SitesBLAST
Comparing CA265_RS15000 FitnessBrowser__Pedo557:CA265_RS15000 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)
43% identity, 99% coverage: 3:488/491 of query aligns to 1:456/456 of 5oqtA
- binding alanine: I38 (= I40), G40 (= G42), T41 (≠ A43), G42 (= G44), F226 (= F253), A227 (= A254), I229 (= I256)
- binding : E24 (≠ T26), G26 (≠ S28), F28 (≠ G30), D29 (≠ A31), M32 (≠ A34), A176 (= A188), R177 (≠ F189), A184 (≠ I196), A188 (≠ G200), L192 (= L204), Q294 (≠ E321), V297 (≠ L329)
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
43% identity, 99% coverage: 1:488/491 of query aligns to 1:458/458 of 6f34A
- binding arginine: I40 (= I40), G42 (= G42), T43 (≠ A43), G44 (= G44), E115 (= E115), Y116 (= Y116), A119 (≠ G119), F228 (= F253), A229 (= A254), I231 (= I256), V314 (= V344)
- binding cholesterol: W201 (≠ G211), Y202 (≠ F212)
- binding : G28 (≠ S28), F30 (≠ G30), D31 (≠ A31), M34 (≠ A34), A178 (= A188), R179 (≠ F189), A186 (≠ I196), I187 (≠ T197), A190 (≠ G200), L194 (= L204), Q296 (≠ E321), 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)
33% identity, 86% coverage: 23:444/491 of query aligns to 28:452/629 of P30825
- N226 (≠ H219) modified: carbohydrate, N-linked (GlcNAc...) asparagine
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
25% identity, 95% coverage: 21:485/491 of query aligns to 6:437/438 of O34739
- C94 (≠ I108) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ S177) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ L204) 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.
- C415 (= C451) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
26% identity, 84% coverage: 37:449/491 of query aligns to 14:393/433 of 6f2wA
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
23% identity, 94% coverage: 13:473/491 of query aligns to 7:434/461 of P76037
- Y110 (= Y116) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
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)
26% identity, 90% coverage: 16:455/491 of query aligns to 38:447/507 of Q01650
- Y117 (= Y93) mutation to A: Strongly decreased leucine transport activity.
- C164 (= C149) modified: Interchain (with C-210 in SLC3A2)
- D223 (≠ N214) to V: in dbSNP:rs17853937
- N230 (≠ Y221) to K: in dbSNP:rs1060250
- A246 (= A247) mutation to V: Nearly abolishes leucine transport activity.
- F252 (= F253) mutation to A: Nearly abolishes leucine transport activity.
- W257 (≠ F258) mutation to A: Nearly abolishes leucine transport activity.
- N258 (≠ D259) mutation to A: Decreased leucine transport activity.; mutation to D: Nearly abolishes leucine transport activity.
- Y259 (≠ A260) mutation to A: Strongly decreased leucine transport activity.
- E303 (≠ K309) mutation to K: Decreased leucine transport activity.
- P375 (≠ K381) mutation to L: Nearly abolishes leucine transport activity.
Sites not aligning to the query:
- 483:507 mutation Missing: Nearly abolishes leucine transport activity.
7dsqB Overall structure of the lat1-4f2hc bound with 3,5-diiodo-l-tyrosine (see paper)
26% identity, 88% coverage: 23:455/491 of query aligns to 3:404/464 of 7dsqB
7dsnB Overall structure of the lat1-4f2hc bound with jx-119 (see paper)
26% identity, 88% coverage: 23:455/491 of query aligns to 3:404/464 of 7dsnB
- binding (2~{S})-2-azanyl-7-[[2-(1,3-benzoxazol-2-yl)phenyl]methoxy]-3,4-dihydro-1~{H}-naphthalene-2-carboxylic acid: T19 (≠ A39), I20 (= I40), G22 (= G42), S23 (≠ A43), G24 (= G44), I97 (≠ E115), I104 (≠ T122), F209 (= F253), A210 (= A254), G212 (≠ I256), I354 (≠ G409), N361 (vs. gap)
- binding cholesterol hemisuccinate: F109 (≠ W127), Y145 (≠ V173), K148 (≠ L176), V153 (≠ I181), Q326 (≠ K375)
Sites not aligning to the query:
7dslB Overall structure of the lat1-4f2hc bound with jx-078 (see paper)
26% identity, 88% coverage: 23:455/491 of query aligns to 3:404/464 of 7dslB
7dskB Overall structure of the lat1-4f2hc bound with jx-075 (see paper)
26% identity, 88% coverage: 23:455/491 of query aligns to 3:404/464 of 7dskB
- binding (2~{S})-2-azanyl-7-(naphthalen-1-ylmethoxy)-3,4-dihydro-1~{H}-naphthalene-2-carboxylic acid: T19 (≠ A39), I20 (= I40), S23 (≠ A43), G24 (= G44), I97 (≠ E115), S100 (≠ V118), S101 (≠ G119), F209 (= F253), G212 (≠ I256), Y216 (≠ A260), V353 (≠ I408), I354 (≠ G409), N361 (vs. gap)
- binding cholesterol hemisuccinate: K148 (≠ L176), A149 (≠ S177), V153 (≠ I181), F157 (≠ S185), H324 (= H373)
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)
24% identity, 97% coverage: 2:478/491 of query aligns to 5:452/487 of P82251
- V40 (= V37) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ IIGAG 40:44) binding
- I44 (= I41) 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 (= A68) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y95) to H: in CSNU; uncertain significance
- G105 (= G101) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W110) to R: in CSNU; uncertain significance
- I120 (≠ E115) to L: in CSNU; uncertain significance
- T123 (≠ V118) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (≠ E147) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (= C149) modified: Interchain (with C-114 in SLC3A1)
- V170 (≠ L180) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ I196) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (= G209) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ T250) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (≠ V251) 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 (≠ I256) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ F258) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ A260) mutation to A: Reduces amino acid transport activity.
- G259 (≠ S282) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ A284) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (≠ T308) 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 (≠ K361) 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 (= A382) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (≠ A413) mutation to A: Markedly reduces amino acid transport activity.
- A382 (vs. gap) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (vs. gap) mutation to A: Complete loss of amino acid transport activity.
- Y386 (vs. gap) mutation to A: Loss of amino acid transport activity.
- K401 (≠ P429) to E: in CSNU; uncertain significance; dbSNP:rs760264924
- L426 (= L456) 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.
6irtB Human lat1-4f2hc complex bound with bch (see paper)
26% identity, 86% coverage: 33:455/491 of query aligns to 6:397/457 of 6irtB
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
26% identity, 82% coverage: 55:455/491 of query aligns to 27:395/455 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, 82% coverage: 55:455/491 of query aligns to 71:439/501 of Q9UPY5
- C86 (≠ A68) 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 (≠ Y116) binding ; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (= C149) 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 (≠ N191) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ T197) 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 (= K198) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
- Y244 (≠ I245) binding
- F254 (= F255) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ L280) 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 (≠ G340) 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 (≠ L350) 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 (≠ D428) 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 (= C451) 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)
26% identity, 82% coverage: 55:455/491 of query aligns to 27:395/453 of 7epzB
Sites not aligning to the query:
6li9B Heteromeric amino acid transporter b0,+at-rbat complex bound with arginine (see paper)
24% identity, 91% coverage: 33:478/491 of query aligns to 7:423/458 of 6li9B
Q9URZ4 Cationic amino acid transporter 1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
22% identity, 84% coverage: 14:425/491 of query aligns to 71:466/587 of Q9URZ4
Sites not aligning to the query:
- 29 modified: Phosphoserine
- 30 modified: Phosphoserine
- 37 modified: Phosphoserine
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
23% identity, 97% coverage: 14:487/491 of query aligns to 4:475/489 of P25737
- Y102 (≠ L112) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ Y116) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (≠ V195) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F253) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (≠ D259) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E267) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ K309) 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 (≠ E312) 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 (≠ T461) mutation to A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D443 (vs. gap) mutation to A: Retains 11% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- D446 (≠ G468) mutation to A: Retains 13% of wild-type lysine uptake activity. Is unable to inhibit CadC.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
28% identity, 41% coverage: 253:455/491 of query aligns to 248:443/503 of Q7YQK4
- C331 (≠ S343) mutation to S: No significant effect on inhibition by HgCl(2). Increased KM and Vmax for Phe.
- C377 (≠ I388) mutation to S: No significant effect on inhibition by HgCl(2).
- C403 (= C418) 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.
Query Sequence
>CA265_RS15000 FitnessBrowser__Pedo557:CA265_RS15000
MGLFTKKPMHLLLEEAGDSGKGLKRTLSAGALVALGVGAIIGAGLFVRTAAAAAQNAGPS
VTIGFIIAAIGCALAGLCYAELSSSIPISGSAYTYTYATMGELMAWVIGWDLVLEYAVGA
ATVGIAWSEYLNKLLVEVLHTSPIPYEWCHSPFQSHPDGTVNGIMNLPALFIVGLLSLLL
IKGTSESAFVNGLIVITKVGIVILIIVLGWGFINESNHHPYIPAATTYVDHAGISHSFGG
FWGVIGAAGTVFFAFIGFDAVSTAAQETKNPKTAMPIGILGSLAVCTVLYILFAHVLTGI
APVEFFRTKGGEASVVAAISEYMTGYSWLSKLVTVAILAGFSSVILVMLLGQSRVFYSMS
KDGLLPKMFSDLHPKFKTPYKANLVILIIVGLFAAFIPGDVVGDMTSIGTLFAFMLVCVA
VIILRKTDPDLPRQFKTPWVPLIPILGVVACGLMILGLGWTNWLRLFGWLALGFIIYFGY
SKKNSHLKDVK
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