SitesBLAST
Comparing 14823 FitnessBrowser__Keio:14823 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)
P0AAF1 Putrescine transporter PotE; Putrescine-proton symporter / putrescine-ornithine antiporter from Escherichia coli (strain K12) (see 2 papers)
100% identity, 100% coverage: 1:439/439 of query aligns to 1:439/439 of P0AAF1
- C62 (= C62) mutation C->A,T: Strong decrease in both uptake and excretion activities.; mutation to S: Moderate decrease in both uptake and excretion activities.
- K68 (= K68) mutation to A: Slight decrease in both uptake and excretion activities.
- E77 (= E77) mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
- Y78 (= Y78) mutation to L: Uptake activity decreases more than excretion activity.
- K82 (= K82) mutation to A: Slight decrease in both uptake and excretion activities.
- Y90 (= Y90) mutation to L: Uptake activity decreases more than excretion activity.
- Y92 (= Y92) mutation to L: Moderate decrease in both uptake and excretion activities.
- W201 (= W201) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- E207 (= E207) mutation E->A,D,N,Q: Lack of both uptake and excretion activities.
- C210 (= C210) mutation to A: Moderate decrease in both uptake and excretion activities.
- C285 (= C285) mutation to A: Moderate decrease in both uptake and excretion activities.
- C286 (= C286) mutation to A: Moderate decrease in both uptake and excretion activities.
- W292 (= W292) mutation W->F,L,Y: Strong decrease in both uptake and excretion activities.
- K301 (= K301) mutation to A: Excretion activity decreases more than uptake activity.
- Y308 (= Y308) mutation to L: Excretion activity decreases more than uptake activity.
- W422 (= W422) mutation to L: Uptake activity decreases more than excretion activity.
- Y425 (= Y425) mutation to F: Moderate decrease in both uptake and excretion activities.; mutation to L: Strong decrease in both uptake and excretion activities.
- E433 (= E433) mutation E->A,D,N,Q: Strong decrease in both uptake and excretion activities.
P60061 Arginine/agmatine antiporter from Escherichia coli (strain K12) (see 3 papers)
33% identity, 100% coverage: 2:438/439 of query aligns to 3:436/445 of P60061
- I23 (≠ M22) binding ; binding
- S26 (= S25) binding
- Y93 (= Y92) mutation to L: Greatly decreased Arg uptake into liposomes.
- A96 (≠ S95) binding ; binding
- C97 (≠ L96) binding
- N101 (= N100) binding ; mutation to A: Vmax for Arg-Agm exchange 1% of wild-type, KM increases 3-fold.; mutation to D: Nearly wild-type Arg-Agm exchange.
- M104 (≠ I103) binding ; mutation to A: 30% decreased affinity for Arg, 50% decreased affinity for Agm.
- W202 (= W201) binding ; mutation to L: Halves Arg uptake into liposomes.
- S203 (≠ A202) binding
- I205 (≠ L204) binding ; binding ; mutation to A: About wild-type affinity for Arg and Agm.
- W293 (= W292) binding ; mutation W->C,H,L: Loss of Arg-Agm exchange.; mutation W->F,Y: Less than 20% Arg-Agm exchange activity. Vmax 15% of wild-type rate.
- S357 (≠ A356) binding ; mutation to A: 20% decreased affinity for Arg, 40% decrease affinity for Agm.
P60063 Arginine/agmatine antiporter from Escherichia coli O157:H7 (see 3 papers)
33% identity, 100% coverage: 2:438/439 of query aligns to 3:436/445 of P60063
- N22 (= N21) mutation to A: No change in antiport activity, 6-fold higher affinity for Arg.
- I23 (≠ M22) binding
- GSG 25:27 (= GSG 24:26) Helix-breaking GSG motif TM1
- S26 (= S25) binding ; mutation to K: 5% Agm antiport.
- G27 (= G26) binding
- Y74 (≠ G73) mutation to A: 50% antiport activity at pH 6.0, 10-fold higher than wild-type antiport activity at pH 7.5, i.e. loss of pH-dependence of substrate transport. No change in binding of Arg or Agm.; mutation Y->C,H,L,M,Q,S: Loss of pH-dependence of substrate transport.; mutation to F: Approximately wild-type antiport.
- Y87 (≠ F86) mutation to A: Markedly reduced binding affinity for Agm but not for Arg. 50% Agm antiport.
- Y93 (= Y92) mutation to A: Reduced binding affinity for Arg, no binding to Agm. 25% Agm antiport.; mutation to K: Almost no binding to both Arg and Agm. 5% Agm antiport.
- A96 (≠ S95) binding
- C97 (≠ L96) binding
- N101 (= N100) binding
- W202 (= W201) Periplasmic (proximal) gate; binding
- I205 (≠ L204) binding
- GVESA 206:210 (≠ GLESA 205:209) Helix-breaking GVESA motif TM6
- E208 (= E207) mutation E->A,D: 5-10% Agm antiport.
- W293 (= W292) binding
- F337 (≠ L336) mutation to A: Severely decreased antiport.
- S357 (≠ A356) binding
- Y365 (= Y364) mutation to A: Markedly weakened binding to Arg but not to Agm. 5% Agm antiport.
5j4nA Crystal structure of the l-arginine/agmatine antiporter adic in complex with agmatine at 2.6 angstroem resolution (see paper)
33% identity, 99% coverage: 4:438/439 of query aligns to 1:432/437 of 5j4nA
3l1lA Structure of arg-bound escherichia coli adic (see paper)
32% identity, 99% coverage: 6:438/439 of query aligns to 1:419/423 of 3l1lA
P0AAE8 Cadaverine/lysine antiporter from Escherichia coli (strain K12) (see paper)
32% identity, 92% coverage: 1:403/439 of query aligns to 1:401/444 of P0AAE8
- C12 (≠ L14) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- W41 (≠ I43) mutation to L: Moderate decrease in cadaverine uptake.
- W43 (= W45) mutation to L: Strong decrease in cadaverine uptake.
- Y55 (≠ W57) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y57 (≠ F59) mutation to L: Strong decrease in cadaverine uptake.
- Y73 (= Y75) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake. 9-fold increase in Km for cadaverine for cadaverine uptake and 10-fold increase in Km for cadaverine for cadaverine excretion.
- E76 (vs. gap) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y89 (= Y92) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake. 10-fold increase in Km for cadaverine for cadaverine uptake and 5-fold increase in Km for cadaverine for cadaverine excretion.
- Y90 (≠ G93) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake.
- Y107 (= Y110) mutation to L: Strong decrease in cadaverine uptake.
- C125 (≠ T128) mutation to S: Does not affect cadaverine excretion and cadaverine uptake.
- Y174 (= Y177) mutation to L: Moderate decrease in cadaverine uptake.
- D185 (≠ F188) mutation to N: Moderate decrease in cadaverine uptake.
- C196 (≠ T199) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- E204 (= E207) mutation to Q: Strong decrease in both cadaverine excretion and cadaverine uptake. 22-fold increase in Km for cadaverine for cadaverine uptake and 6-fold increase in Km for cadaverine for cadaverine excretion.
- Y235 (= Y238) mutation to L: Strong decrease in both cadaverine excretion and cadaverine uptake. 23-fold increase in Km for cadaverine for cadaverine uptake and 7-fold increase in Km for cadaverine for cadaverine excretion.
- Y246 (≠ V249) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C282 (= C285) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- R299 (≠ S302) mutation to A: Strong decrease in cadaverine excretion but not in cadaverine uptake.
- D303 (≠ E306) mutation to N: Strong decrease in both cadaverine excretion and cadaverine uptake. 24-fold increase in Km for cadaverine for cadaverine uptake and 9-fold increase in Km for cadaverine for cadaverine excretion.
- Y310 (≠ F313) mutation to L: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- Y366 (= Y364) mutation to L: Strong decrease in cadaverine uptake. 15-fold increase in Km for cadaverine for cadaverine uptake.
- Y368 (≠ L366) mutation to L: Strong decrease in cadaverine uptake.
- C370 (≠ M368) mutation to S: Strong decrease in both cadaverine excretion and cadaverine uptake.
- E377 (≠ Q375) mutation to Q: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C389 (vs. gap) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C394 (≠ A396) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
- C397 (≠ S399) mutation to S: Moderate decrease in both cadaverine excretion and cadaverine uptake.
Sites not aligning to the query:
- 408 E→Q: Moderate decrease in cadaverine uptake.
- 423 Y→L: Strong decrease in both cadaverine excretion and cadaverine uptake.
6f2wA Bacterial asc transporter crystal structure in open to in conformation (see paper)
22% identity, 97% coverage: 14:439/439 of query aligns to 7:432/433 of 6f2wA
5oqtA Crystal structure of a bacterial cationic amino acid transporter (cat) homologue (see paper)
23% identity, 64% coverage: 36:317/439 of query aligns to 54:341/456 of 5oqtA
Sites not aligning to the query:
6f34A Crystal structure of a bacterial cationic amino acid transporter (cat) homologue bound to arginine. (see paper)
24% identity, 71% coverage: 6:317/439 of query aligns to 24:343/458 of 6f34A
- binding arginine: I40 (≠ M22), G42 (= G24), T43 (≠ S25), G44 (= G26), E115 (≠ S95), Y116 (≠ L96), A119 (= A99), F228 (≠ W201), A229 (= A202), I231 (≠ L204), V314 (≠ S288)
- binding cholesterol: W201 (≠ F170), Y202 (≠ W171)
- binding : G28 (= G10), F30 (≠ V12), D31 (≠ Q13), M34 (≠ I16), A178 (≠ G147), R179 (≠ Q148), A186 (≠ W155), I187 (≠ G156), A190 (≠ I159), L194 (≠ G163), Q296 (≠ T270), V299 (= V273)
O34739 Serine/threonine exchanger SteT from Bacillus subtilis (strain 168) (see paper)
25% identity, 85% coverage: 6:379/439 of query aligns to 9:378/438 of O34739
- C94 (≠ A88) mutation to S: Retains 25% of the transport activity; when associated with S-141; S-168; S-291 and S-415.
- C141 (= C135) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-168; S-291 and S-415.
- C168 (≠ G163) mutation to S: Retains 25% of the transport activity; when associated with S-94; S-141; S-291 and S-415.
- C291 (≠ S288) 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.
P63235 Glutamate/gamma-aminobutyrate antiporter; Glu/GABA antiporter; Extreme acid sensitivity protein from Escherichia coli (strain K12) (see 2 papers)
22% identity, 65% coverage: 120:406/439 of query aligns to 126:430/511 of P63235
- L212 (≠ W201) mutation to A: 70% decrease in substrate transport.
- E218 (= E207) mutation to A: At least 90% decrease in substrate transport.
- E304 (≠ S288) mutation to A: At least 90% decrease in substrate transport.
- W308 (= W292) mutation to A: At least 90% decrease in substrate transport.
- Y378 (≠ N360) mutation to A: At least 90% decrease in substrate transport.
- Y382 (= Y364) mutation to A: At least 90% decrease in substrate transport.
Sites not aligning to the query:
- 25 M→A: 25% decrease in substrate transport.
- 30 Y→A: At least 90% decrease in substrate transport.
- 471:511 mutation Missing: Shifts the pH-dependent substrate transport towards higher pH values. Transports Gln, but not Glu, at pH 7.0 or higher.
- 491 H→A: Allows substrate transport at pH 6.5.
- 497 R→A: Allows substrate transport at pH 6.5.
- 499 R→A: Allows substrate transport at pH 6.5.
- 502 H→A: Allows substrate transport at pH 6.5.
- 503 Y→A: Allows substrate transport at pH 6.5.
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)
22% identity, 86% coverage: 4:381/439 of query aligns to 35:417/535 of Q9UHI5
- I53 (≠ M22) binding
- Y93 (≠ F59) 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 (= N100) 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 (≠ L119) modified: Interchain (with C-210 in SLC3A2)
- W174 (≠ V137) mutation to A: Does not affect protein expression, plasma membrane localization, or L-alanine uptake.
- F243 (≠ W201) mutation to A: Abolishes leucine and tryptophan transport activities.
- G246 (≠ L204) 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 (≠ F261) to I: found in a patient with age-related hearing loss; does not affect L-alanine transport activity. Decreases L-tyrosine transport activity
- N395 (= N360) binding ; mutation to Q: Strongly reduces L-leucine uptake activity. Strongly reduces L-tryptophan uptake activity.
- Y396 (≠ I361) mutation to A: Strongly reduces L-leucine uptake activity.
- T402 (≠ S367) to M: found in a patient with age-related hearing loss; strongly decreased L-alanine transport activity. Decreases L-tyrosine transport activity
Sites not aligning to the query:
- 418 R → C: found in a patient with age-related hearing loss; decreases L-alanine transport activity. Decreases L-tyrosine transport activity
- 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
7epzB Overall structure of erastin-bound xct-4f2hc complex (see paper)
25% identity, 71% coverage: 40:352/439 of query aligns to 34:348/453 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)
26% identity, 71% coverage: 40:352/439 of query aligns to 78:392/501 of Q9UPY5
- C86 (≠ T48) 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 (≠ N100) 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 (≠ R144) mutation to A: Increases sensitivity to erastin-induced ferroptosis.
- C197 (≠ S150) 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 (≠ S151) mutation to A: Loss of L-cystine transport activity. Does not affect location at the celle membrane. Does not affect expression level.
- Y244 (≠ S208) binding
- F254 (vs. gap) mutation to A: Increases resistance to erastin-induced ferroptosis. Decreases sensitivity to erastin-induced inhibition of L-cystine transport activity.
- C271 (≠ T231) 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 (= C285) 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 (= F294) 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.
Sites not aligning to the query:
- 396 R→A: Loss of L-cystine transport activity.; R→K: Loss of L-cystine transport activity.; R→N: Loss of L-cystine transport activity.
- 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.
7p9uB Cryo em structure of system xc- in complex with glutamate (see paper)
25% identity, 71% coverage: 40:352/439 of query aligns to 34:348/455 of 7p9uB
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)
22% identity, 95% coverage: 4:421/439 of query aligns to 34:465/531 of Q9QXW9
- Y130 (≠ L97) mutation to A: Increases T2 import. Increases T3 and enables T4 import. Does not affect L-leucine and L-phenylalanine uptake.
- N133 (= N100) 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 (≠ W201) mutation to W: Increases T2 import. Does not affect T3 import. Does not affect L-leucine and L-phenylalanine uptake.
7cmiB The lat2-4f2hc complex in complex with leucine (see paper)
22% identity, 82% coverage: 21:381/439 of query aligns to 12:377/458 of 7cmiB
7cmhB The lat2-4f2hc complex in complex with tryptophan (see paper)
22% identity, 82% coverage: 21:381/439 of query aligns to 12:377/458 of 7cmhB
7b00A Human lat2-4f2hc complex in the apo-state (see paper)
22% identity, 82% coverage: 21:381/439 of query aligns to 12:377/457 of 7b00A
Sites not aligning to the query:
Q22397 Amino acid transporter protein 6 from Caenorhabditis elegans (see paper)
24% identity, 75% coverage: 2:332/439 of query aligns to 13:355/523 of Q22397
Sites not aligning to the query:
- 521:523 PDZ-binding motif; mutation Missing: Abolishes the interaction with nrfl-1.
Query Sequence
>14823 FitnessBrowser__Keio:14823
MSQAKSNKMGVVQLTILTMVNMMGSGIIMLPTKLAEVGTISIISWLVTAVGSMALAWAFA
KCGMFSRKSGGMGGYAEYAFGKSGNFMANYTYGVSLLIANVAIAISAVGYGTELLGASLS
PVQIGLATIGVLWICTVANFGGARITGQISSITVWGVIIPVVGLCIIGWFWFSPTLYVDS
WNPHHAPFFSAVGSSIAMTLWAFLGLESACANTDVVENPERNVPIAVLGGTLGAAVIYIV
STNVIAGIVPNMELANSTAPFGLAFAQMFTPEVGKVIMALMVMSCCGSLLGWQFTIAQVF
KSSSDEGYFPKIFSRVTKVDAPVQGMLTIVIIQSGLALMTISPSLNSQFNVLVNLAVVTN
IIPYILSMAALVIIQKVANVPPSKAKVANFVAFVGAMYSFYALYSSGEEAMLYGSIVTFL
GWTLYGLVSPRFELKNKHG
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