SitesBLAST
Comparing N515DRAFT_2925 FitnessBrowser__Dyella79:N515DRAFT_2925 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)
48% identity, 95% coverage: 21:477/480 of query aligns to 18:456/456 of 5oqtA
- binding alanine: I38 (≠ V41), G40 (= G43), T41 (= T44), G42 (= G45), F226 (= F246), A227 (= A247), I229 (= I249)
- binding : E24 (≠ T27), G26 (= G29), F28 (≠ W31), D29 (≠ G32), M32 (≠ A35), A176 (≠ S189), R177 (≠ G190), A184 (= A197), A188 (≠ G201), L192 (≠ V205), Q294 (≠ L315), V297 (≠ L318)
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
47% identity, 99% coverage: 4:477/480 of query aligns to 2:458/458 of 6f34A
- binding arginine: I40 (≠ V41), G42 (= G43), T43 (= T44), G44 (= G45), E115 (= E116), Y116 (= Y117), A119 (≠ S120), F228 (= F246), A229 (= A247), I231 (= I249), V314 (= V333)
- binding cholesterol: W201 (≠ R212), Y202 (= Y213)
- binding : G28 (= G29), F30 (≠ W31), D31 (≠ G32), M34 (≠ A35), A178 (≠ S189), R179 (≠ G190), A186 (= A197), I187 (≠ L198), A190 (≠ G201), L194 (≠ V205), Q296 (≠ L315), V299 (≠ L318)
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)
34% identity, 88% coverage: 3:423/480 of query aligns to 11:439/629 of P30825
- N226 (vs. gap) 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)
24% identity, 94% coverage: 13:465/480 of query aligns to 24:454/531 of Q9QXW9
- Y130 (= Y117) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (≠ S120) 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 (= F246) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
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, 93% coverage: 5:452/480 of query aligns to 27:452/507 of Q01650
- Y117 (= Y94) mutation to A: Strongly decreased leucine transport activity.
- C164 (≠ L143) modified: Interchain (with C-210 in SLC3A2)
- D223 (= D215) to V: in dbSNP:rs17853937
- N230 (≠ F222) to K: in dbSNP:rs1060250
- A246 (≠ G240) mutation to V: Nearly abolishes leucine transport activity.
- F252 (= F246) mutation to A: Nearly abolishes leucine transport activity.
- W257 (≠ F251) mutation to A: Nearly abolishes leucine transport activity.
- N258 (≠ E252) mutation to A: Decreased leucine transport activity.; mutation to D: Nearly abolishes leucine transport activity.
- Y259 (≠ A253) mutation to A: Strongly decreased leucine transport activity.
- E303 (vs. gap) mutation to K: Decreased leucine transport activity.
- P375 (≠ L370) mutation to L: Nearly abolishes leucine transport activity.
Sites not aligning to the query:
- 483:507 mutation Missing: Nearly abolishes leucine 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, 95% coverage: 9:465/480 of query aligns to 20:455/535 of Q9UHI5
- I53 (≠ V41) binding
- Y93 (= Y80) 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 (≠ S120) 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 (≠ A153) modified: Interchain (with C-210 in SLC3A2)
- W174 (= W179) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (= F246) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ I249) 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 (≠ P304) to I: found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity
- N395 (≠ T399) binding ; mutation to Q: Strongly reduces L-leucine uptake activity. Strongly reduces L-tryptophan uptake activity.
- Y396 (≠ L400) mutation to A: Strongly reduces L-leucine uptake activity.
- T402 (≠ V406) to M: found in a patient with age-related hearing loss; strongly decreased L-alanine transport activity. Decreases L-tyrosine transport activity
- R418 (= R422) 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
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
28% identity, 91% coverage: 32:467/480 of query aligns to 6:425/433 of 6f2wA
7dsqB Overall structure of the lat1-4f2hc bound with 3,5-diiodo-l-tyrosine (see paper)
27% identity, 90% coverage: 23:452/480 of query aligns to 2:409/464 of 7dsqB
7dsnB Overall structure of the lat1-4f2hc bound with jx-119 (see paper)
27% identity, 90% coverage: 23:452/480 of query aligns to 2:409/464 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 (≠ A40), I20 (≠ V41), G22 (= G43), S23 (≠ T44), G24 (= G45), I97 (≠ Y117), I104 (≠ V124), F209 (= F246), A210 (= A247), G212 (≠ I249), I354 (vs. gap), N361 (≠ T399)
- binding cholesterol hemisuccinate: F109 (≠ Y131), Y145 (= Y182), K148 (≠ R186), V153 (≠ L191), Q326 (≠ K364)
Sites not aligning to the query:
7dslB Overall structure of the lat1-4f2hc bound with jx-078 (see paper)
27% identity, 90% coverage: 23:452/480 of query aligns to 2:409/464 of 7dslB
7dskB Overall structure of the lat1-4f2hc bound with jx-075 (see paper)
27% identity, 90% coverage: 23:452/480 of query aligns to 2:409/464 of 7dskB
- binding (2~{S})-2-azanyl-7-(naphthalen-1-ylmethoxy)-3,4-dihydro-1~{H}-naphthalene-2-carboxylic acid: T19 (≠ A40), I20 (≠ V41), S23 (≠ T44), G24 (= G45), I97 (≠ Y117), S100 (= S120), S101 (≠ A121), F209 (= F246), G212 (≠ I249), Y216 (≠ A253), V353 (vs. gap), I354 (vs. gap), N361 (≠ T399)
- binding cholesterol hemisuccinate: K148 (≠ R186), A149 (≠ E187), V153 (≠ L191), F157 (≠ M195), H324 (= H362)
Sites not aligning to the query:
6irtB Human lat1-4f2hc complex bound with bch (see paper)
27% identity, 87% coverage: 35:452/480 of query aligns to 7:402/457 of 6irtB
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
26% identity, 82% coverage: 33:426/480 of query aligns to 3:382/458 of 7cmiB
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
26% identity, 82% coverage: 33:426/480 of query aligns to 3:382/458 of 7cmhB
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
25% identity, 82% coverage: 33:426/480 of query aligns to 3:382/457 of 7b00A
Sites not aligning to the query:
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
24% identity, 77% coverage: 71:441/480 of query aligns to 44:392/455 of 7p9uB
7epzB Overall structure of erastin-bound xct-4f2hc complex (see paper)
24% identity, 77% coverage: 71:441/480 of query aligns to 44:392/453 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)
24% identity, 74% coverage: 22:377/480 of query aligns to 11:358/489 of P25737
- Y102 (≠ M113) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ Y117) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (= K199) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F246) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (= E252) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E260) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ V305) 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 (≠ A308) 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.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 438 E→A: Retains 14% of wild-type lysine uptake activity. Is unable to inhibit CadC.
- 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.
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)
24% identity, 77% coverage: 71:441/480 of query aligns to 88:436/501 of Q9UPY5
- R135 (≠ G118) binding ; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (≠ I141) 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 (≠ N192) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ L198) 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 (= K199) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
- Y244 (≠ F246) binding
- F254 (≠ T256) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ L273) 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 (≠ L330) 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 (≠ I339) 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 (≠ T399) 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 (≠ A417) 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 (= C440) 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.
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.
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)
22% identity, 96% coverage: 8:467/480 of query aligns to 10:452/487 of P82251
- V40 (≠ I38) to M: in CSNU; uncertain significance
- IIGSG 43:47 (≠ VIGTG 41:45) binding
- I44 (= I42) to T: in CSNU; type I; dbSNP:rs121908485
- S51 (≠ V49) to F: in CSNU; uncertain significance
- P52 (≠ T50) to L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- A70 (≠ M67) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y96) to H: in CSNU; uncertain significance
- G105 (= G102) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W111) to R: in CSNU; uncertain significance
- I120 (≠ E116) to L: in CSNU; uncertain significance
- T123 (≠ I119) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (= V139) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ I141) modified: Interchain (with C-114 in SLC3A1)
- V170 (≠ I185) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (= A197) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (= G210) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (≠ R239) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (≠ G240) to V: in CSNU; non-classic type I; dbSNP:rs140873167
- N227 (≠ M243) to D: in CSNU; decreased amino acid transport activity
- W230 (≠ F246) to R: in CSNU; complete loss of amino acid transport activity; mutation to A: Abolishes amino acid transport activity.
- D233 (≠ I249) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ F251) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ A253) mutation to A: Reduces amino acid transport activity.
- G259 (≠ S275) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ V277) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (= S302) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ S331) mutation to S: Does not affect amino acid transport activity.
- A324 (≠ Q341) to E: in CSNU; uncertain significance
- V330 (≠ I347) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ M348) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (= R350) 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 (≠ N371) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (= S396) mutation to A: Markedly reduces amino acid transport activity.
- A382 (≠ T399) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (≠ L400) mutation to A: Complete loss of amino acid transport activity.
- Y386 (≠ F403) mutation to A: Loss of amino acid transport activity.
- K401 (≠ P418) to E: in CSNU; uncertain significance; dbSNP:rs760264924
- L426 (= L441) 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.
Query Sequence
>N515DRAFT_2925 FitnessBrowser__Dyella79:N515DRAFT_2925
MLKQLFARKTDFSDADDCHGGPSLRRTLGKWGITALGIGAVIGTGIFVVTGQAAAEHAGP
AVLISFMLAAICSGFTALCYAEFATLIPISGSSYSYAYATLGELVAWFIGWNMVLEYGIS
ASAVAASWTGYFTSLLDHVGIHLPVALTEAPLAFKDGHLVTTGHLLNLPAVAIVLALTWL
CYVGIRESSGLNVLMVALKVGLIIVVVVAGYRYVDPANWHPFIPAEQEPGKYGWSGIMRG
AAMVFFAYIGFEATSTAAQECKNPQKDLPFGTLVSLVICTVLYLAMAAVLTGLIPYTELG
TSEPVVTAIRNHPELGWLRLVVEIGAMIGLSSVILVMIIAQPRIFMIMSRDGLLPPVFNR
IHPKHRTPHLNTVITGIGIAILAAVFPLDLLADLTSMGTLIAFVAVCAGVLILRYTAPEL
PRLFRVPAAWFVCTAGVFSCLALLYFMAWFNWLLMIIWTAIGLAIYFGYGMRHSRLRRAS
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