ A354)
- binding cholesterol: W201 (≠ F241), Y202 (= Y242)
- binding : G28 (= G32), F30 (≠ R34), D31 (= D35), M34 (≠ S38), A178 (≠ R218), R179 (≠ T219), A186 (≠ V226), I187 (≠ L227), A190 (≠ G230), L194 (= L234), Q296 (≠ L336), V299 (≠ M339)
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
40% identity, 99% coverage: 7:559/561 of query aligns to 1:455/456 of 5oqtA
- binding alanine: I38 (= I44), G40 (= G46), T41 (≠ A47), G42 (= G48), F226 (= F268), A227 (= A269), I229 (= I271)
- binding : E24 (≠ V30), G26 (= G32), F28 (≠ R34), D29 (= D35), M32 (≠ S38), A176 (≠ R218), R177 (≠ T219), A184 (≠ V226), A188 (≠ G230), L192 (= L234), Q294 (≠ L336), V297 (≠ M339)
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)
31% identity, 55% coverage: 251:561/561 of query aligns to 247:612/629 of P30825
Sites not aligning to the query:
- 226 modified: carbohydrate, N-linked (GlcNAc...) asparagine
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)
23% identity, 73% coverage: 1:407/561 of query aligns to 7:369/531 of Q9QXW9
- Y130 (= Y119) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (≠ S122) 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 (= F268) 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)
25% identity, 74% coverage: 9:424/561 of query aligns to 23:398/503 of Q7YQK4
- C88 (≠ A74) 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 (≠ S81) 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 (≠ M151) mutation to S: No change to KM or Vmax for Phe.
- C172 (≠ K162) mutation to S: No change to KM or Vmax for Phe.
- C174 (≠ Q164) mutation to S: No change to KM or Vmax for Phe.
- C183 (≠ S173) 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 (= G230) mutation to D: Decreased KM and Vmax for Trp. Increased KM and Vmax for Phe; when associated with L-234.
- W234 (= W248) 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 (≠ I351) mutation to S: No significant effect on inhibition by HgCl(2). Increased KM and Vmax for Phe.
- C377 (≠ V400) mutation to S: No significant effect on inhibition by HgCl(2).
Sites not aligning to the query:
- 403 C→S: No significant effect on inhibition by HgCl(2).
- 439 C→S: Prevents insertion into the plasma membrane and possibly protein folding.
- 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.
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
28% identity, 30% coverage: 259:427/561 of query aligns to 207:377/461 of P76037
Sites not aligning to the query:
- 110 Y→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)
20% identity, 80% coverage: 4:450/561 of query aligns to 3:412/487 of P82251
- V40 (≠ I41) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ IVGAG 44:48) binding L-arginine
- I44 (≠ V45) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (≠ T52) to F: in CSNU; uncertain significance
- P52 (≠ I53) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (≠ T71) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y98) to H: in CSNU; uncertain significance
- G105 (= G104) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W113) to R: in CSNU; uncertain significance
- I120 (≠ E118) to L: in CSNU; uncertain significance
- T123 (≠ V121) 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 (≠ M151) modified: Interchain (with C-114 in SLC3A1)
- V170 (≠ I214) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ V226) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (= G239) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ F268) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (= A269) 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 L-arginine; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ F273) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ S275) mutation to A: Reduces amino acid transport activity.
- G259 (≠ C297) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ I299) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (≠ N324) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ A350) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ S353) to E: in CSNU; uncertain significance
- V330 (≠ Q359) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ L360) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (= R371) 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 (= A392) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (= S417) mutation to A: Markedly reduces amino acid transport activity.
- A382 (≠ T420) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (≠ F421) mutation to A: Complete loss of amino acid transport activity.
- Y386 (≠ F424) mutation to A: Loss of amino acid transport activity.
- K401 (≠ L439) 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.
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)
24% identity, 69% coverage: 19:407/561 of query aligns to 26:370/535 of Q9UHI5
- I53 (= I44) binding L-leucine
- Y93 (= Y82) 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 (≠ S122) Important for substrate specificity; binding L-tryptophan; 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 (≠ H144) modified: Interchain (with C-210 in SLC3A2)
- W174 (≠ A170) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (= F268) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ I271) Important for substrate specificity; binding L-leucine; 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 (≠ L327) to I: found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity; dbSNP:rs142951280
Sites not aligning to the query:
- 395 binding L-tryptophan; N→Q: Strongly reduces L-leucine uptake activity. Strongly reduces L-tryptophan uptake activity.
- 396 Y→A: Strongly reduces L-leucine uptake activity.
- 402 T → M: found in a patient with age-related hearing loss; strongly decreased L-alanine transport activity. Decreases L-tyrosine transport activity; dbSNP:rs758342760
- 418 R → C: found in a patient with age-related hearing loss; decreases L-alanine transport activity. Decreases L-tyrosine transport activity; dbSNP:rs146946494
- 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
7epzB Overall structure of erastin-bound xct-4f2hc complex (see paper)
21% identity, 66% coverage: 76:448/561 of query aligns to 47:380/453 of 7epzB
Sites not aligning to the query:
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
21% identity, 66% coverage: 76:448/561 of query aligns to 47:380/455 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)
22% identity, 66% coverage: 76:448/561 of query aligns to 91:424/501 of Q9UPY5
- R135 (≠ Y119) binding L-glutamate; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (≠ S161) 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 (≠ G213) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ L227) 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 (= K228) 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 (≠ T278) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ I295) 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 (≠ I351) 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 (≠ L360) 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 (vs. gap) 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 (≠ G438) 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.
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.
- 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.
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
24% identity, 65% coverage: 41:407/561 of query aligns to 10:330/458 of 7cmiB