SitesBLAST
Comparing N515DRAFT_4009 FitnessBrowser__Dyella79:N515DRAFT_4009 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
33% identity, 96% coverage: 10:435/445 of query aligns to 1:431/433 of 6f2wA
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
31% identity, 97% coverage: 3:433/445 of query aligns to 2:434/438 of O34739
- C94 (≠ F95) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ A142) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ V169) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ F293) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
- C415 (≠ A414) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.
6li9B Heteromeric amino acid transporter b0,+at-rbat complex bound with arginine (see paper)
32% identity, 88% coverage: 21:411/445 of query aligns to 9:404/458 of 6li9B
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)
32% identity, 88% coverage: 21:411/445 of query aligns to 38:433/487 of P82251
- V40 (= V23) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ IIGGG 26:30) binding
- I44 (= I27) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (≠ N34) to F: in CSNU; uncertain significance
- P52 (= P35) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (≠ V53) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y82) to H: in CSNU; uncertain significance
- G105 (= G88) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W97) to R: in CSNU; uncertain significance
- I120 (= I103) to L: in CSNU; uncertain significance
- T123 (≠ G106) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (≠ L125) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (vs. gap) modified: Interchain (with C-114 in SLC3A1)
- V170 (≠ L149) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ L161) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (= G174) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ A200) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (= A201) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (≠ V204) to D: in CSNU; decreased amino acid transport activity
- W230 (≠ F206) to R: in CSNU; complete loss of amino acid transport activity; mutation to A: Abolishes amino acid transport activity.
- D233 (≠ S209) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ F211) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ Y213) mutation to A: Reduces amino acid transport activity.
- G259 (= G235) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ L237) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (= S262) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ L298) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ G301) to E: in CSNU; uncertain significance
- V330 (= V307) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ M308) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (≠ D310) 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 (= A331) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (≠ T356) mutation to A: Markedly reduces amino acid transport activity.
- A382 (≠ D359) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (= W360) mutation to A: Complete loss of amino acid transport activity.
- Y386 (≠ C363) mutation to A: Loss of amino acid transport activity.
- K401 (≠ D377) to E: in CSNU; uncertain significance; dbSNP:rs760264924
- L426 (≠ V404) 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.
7nf6B Ovine b0,+at-rbat heterodimer (see paper)
31% identity, 88% coverage: 21:411/445 of query aligns to 10:405/455 of 7nf6B
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)
31% identity, 93% coverage: 17:428/445 of query aligns to 44:463/535 of Q9UHI5
- I53 (= I26) binding
- Y93 (= Y66) 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 (≠ S107) Important for substrate specificity; binding ; 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 (≠ T129) modified: Interchain (with C-210 in SLC3A2)
- W174 (vs. gap) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (= F206) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ S209) Important for substrate specificity; binding ; 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 (≠ P265) to I: found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity
- N395 (≠ D359) binding ; mutation to Q: Strongly reduces L-leucine uptake activity. Strongly reduces L-tryptophan uptake activity.
- Y396 (≠ W360) mutation to A: Strongly reduces L-leucine uptake activity.
- T402 (vs. gap) to M: found in a patient with age-related hearing loss; strongly decreased L-alanine transport activity. Decreases L-tyrosine transport activity
- R418 (≠ G379) to C: found in a patient with age-related hearing loss; decreases L-alanine transport activity. Decreases L-tyrosine transport activity
- V460 (≠ I425) to 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
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
32% identity, 93% coverage: 17:428/445 of query aligns to 4:423/458 of 7cmiB
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
32% identity, 93% coverage: 17:428/445 of query aligns to 4:423/458 of 7cmhB
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
32% identity, 93% coverage: 17:428/445 of query aligns to 4:423/457 of 7b00A
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)
30% identity, 93% coverage: 17:428/445 of query aligns to 43:462/531 of Q9QXW9
- Y130 (= Y104) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (≠ S107) 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 (= F206) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
7dsqB Overall structure of the lat1-4f2hc bound with 3,5-diiodo-l-tyrosine (see paper)
30% identity, 96% coverage: 10:437/445 of query aligns to 4:440/464 of 7dsqB
7dsnB Overall structure of the lat1-4f2hc bound with jx-119 (see paper)
30% identity, 96% coverage: 10:437/445 of query aligns to 4:440/464 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 (≠ G25), I20 (= I26), G22 (= G28), S23 (≠ G29), G24 (= G30), I97 (= I103), I104 (≠ A110), F209 (= F206), A210 (= A207), G212 (≠ S209), I354 (≠ L352), N361 (≠ D359)
- binding cholesterol hemisuccinate: F109 (= F115), Y145 (≠ F147), K148 (= K150), V153 (= V155), Q326 (≠ R324)
Sites not aligning to the query:
7dslB Overall structure of the lat1-4f2hc bound with jx-078 (see paper)
30% identity, 96% coverage: 10:437/445 of query aligns to 4:440/464 of 7dslB
7dskB Overall structure of the lat1-4f2hc bound with jx-075 (see paper)
30% identity, 96% coverage: 10:437/445 of query aligns to 4:440/464 of 7dskB
- binding (2~{S})-2-azanyl-7-(naphthalen-1-ylmethoxy)-3,4-dihydro-1~{H}-naphthalene-2-carboxylic acid: T19 (≠ G25), I20 (= I26), S23 (≠ G29), G24 (= G30), I97 (= I103), S100 (≠ G106), S101 (= S107), F209 (= F206), G212 (≠ S209), Y216 (= Y213), V353 (≠ L351), I354 (≠ L352), N361 (≠ D359)
- binding cholesterol hemisuccinate: K148 (= K150), A149 (≠ L151), V153 (= V155), F157 (= F159), H324 (= H322)
Sites not aligning to the query:
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, 96% coverage: 10:436/445 of query aligns to 47:482/507 of Q01650
- Y117 (= Y80) mutation to A: Strongly decreased leucine transport activity.
- C164 (≠ F123) modified: Interchain (with C-210 in SLC3A2)
- D223 (≠ G182) to V: in dbSNP:rs17853937
- N230 (= N194) to K: in dbSNP:rs1060250
- A246 (vs. gap) mutation to V: Nearly abolishes leucine transport activity.
- F252 (= F206) mutation to A: Nearly abolishes leucine transport activity.
- W257 (≠ F211) mutation to A: Nearly abolishes leucine transport activity.
- N258 (≠ T212) mutation to A: Decreased leucine transport activity.; mutation to D: Nearly abolishes leucine transport activity.
- Y259 (= Y213) mutation to A: Strongly decreased leucine transport activity.
- E303 (≠ D257) mutation to K: Decreased leucine transport activity.
- P375 (≠ V330) mutation to L: Nearly abolishes leucine transport activity.
Sites not aligning to the query:
- 483:507 mutation Missing: Nearly abolishes leucine transport activity.
6irtB Human lat1-4f2hc complex bound with bch (see paper)
30% identity, 94% coverage: 21:437/445 of query aligns to 8:433/457 of 6irtB
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)
30% identity, 96% coverage: 10:437/445 of query aligns to 43:479/503 of Q7YQK4
- C88 (≠ A55) 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 (= C65) 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 (vs. gap) mutation to S: No change to KM or Vmax for Phe.
- C172 (≠ A135) mutation to S: No change to KM or Vmax for Phe.
- C174 (≠ A137) mutation to S: No change to KM or Vmax for Phe.
- C183 (≠ L146) 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 (= G182) mutation to D: Decreased KM and Vmax for Trp. Increased KM and Vmax for Phe; when associated with L-234.
- W234 (≠ G193) 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 (≠ T290) mutation to S: No significant effect on inhibition by HgCl(2). Increased KM and Vmax for Phe.
- C377 (≠ S336) mutation to S: No significant effect on inhibition by HgCl(2).
- C403 (≠ A362) mutation to S: No significant effect on inhibition by HgCl(2).
- C439 (≠ V399) mutation to S: Prevents insertion into the plasma membrane and possibly protein folding.
- C454 (≠ A414) 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:
- 492 C→S: No significant effect on inhibition by HgCl(2). Slightly decreased KM and Vmax for Phe.
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
28% identity, 90% coverage: 34:433/445 of query aligns to 21:428/455 of 7p9uB
7epzB Overall structure of erastin-bound xct-4f2hc complex (see paper)
28% identity, 90% coverage: 34:433/445 of query aligns to 21:428/453 of 7epzB
Sites not aligning to the query:
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)
28% identity, 90% coverage: 34:433/445 of query aligns to 65:472/501 of Q9UPY5
- C86 (≠ A55) 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 (≠ Y104) binding ; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (vs. gap) 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 (= Q156) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ L162) 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 (= K163) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
- Y244 (≠ F206) binding
- F254 (≠ N216) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ F233) 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 (≠ T290) 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 (≠ V299) 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 (≠ D359) 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 (vs. gap) 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 (≠ V399) 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.
Query Sequence
>N515DRAFT_4009 FitnessBrowser__Dyella79:N515DRAFT_4009
MSDTPASGYMRRLTSWDAAMIVVGGIIGGGIFLNPGIAAQRTESGLALLLVWVGAGVLTL
IGALCYAELGARRPHAGGSYVYLREAFGSLAGFLFGWTMLLVIYSGSAAAVATIFASYAS
GVFGLPPGTIKPLAAGALVFVAGINLFGLKLGAQVQNLFTLLKLLAVAVLVVCGLFLAGA
DGAGVLASDPARGNVGFIGAALPVLFAYSGFTYLNNLAGEVREPQRTLPRALFFGMLAVI
VVYALVNVAYLAVLGHDGLARSNTPAADVMSRVFGPIGAKVIAIGIAVSTLGFCNITLVA
GARVLQVMGDDGLFFRNVARLHPRHRTPNVALLLLSGWAVFLAMAFNFGQLLDYATFGDW
LACAVGVVTIFWYRSRDKGGADFRVPGYPVLPLIFVGVVGWIVVATLLAKPIQACIVLAV
MAVGIPVFHVWRRMFPASALPSQSP
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