SitesBLAST
Comparing N515DRAFT_0606 FitnessBrowser__Dyella79:N515DRAFT_0606 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)
47% identity, 98% coverage: 7:475/477 of query aligns to 1:456/456 of 5oqtA
- binding alanine: I38 (= I43), G40 (= G45), T41 (≠ V46), G42 (= G47), F226 (= F245), A227 (= A246), I229 (≠ F248)
- binding : E24 (≠ V29), G26 (= G31), F28 (≠ W33), D29 (≠ Q34), M32 (≠ A37), A176 (= A184), R177 (= R185), A184 (= A192), A188 (= A196), L192 (= L200), Q294 (≠ L313), V297 (= V316)
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
46% identity, 99% coverage: 6:475/477 of query aligns to 2:458/458 of 6f34A
- binding arginine: I40 (= I43), G42 (= G45), T43 (≠ V46), G44 (= G47), E115 (= E118), Y116 (= Y119), A119 (≠ I122), F228 (= F245), A229 (= A246), I231 (≠ F248), V314 (= V331)
- binding cholesterol: W201 (≠ F207), Y202 (= Y208)
- binding : G28 (= G31), F30 (≠ W33), D31 (≠ Q34), M34 (≠ A37), A178 (= A184), R179 (= R185), A186 (= A192), I187 (= I193), A190 (= A196), L194 (= L200), Q296 (≠ L313), V299 (= V316)
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)
32% identity, 88% coverage: 1:418/477 of query aligns to 7:439/629 of P30825
- N226 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
27% identity, 86% coverage: 27:435/477 of query aligns to 2:392/433 of 6f2wA
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)
28% identity, 87% coverage: 27:442/477 of query aligns to 36:437/531 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 (≠ I122) 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 (= F245) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
29% identity, 89% coverage: 22:444/477 of query aligns to 4:406/438 of O34739
- C94 (≠ I111) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ S173) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ L200) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ L328) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-415.
Sites not aligning to the query:
- 415 C→S: Retains 25% of the transport activity; when associated with S-94; S-141; S-168 and S-291.
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)
27% identity, 91% coverage: 9:442/477 of query aligns to 6:438/535 of Q9UHI5
- I53 (= I43) binding
- 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 (≠ I122) 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 (≠ W148) modified: Interchain (with C-210 in SLC3A2)
- W174 (≠ A174) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (= F245) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ F248) 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 (= V304) to I: found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity
- N395 (≠ S399) binding ; mutation to Q: Strongly reduces L-leucine uptake activity. Strongly reduces L-tryptophan uptake activity.
- Y396 (≠ A400) mutation to A: Strongly reduces L-leucine uptake activity.
- T402 (≠ I404) to M: found in a patient with age-related hearing loss; strongly decreased L-alanine transport activity. Decreases L-tyrosine transport activity
- R418 (= R420) to C: found in a patient with age-related hearing loss; decreases L-alanine transport activity. Decreases L-tyrosine transport activity
Sites not aligning to the query:
- 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
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
28% identity, 86% coverage: 31:442/477 of query aligns to 1:398/458 of 7cmiB
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
28% identity, 86% coverage: 31:442/477 of query aligns to 1:398/458 of 7cmhB
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
28% identity, 86% coverage: 31:442/477 of query aligns to 1:398/457 of 7b00A
Sites not aligning to the query:
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
24% identity, 95% coverage: 23:473/477 of query aligns to 15:446/461 of P76037
- Y110 (= Y119) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
7epzB Overall structure of erastin-bound xct-4f2hc complex (see paper)
26% identity, 75% coverage: 70:426/477 of query aligns to 41:381/453 of 7epzB
Sites not aligning to the query:
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
26% identity, 75% coverage: 70:426/477 of query aligns to 41:381/455 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, 75% coverage: 70:426/477 of query aligns to 85:425/501 of Q9UPY5
- C86 (≠ A71) 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 (≠ Y119) binding ; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (≠ V143) 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 (≠ N187) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ I193) 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 (= K194) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
- Y244 (≠ F245) binding
- F254 (≠ T255) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ L272) 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 (≠ L328) 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 (≠ L337) 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 (≠ K391) 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 (≠ K415) 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:
- 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.
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, 96% coverage: 9:465/477 of query aligns to 9:452/487 of P82251
- V40 (≠ I40) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ IIGVG 43:47) binding
- I44 (= I44) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (≠ G53) to F: in CSNU; uncertain significance
- P52 (≠ Q54) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (vs. gap) 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 (≠ L121) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (≠ I141) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ V143) modified: Interchain (with C-114 in SLC3A1)
- V170 (≠ T180) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (= A192) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (= G205) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ F245) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (= A246) 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 (≠ Y250) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ T252) mutation to A: Reduces amino acid transport activity.
- G259 (≠ S274) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ G276) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (≠ D301) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ M336) mutation to S: Does not affect amino acid transport activity.
- A324 (= A339) to E: in CSNU; uncertain significance
- V330 (≠ A345) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ L346) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (= R348) 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 (≠ P369) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (≠ V397) mutation to A: Markedly reduces amino acid transport activity.
- A382 (= A400) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (≠ F401) mutation to A: Complete loss of amino acid transport activity.
- Y386 (≠ I404) mutation to A: Loss of amino acid transport activity.
- K401 (≠ P416) to E: in CSNU; uncertain significance; dbSNP:rs760264924
- L426 (≠ A443) 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.
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)
27% identity, 91% coverage: 18:449/477 of query aligns to 38:454/507 of Q01650
- Y117 (= Y96) mutation to A: Strongly decreased leucine transport activity.
- C164 (≠ L145) modified: Interchain (with C-210 in SLC3A2)
- D223 (≠ N213) to V: in dbSNP:rs17853937
- N230 (≠ H230) to K: in dbSNP:rs1060250
- A246 (= A246) mutation to V: Nearly abolishes leucine transport activity.
- F252 (vs. gap) mutation to A: Nearly abolishes leucine transport activity.
- W257 (≠ Y250) mutation to A: Nearly abolishes leucine transport activity.
- N258 (≠ D251) mutation to A: Decreased leucine transport activity.; mutation to D: Nearly abolishes leucine transport activity.
- Y259 (≠ T252) mutation to A: Strongly decreased leucine transport activity.
- E303 (≠ D301) mutation to K: Decreased leucine transport activity.
- P375 (≠ R368) 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)
27% identity, 89% coverage: 27:449/477 of query aligns to 4:411/464 of 7dsqB
7dsnB Overall structure of the lat1-4f2hc bound with jx-119 (see paper)
27% identity, 89% coverage: 27:449/477 of query aligns to 4:411/464 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 (≠ G42), I20 (= I43), G22 (= G45), S23 (≠ V46), G24 (= G47), I97 (≠ E118), I104 (≠ V125), F209 (vs. gap), A210 (vs. gap), G212 (vs. gap), I354 (= I395), N361 (≠ I402)
- binding cholesterol hemisuccinate: F109 (≠ W130), Y145 (≠ F178), K148 (≠ E181), V153 (≠ F186), Q326 (≠ R362)
Sites not aligning to the query:
7dslB Overall structure of the lat1-4f2hc bound with jx-078 (see paper)
27% identity, 89% coverage: 27:449/477 of query aligns to 4:411/464 of 7dslB
7dskB Overall structure of the lat1-4f2hc bound with jx-075 (see paper)
27% identity, 89% coverage: 27:449/477 of query aligns to 4:411/464 of 7dskB
- binding (2~{S})-2-azanyl-7-(naphthalen-1-ylmethoxy)-3,4-dihydro-1~{H}-naphthalene-2-carboxylic acid: T19 (≠ G42), I20 (= I43), S23 (≠ V46), G24 (= G47), I97 (≠ E118), S100 (≠ L121), S101 (≠ I122), F209 (vs. gap), G212 (vs. gap), Y216 (≠ T252), V353 (= V389), I354 (= I395), N361 (≠ I402)
- binding cholesterol hemisuccinate: K148 (≠ E181), A149 (≠ W182), V153 (≠ F186), F157 (≠ V190), H324 (= H360)
Sites not aligning to the query:
Query Sequence
>N515DRAFT_0606 FitnessBrowser__Dyella79:N515DRAFT_0606
MSVVSKLVRHKSVEQLQADVGKRGDFRRVLGLWQLTAIGIGGIIGVGVFVLAGQQAALNA
GPAVAISFLIAGIASAAAALCYAEFAGLIPVTGSAYTYGYAVLGELAAWLIGWDLLLEYA
LIVAVVAIGWSGYVQSALASIGVDLPVWAKGAIGTGEGHVFNVVAALVTLGVSALLIFRT
EWGARFNTFVVAIKVAAVALVIGVGAFYVKPENWVPFIPERIVGSDGVGHFGFQGVATAA
AVVFFAVFGYDTLTTAAEESKNPQRDLPRAVLLSLGISMAMYLAVSMVLTGIAHYTTLKT
DAPVADAFKGLGLHWVALTVSVSAVFGLISVLFAFMLGATRIWFALARDGLLPGWFAKPH
PRYGTPHRPTIVLGVFTALVAGLLPIEEVAKLVNIGVLSAFIVICSSVLILRKRKPDLYR
AFRTPLVPLIPLVGIGFSIWLLAELPWVTWEVFLIWVSIGLVVYFGYGIRHSKLEKA
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