SitesBLAST
Comparing 203165 FitnessBrowser__MR1:203165 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)
P76037 Putrescine importer PuuP from Escherichia coli (strain K12) (see paper)
64% identity, 98% coverage: 5:437/443 of query aligns to 15:447/461 of P76037
- Y110 (= Y100) mutation to X: The uptake activity is reduced to one-eighth of that of wild-type.
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
26% identity, 79% coverage: 48:396/443 of query aligns to 64:412/458 of 6f34A
- binding arginine: E115 (≠ D99), Y116 (= Y100), A119 (vs. gap), F228 (= F206), A229 (≠ S207), I231 (≠ L209), V314 (≠ S294)
- binding cholesterol: W201 (≠ G177), Y202 (≠ E178)
- binding : A178 (= A147), R179 (≠ N148), A186 (≠ F155), I187 (≠ A156), A190 (= A159), L194 (≠ V163), Q296 (≠ G276), V299 (≠ F279)
Sites not aligning to the query:
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
26% identity, 79% coverage: 48:396/443 of query aligns to 62:410/456 of 5oqtA
Sites not aligning to the query:
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)
24% identity, 86% coverage: 2:382/443 of query aligns to 22:438/629 of P30825
- N226 (vs. gap) modified: carbohydrate, N-linked (GlcNAc...) asparagine
P25737 Lysine-specific permease LysP; Lysine transporter LysP; Trigger transporter LysP from Escherichia coli (strain K12) (see 2 papers)
22% identity, 71% coverage: 2:317/443 of query aligns to 7:334/489 of P25737
- Y102 (≠ S96) mutation to L: Retains 4% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- W106 (≠ Y100) mutation to L: Retains 20% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- K163 (vs. gap) mutation to A: Retains 24% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- F216 (= F206) mutation to L: Retains 13% of wild-type lysine uptake activity. Increases the capacity to inhibit CadC in the presence of lysine.
- E222 (≠ D212) mutation to A: Abolishes lysine uptake. Strongly inhibits CadC.
- E230 (= E220) mutation to V: Abolishes lysine uptake. Shows significant less inhibition of CadC.
- D275 (≠ E261) 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 (= D264) 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.
P24207 Phenylalanine-specific permease; Phenylalanine:H(+) symporter PheP from Escherichia coli (strain K12) (see 3 papers)
25% identity, 52% coverage: 2:232/443 of query aligns to 13:246/458 of P24207
- R26 (≠ W15) mutation R->G,S,Q: Strong decrease in phenylalanine transport activity.
- P54 (≠ G43) mutation to A: 50% of wild-type phenylalanine transport activity.; mutation to G: No change in phenylalanine transport activity.; mutation to L: 26% of wild-type phenylalanine transport activity.
- F87 (≠ A76) mutation to L: No effect on phenylalanine transport activity.
- F90 (≠ Y79) mutation to L: 65% of wild-type phenylalanine transport activity.
- Y92 (≠ Q81) mutation to L: 41% of wild-type phenylalanine transport activity.
- Y94 (≠ N83) mutation to L: 69% of wild-type phenylalanine transport activity.
- W95 (≠ F84) mutation to L: 10% of wild-type phenylalanine transport activity.
- F98 (≠ N87) mutation to L: No effect on phenylalanine transport activity.
- F101 (= F90) mutation to L: 38% of wild-type phenylalanine transport activity.
- W105 (= W94) mutation to L: 39% of wild-type phenylalanine transport activity.
- Y107 (≠ S96) mutation to L: No effect on phenylalanine transport activity.
- W108 (≠ L97) mutation to L: 71% of wild-type phenylalanine transport activity.
- F111 (≠ Y100) mutation to L: 60% of wild-type phenylalanine transport activity.; mutation to Y: Enables the transport of tryptophan to almost the same steady-state level as that of phenylalanine.
- E118 (≠ N107) mutation E->G,L,V,N: Loss of activity.
- K168 (≠ Q157) mutation K->L,R: Strong decrease in phenylalanine transport activity.; mutation to N: Loss of activity.
- E226 (≠ D212) mutation E->A,Q,K,R,W: Loss of activity.
Sites not aligning to the query:
- 252 mutation R->D,E,F,W,P: Loss of activity.
- 341 P→A: 5% of wild-type phenylalanine transport activity.; mutation P->G,Q,K,R: Loss of activity.; P→S: 3% of wild-type phenylalanine transport activity.; P→T: 17% of wild-type phenylalanine transport activity.
- 442 P→A: 46% of wild-type phenylalanine transport activity.; P→G: 52% of wild-type phenylalanine transport activity.; P→L: 43% of wild-type phenylalanine transport activity.
8b70A Kima from b. Subtilis with nucleotide second-messenger c-di-amp bound (see paper)
24% identity, 58% coverage: 62:317/443 of query aligns to 59:303/572 of 8b70A
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 445, 446, 447, 472, 545, 546, 548
- binding potassium ion: 15, 19, 22, 343
P96589 Potassium transporter KimA; K(+) importer A; Potassium-proton symporter KimA from Bacillus subtilis (strain 168) (see paper)
23% identity, 58% coverage: 62:317/443 of query aligns to 80:337/607 of P96589
- D117 (= D99) binding ; mutation D->A,N,E: No effect on growth.
- T121 (≠ M103) mutation to A: Decreases potassium uptake.
- S125 (≠ N107) binding ; mutation to A: Decreases potassium uptake.
- E233 (≠ D212) mutation E->A,Q: Abolishes potassium uptake.
Sites not aligning to the query:
- 36 binding ; binding ; mutation D->A,N: Abolishes potassium uptake.
- 43 binding ; Y→N: Abolishes potassium uptake.
- 377 Y→A: Decreases potassium uptake.
6s3kB Kima from bacillus subtilis in inward-facing, occluded state (see paper)
23% identity, 58% coverage: 62:317/443 of query aligns to 54:311/573 of 6s3kB
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)
25% identity, 73% coverage: 57:380/443 of query aligns to 91:413/501 of Q9UPY5
- R135 (≠ M103) binding ; mutation to A: Loss of L-cystine transport activity.; mutation to K: Loss of L-cystine transport activity.
- C158 (≠ V122) 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 (≠ N150) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ A156) 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 (≠ Q157) 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 (≠ S216) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ L233) 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 (≠ V291) 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 (≠ A300) 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 (≠ A363) 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.
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.
- 414 C→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.
- 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.
7epzB Overall structure of erastin-bound xct-4f2hc complex (see paper)
25% identity, 73% coverage: 57:380/443 of query aligns to 47:369/453 of 7epzB
Sites not aligning to the query:
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
25% identity, 73% coverage: 57:380/443 of query aligns to 47:369/455 of 7p9uB
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
22% identity, 85% coverage: 1:377/443 of query aligns to 1:364/438 of O34739
- C94 (≠ V92) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (≠ T136) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ I160) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ A298) 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.
3l1lA Structure of arg-bound escherichia coli adic (see paper)
24% identity, 48% coverage: 41:251/443 of query aligns to 32:225/423 of 3l1lA
Sites not aligning to the query:
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
26% identity, 80% coverage: 70:425/443 of query aligns to 64:421/433 of 6f2wA
Sites not aligning to the query:
P15993 Aromatic amino acid transport protein AroP; Aromatic amino acid:H(+) symporter AroP; General aromatic amino acid permease; General aromatic transport system from Escherichia coli (strain K12) (see paper)
26% identity, 38% coverage: 64:231/443 of query aligns to 67:237/457 of P15993
- Y103 (= Y100) Key residue for tryptophan transport; mutation to F: Decreases tryptophan transport to less than 50% of wild-type levels and reduces the ability of tryptophan to inhibit phenylalanine transport from 95 to 62%.
P46349 Gamma-aminobutyric acid permease; GABA permease; 4-aminobutyrate permease; Gamma-aminobutyrate permease; Proline transporter GabP from Bacillus subtilis (strain 168) (see paper)
22% identity, 72% coverage: 1:318/443 of query aligns to 1:321/469 of P46349
- G33 (≠ T33) mutation to D: Lack of activity.
- G42 (≠ S42) mutation to S: Lack of activity.
- G301 (= G295) mutation to V: Lack of activity.
Sites not aligning to the query:
- 338 G→E: Lack of activity.
- 341 F→S: Lack of activity.
- 414 G→R: Lack of activity.
8b71A Upright kima dimer with bound c-di-amp from b. Subtilis (see paper)
33% identity, 19% coverage: 62:147/443 of query aligns to 51:138/552 of 8b71A
Sites not aligning to the query:
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: 283, 403, 408, 425, 426, 427, 432, 452, 454, 514, 525, 526, 528
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)
21% identity, 76% coverage: 52:386/443 of query aligns to 70:408/487 of P82251
- A70 (= A52) to V: in CSNU; partial loss of amino acid transport activity; dbSNP:rs769448665
- Y99 (= Y79) to H: in CSNU; uncertain significance
- G105 (≠ S85) to R: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908480
- W114 (= W94) to R: in CSNU; uncertain significance
- I120 (vs. gap) to L: in CSNU; uncertain significance
- T123 (vs. gap) to M: in CSNU; partial loss of amino acid transport activity; dbSNP:rs79987078
- V142 (≠ L115) to A: no effect on amino acid transport activity; dbSNP:rs12150889
- C144 (≠ A117) modified: Interchain (with C-114 in SLC3A1)
- V170 (≠ I143) to M: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs121908479
- A182 (≠ F155) to T: in CSNU; type III; partial loss of amino acid transport activity; dbSNP:rs79389353
- G195 (≠ H170) to R: in CSNU; type III; decreased amino acid transport activity; dbSNP:rs121908482
- L223 (= L204) to M: slightly decreased amino acid transport activity; dbSNP:rs1007160
- A224 (≠ C205) 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 (≠ L209) binding ; mutation to A: Complete loss of amino acid transport activity.
- W235 (≠ F211) mutation to A: Complete loss of amino acid transport activity.
- Q237 (≠ G213) mutation to A: Reduces amino acid transport activity.
- G259 (vs. gap) to R: in CSNU; type III; impairs protein stability and dimer formation; dbSNP:rs121908483
- P261 (≠ T235) to L: in CSNU; types I and III; dbSNP:rs121908486
- S286 (≠ F260) to F: in CSNU; uncertain significance; dbSNP:rs755135545
- C321 (≠ A297) mutation to S: Does not affect amino acid transport activity.
- A324 (= A300) to E: in CSNU; uncertain significance
- V330 (= V308) to M: in CSNU; type III; dbSNP:rs201618022
- A331 (≠ M309) to V: in CSNU; non-classic type I; dbSNP:rs768466784
- R333 (= R311) 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 (≠ N333) to T: in CSNU; type III; severe loss of amino acid transport activity; dbSNP:rs939028046
- S379 (≠ A360) mutation to A: Markedly reduces amino acid transport activity.
- A382 (= A363) to T: in CSNU; severe loss of amino acid transport activity; dbSNP:rs774878350
- W383 (≠ F364) mutation to A: Complete loss of amino acid transport activity.
- Y386 (≠ V367) mutation to A: Loss of amino acid transport activity.
- K401 (≠ E379) to E: in CSNU; uncertain significance; dbSNP:rs760264924
Sites not aligning to the query:
- 40 V → M: in CSNU; uncertain significance
- 43:47 binding
- 44 I → T: in CSNU; type I; dbSNP:rs121908485
- 51 S → F: in CSNU; uncertain significance
- 52 P → L: in CSNU; impairs protein stability and dimer formation; dbSNP:rs1198613438
- 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.
6li9B Heteromeric amino acid transporter b0,+at-rbat complex bound with arginine (see paper)
21% identity, 76% coverage: 52:386/443 of query aligns to 41:379/458 of 6li9B
Sites not aligning to the query:
Query Sequence
>203165 FitnessBrowser__MR1:203165
MSQQKPGLKQSLNLWQVVVMGLAYLTPMAVFDTFGIVSEITSGHVATSYLLALAGILFTA
FSYGHLVRKYPYAGSAYTYAQKNFSPNVGFMVGWSSLLDYMFMPMINMLLAKIYLTAMFP
NVEPWIFIFGLVTVMTVLNLRGIDLVANFNGVIVFAQIAIILVFIGLMAHSLSLGEGEGV
IASVRPFYSEQVTLAPLFTGATILCFSFLGFDGLSSLSEETKDAKRVIPRAILLTALIGG
VIFVSVSYFLQLYFPDISRFEQLDAVLPEIALYVGGNLFQSIVLVATTIAVLASGMAAHA
GVARILYVMGRDNMLPNKGFGYVHPKWRTPAFNVVLVGLLALSAVSFDLEMALALVNFGA
LVAFTFVNLSVIVQFYIKEKRNQSLKEHLQYFVLPLCGAATIGVLWINLEPQSLELGLIW
GAVGMLYLALRSLRLRKAVELQS
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